| Bomi1
| Inter-alpha-trypsin inhibitor heavy chain H1
| Bos taurus
| Q0VCM5
| https://www.uniprot.org/uniprot/Q0VCM5
| Whey
| NP_001068821.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068821.1
| 906
| 101237
| https://www.uniprot.org/uniprot/Q0VCM5.fasta
| ITIH1
| 508356
| https://www.ncbi.nlm.nih.gov/gene/508356
| Reviewed: Experimental evidence at protein level
| IαI family proteins are mainly secreted by the liver and
present in the blood;
| plasma serine-proteinase
inhibitor; ITIH4 is a liver-derived member of the ITI family
with diverse functions as an anti-apoptotic and matrix-
stabilizing molecule that is important throughout
development; ITIH4 is a significant biomarker to assess
particulate matter in patients with chronic
obstructive pulmonary disease
| plasma serine-proteinase
inhibitor; ITIH4 is a liver-derived member of the ITI family
with diverse functions as an anti-apoptotic and matrix-
stabilizing molecule that is important throughout
development; ITIH4 is a significant biomarker to assess
particulate matter in patients with chronic
obstructive pulmonary disease
| acute phase protein in cattle- was isolated from heifers with experimentally induced 'summer mastitis'
| Glycosylated: two potential N-glycosylation sites of H1 are effectively
fully occupied by complex-type N-glycans- predominantly
of biantennary type; H2 heavy chain
carries only one complex-type N-glycan attached to Asn64; O-glycan carried by Thr637, two or three additional O-linked
carbohydrate chains are present on H2-consist of a type-1 core structure with one or two NeuAc
moieties;
| O glycans influences the metabolism of IaI- preferentially cleaves the H2 heavy chain in its Cterminal
part which is enhanced by charge-mediated
interactions between the glycosaminoglycan chain of IaI and
elastase- mediated byO-glycan chains located in the C-terminal part of H2
|
|
| F1MNW4,Q3T052
| 1. Flahaut, C., Capon, C., Balduyck, M., Ricart, G., Sautiere, P., & Mizon, J. (1998). Glycosylation pattern of human inter-alpha-inhibitor heavy chains. The Biochemical Journal, 333 ( Pt 3), 749–756. https://doi.org/10.1042/bj3330749.
2. Soler, L., Dąbrowski, R., García, N., Alava, M. A., Lampreave, F., Piñeiro, M., … Bochniarz, M. (2019). Acute-phase inter-alpha-trypsin inhibitor heavy chain 4 (ITIH4) levels in serum and milk of cows with subclinical mastitis caused by Streptococcus species and coagulase-negative Staphylococcus species. Journal of Dairy Science, 102(1), 539–546. https://doi.org/10.3168/jds.2018-14953.
3. Zhuo, L., Hascall, V. C., & Kimata, K. (2004). Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan-protein complex. The Journal of Biological Chemistry, 279(37), 38079–38082. https://doi.org/10.1074/jbc.R300039200.
4. Hutadilok, N., Ghosh, P., & Brooks, P. M. (1988). Binding of haptoglobin, inter-alpha-trypsin inhibitor, and alpha 1 proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals. Annals of the Rheumatic Diseases, 47(5), 377–385. https://doi.org/10.1136/ard.47.5.377.
5. Zhuo, L., Kanamori, A., Kannagi, R., Itano, N., Wu, J., Hamaguchi, M., … Kimata, K. (2006). SHAP potentiates the CD44-mediated leukocyte adhesion to the hyaluronan substratum. The Journal of Biological Chemistry, 281(29), 20303–20314. https://doi.org/10.1074/jbc.M506703200.
6. Castillo, G. M., & Templeton, D. M. (1993). Subunit structure of bovine ESF (extracellular-matrix stabilizing factor(s)). A chondroitin sulfate proteoglycan with homology to human I alpha i (inter-alpha-trypsin inhibitors). FEBS Letters, 318(3), 292–296. https://doi.org/10.1016/0014-5793(93)80531-x.
7. Blom, A. M., Mörgelin, M., Oyen, M., Jarvet, J., & Fries, E. (1999). Structural characterization of inter-alpha-inhibitor. Evidence for an extended shape. The Journal of Biological Chemistry, 274(1), 298–304. https://doi.org/10.1074/jbc.274.1.298.
8. Yoneda, M., Suzuki, S., & Kimata, K. (1990). Hyaluronic acid associated with the surfaces of cultured fibroblasts is linked to a serum-derived 85-kDa protein. The Journal of Biological Chemistry, 265(9), 5247–5257. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1690737
|
| Bomi10
| Clusterin
| Bos taurus
| P17697
| https://www.uniprot.org/uniprot/P17697
| Whey
| NP_776327.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776327.1
| 439
| 51114
| https://www.uniprot.org/uniprot/P17697.fasta
| CLU
| 280750
| https://www.ncbi.nlm.nih.gov/gene/280750
| Reviewed: Experimental evidence at protein level
| normal human spermatozoa ; In normal human lung,fibroblast-like cells and sporadic areas of bronchial epithelial cells
| Important roles in immune regulation, ageing, tissue remodeling, lipid transport, membrane recycling, complements cascade, DNA repair, cell adhesion, and cell-cell interactions, cancer progression, vascular damage, diabetes, kidney and neuron degeneration; protects cells against cytotoxic agents that induce apoptosis, and acts as a pro-death signal, inhibiting cell growth and survival
| Important roles in immune regulation, ageing, tissue remodeling, lipid transport, membrane recycling, complements cascade, DNA repair, cell adhesion, and cell-cell interactions, cancer progression, vascular damage, diabetes, kidney and neuron degeneration; protects cells against cytotoxic agents that induce apoptosis, and acts as a pro-death signal, inhibiting cell growth and survival
| more abundant in human
milk than in bovine milk; most abundant
proteins in the human MFGM fraction; linked to cell
damage and apoptosis and has been shown to be overexpressed at
damaged or stressed tissues and to provide a chaperone-like
activity to protect other proteins against damage
| heavy
glycosylation; carbohydrate comprises approximately
20-25% of the total mass of the mature molecule; six N-linked glycosylation
sites have been identified, three in the alpha chain (α64N,
α81N, and α123N) and three in the beta chain (ß64N, ß127N,
and ß147N); types of oligosaccharides attached to the
clusterin peptide are diverse;
| hydrophilic carbohydrate moieties might enhance the chaperone action of clusterin by
helping it keep such complexes in solution
|
| mutations in the protein
might lead to its altered localization and functions in the cell
|
| 1. Yang, Y., Bu, D., Zhao, X., Sun, P., Wang, J., & Zhou, L. (2013). Proteomic analysis of cow, yak, buffalo, goat and camel milk whey proteins: quantitative differential expression patterns. Journal of Proteome Research, 12(4), 1660–1667. https://doi.org/10.1021/pr301001m.
2. Xiu, P., Dong, X., Dong, X., Xu, Z., Zhu, H., Liu, F., … Sun, X. (2013). Secretory clusterin contributes to oxaliplatin resistance by activating Akt pathway in hepatocellular carcinoma. Cancer Science, 104(3), 375–382. https://doi.org/10.1111/cas.12088.
3. Hettinga, K., van Valenberg, H., de Vries, S., Boeren, S., van Hooijdonk, T., van Arendonk, J., & Vervoort, J. (2011). The host defense proteome of human and bovine milk. PloS One, 6(4), e19433. https://doi.org/10.1371/journal.pone.0019433.
4. Lambert, J.-C., Heath, S., Even, G., Campion, D., Sleegers, K., Hiltunen, M., … Amouyel, P. (2009). Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer’s disease. Nature Genetics, 41(10), 1094–1099. https://doi.org/10.1038/ng.439.
5. Stewart, E. M., Aquilina, J. A., Easterbrook-Smith, S. B., Murphy-Durland, D., Jacobsen, C., Moestrup, S., & Wilson, M. R. (2007). Effects of glycosylation on the structure and function of the extracellular chaperone clusterin. Biochemistry, 46(5), 1412–1422. https://doi.org/10.1021/bi062082v.
6. Wang, X., Zou, F., Zhong, J., Yue, L., Wang, F., Wei, H., … Xiu, P. (2018). Secretory Clusterin Mediates Oxaliplatin Resistance via the Gadd45a/PI3K/Akt Signaling Pathway in Hepatocellular Carcinoma. Journal of Cancer, 9(8), 1403–1413. https://doi.org/10.7150/jca.23849.
7. Zhong, J., Yu, X., Dong, X., Lu, H., Zhou, W., Li, L., … Shi, X. (2018). Downregulation of secreted clusterin potentiates the lethality of sorafenib in hepatocellular carcinoma in association with the inhibition of ERK1/2 signals. International Journal of Molecular Medicine, 41(5), 2893–2900. https://doi.org/10.3892/ijmm.2018.3463.
8. Wang, C., Jiang, K., Kang, X., Gao, D., Sun, C., Li, Y., … Liu, Y. (2012). Tumor-derived secretory clusterin induces epithelial-mesenchymal transition and facilitates hepatocellular carcinoma metastasis. The International Journal of Biochemistry & Cell Biology, 44(12), 2308–2320. https://doi.org/10.1016/j.biocel.2012.09.012.
9. Trougakos, I. P., & Gonos, E. S. (2006). Regulation of clusterin/apolipoprotein J, a functional homologue to the small heat shock proteins, by oxidative stress in ageing and age-related diseases. Free Radical Research, 40(12), 1324–1334. https://doi.org/10.1080/10715760600902310.
10. Lourda, M., Trougakos, I. P., & Gonos, E. S. (2007). Development of resistance to chemotherapeutic drugs in human osteosarcoma cell lines largely depends on up-regulation of Clusterin/Apolipoprotein J. International Journal of Cancer, 120(3), 611–622. https://doi.org/10.1002/ijc.22327.
11. Han, Z., Wang, Z., Cheng, G., Liu, B., Li, P., Li, J., … Zhang, W. (2012). Presence, localization, and origin of clusterin in normal human spermatozoa. Journal of Assisted Reproduction and Genetics, 29(8), 751–757. https://doi.org/10.1007/s10815-012-9779-x.
|
| Bomi100
| Cystatin-C
| Bos taurus
| P01035
| https://www.uniprot.org/uniprot/P01035
| Whey
| NP_776454.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776454.1
| 148
| 16265
| https://www.uniprot.org/uniprot/P01035.fasta
| CST3
| 281102
| https://www.ncbi.nlm.nih.gov/gene/281102
| Reviewed: Experimental evidence at protein level
| Parotid glands, osteoblast,
| Inhibits bone resorption; inhibits such proteases as papain
and cathepsin B, L and K;
| Inhibits bone resorption; inhibits such proteases as papain
and cathepsin B, L and K;
| role in the protection from bacterial infection
| 2 intracellular disulfide bonds; no glycosylation; chicken cystatin is phosphorylated;
|
|
|
|
| 1. Matsuoka, Y., Serizawa, A., Yoshioka, T., Yamamura, J., Morita, Y., Kawakami, H., … Kumegawa, M. (2002). Cystatin C in milk basic protein (MBP) and its inhibitory effect on bone resorption in vitro. Bioscience, Biotechnology, and Biochemistry, 66(12), 2531–2536. https://doi.org/10.1271/bbb.66.2531.
2. Mudaliar, M., Tassi, R., Thomas, F. C., McNeilly, T. N., Weidt, S. K., McLaughlin, M., … Zadoks, R. N. (2016). Mastitomics, the integrated omics of bovine milk in an experimental model of Streptococcus uberis mastitis: 2. Label-free relative quantitative proteomics. Molecular BioSystems, 12(9), 2748–2761. https://doi.org/10.1039/c6mb00290k.
|
| Bomi1000
| SIN3 transcription regulator family member B
| Bos taurus
| E1BGW5
| https://www.uniprot.org/uniprot/E1BGW5
| Whey, Exosome
|
|
| 1122
| 128262
| https://www.uniprot.org/uniprot/E1BGW5.fasta
| SIN3B
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1006
| Autophagy related 2B
| Bos taurus
| E1BH30
| https://www.uniprot.org/uniprot/E1BH30
| Whey, MFGM
| NP_001193682.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193682.1
| 2078
| 232113
| https://www.uniprot.org/uniprot/E1BH30.fasta
| ATG2B
| 519961
| https://www.ncbi.nlm.nih.gov/gene/519961
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1007
| MYC binding protein 2, E3 ubiquitin protein ligase
| Bos taurus
| E1BH40
| https://www.uniprot.org/uniprot/E1BH40
| Whey
|
|
| 4553
| 501014
| https://www.uniprot.org/uniprot/E1BH40.fasta
| MYCBP2
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi101
| Kininogen-1
| Bos taurus
| P01044
| https://www.uniprot.org/uniprot/P01044
| Whey
| NP_786968.2
| https://www.ncbi.nlm.nih.gov/protein/NP_786968.2
| 436
| 48428
| https://www.uniprot.org/uniprot/P01044-2.fasta
| KNG1
| 280833
| https://www.ncbi.nlm.nih.gov/gene/280833
| Reviewed: Experimental evidence at protein level
| tears, CSF, saliva
| accelerate the activation of
factor XII, prekallikrein, and factor XI as cofactor; Fragment 1.2 has also been shown to be
a potent inhibitor of the contact activation of factor XII;
| accelerate the activation of
factor XII, prekallikrein, and factor XI as cofactor; Fragment 1.2 has also been shown to be
a potent inhibitor of the contact activation of factor XII;
| maintaining the bone
strength and content of hydroxyproline
| Bovine fragment 1.2 of HMW kininogen has four
oligosaccharide chains that attached to serine and
threonine residues. The residues with oligosaccharide
chains are S10, T10, T12, S18 from the amino-terminal of
the fragment 1.2;
|
|
|
|
| 1. Wilson, W. E., Lazarus, L. H., & Tomer, K. B. (1989). Bradykinin and kininogens in bovine milk. The Journal of Biological Chemistry, 264(30), 17777–17783. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/2808351.
2. Yamamura, J. I., Takada, Y., Goto, M., Kumegawa, M., & Aoe, S. (2000). Bovine milk kininogen fragment 1·2 promotes the proliferation of osteoblastic MC3T3-E1 cells. Biochemical and Biophysical Research Communications, 269(2), 628–632. https://doi.org/10.1006/bbrc.2000.2326.
|
| Bomi1014
| Sterile alpha motif domain containing 7
| Bos taurus
| E1BHF0
| https://www.uniprot.org/uniprot/E1BHF0
| Whey
|
|
| 440
| 48691
| https://www.uniprot.org/uniprot/E1BHF0.fasta
| SAMD7
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1018
| Ubiquitin protein ligase E3 component n-recognin 4
| Bos taurus
| E1BHT5
| https://www.uniprot.org/uniprot/E1BHT5
| Whey, MFGM, Exosome
| NP_001192721.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192721.1
| 5181
| 571959
| https://www.uniprot.org/uniprot/E1BHT5.fasta
| UBR4
| 514561
| https://www.ncbi.nlm.nih.gov/gene/514561
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi102
| Beta-2-microglobulin
| Bos taurus
| P01888
| https://www.uniprot.org/uniprot/P01888
| Whey
| NP_776318.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776318.1
| 118
| 13677
| https://www.uniprot.org/uniprot/P01888.fasta
| B2M
| 280729
| https://www.ncbi.nlm.nih.gov/gene/280729
| Reviewed: Experimental evidence at protein level
| human urine, plasma, and cerebrospinal fiuid.
| Component of class 1 MHC ; its presence is necessary for posttranslational
processing and insertion of HLA heavy chains
into the membrane; stabilize the
structure of the heavy chain and its removal causes loss of
alloantigenic sites on HLA; the MHC class I antigens, in complex with ,ß2m,
participate in specific recognition and functional events
involving both foreign antigens and receptors on cytotoxic T-cell lymphocytes; major protein constituent of the amyloid fibrils in Hemodialysis-associated amyloidosis
| Component of class 1 MHC ; its presence is necessary for posttranslational
processing and insertion of HLA heavy chains
into the membrane; stabilize the
structure of the heavy chain and its removal causes loss of
alloantigenic sites on HLA; the MHC class I antigens, in complex with ,ß2m,
participate in specific recognition and functional events
involving both foreign antigens and receptors on cytotoxic T-cell lymphocytes; major protein constituent of the amyloid fibrils in Hemodialysis-associated amyloidosis
| highest
at the beginning of lactation; transmission of humoral immunity from a mother to
her young in the mouse occurs mostly postnatally by the
uptake of IgG from maternal milk into the pup’s systemic
circulation. IgG binds to the brush
borders of jejunal epithelial cells which fails to happen if ß2M gene is dirupted
| incubating normal ß2M with glucose produces advanced glycatione end products that make ß2M more acidic- promotes amyloidosis
|
| 1BMG, 2XFX, 3L9R, 3PWV, 4F7C, 4F7E, 4IIQ, 4L8S, 4L9L, 4LCC
|
|
| 1. Miyata, T., Oda, O., Inagi, R., Iida, Y., Araki, N., Yamada, N., … Kinoshita, T. (1993). β2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. Journal of Clinical Investigation, 92(3), 1243–1252. https://doi.org/10.1172/JCI116696.
2. Groves, M. L., & Greenberg, R. (1977). Bovine homologue of beta2-microglobulin isolated from milk. Biochemical and Biophysical Research Communications, 77(1), 320–327. https://doi.org/10.1016/s0006-291x(77)80199-x.
3. Becker, J. W., & Reeke, G. N. (1985). Three-dimensional structure of β 2 -microglobulin. Proceedings of the National Academy of Sciences of the United States of America, 82(12), 4225–4229. https://doi.org/10.1073/pnas.82.12.4225.
4. Berggård, I., & Bearn, A. G. (1968). Isolation and properties of a low molecular weight beta-2-globulin occurring in human biological fluids. The Journal of Biological Chemistry, 243(15), 4095–4103. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/4175239.
|
| Bomi1021
| Protein phosphatase 1 regulatory subunit 13B
| Bos taurus
| E1BHY2
| https://www.uniprot.org/uniprot/E1BHY2
| Whey
|
|
| 1096
| 119606
| https://www.uniprot.org/uniprot/E1BHY2.fasta
| PPP1R13B
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1022
| ELM2 and Myb/SANT domain containing 1
| Bos taurus
| E1BI11
| https://www.uniprot.org/uniprot/E1BI11
| Whey
| XP_005212176.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005212176.1
| 1102
| 120962
| https://www.uniprot.org/uniprot/E1BI11.fasta
| ELMSAN1
| 505848
| https://www.ncbi.nlm.nih.gov/gene/505848
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1024
| GM2 ganglioside activator
| Bos taurus
| E1BI28
| https://www.uniprot.org/uniprot/E1BI28
| Whey
|
|
| 193
| 20888
| https://www.uniprot.org/uniprot/E1BI28.fasta
| GM2A
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1025
| Coiled-coil domain containing 158
| Bos taurus
| E1BI42
| https://www.uniprot.org/uniprot/E1BI42
| Whey
|
|
| 1050
| 120346
| https://www.uniprot.org/uniprot/E1BI42.fasta
| CCDC158
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1026
| Interleukin 18 binding protein
| Bos taurus
| E1BI67
| https://www.uniprot.org/uniprot/E1BI67
| Whey
|
|
| 193
| 21559
| https://www.uniprot.org/uniprot/E1BI67.fasta
| IL18BP
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1029
| PTPRF interacting protein alpha 3
| Bos taurus
| E1BIA1
| https://www.uniprot.org/uniprot/E1BIA1
| Whey, Exosome
|
|
| 1221
| 136276
| https://www.uniprot.org/uniprot/E1BIA1.fasta
| PPFIA3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi103
| Alpha-S1-casein
| Bos taurus
| P02662
| https://www.uniprot.org/uniprot/P02662
| Whey
| NP_851372.1
| https://www.ncbi.nlm.nih.gov/protein/NP_851372.1
| 214
| 24529
| https://www.uniprot.org/uniprot/P02662.fasta
| CSN1S1
| 282208
| https://www.ncbi.nlm.nih.gov/gene/282208
| Reviewed: Experimental evidence at protein level
|
| A major allergen
| A major allergen
| found to enhance
calcium absorption resulted in the production of greater
bone mass and correspondingly increased resistance to
bone fracture in the rat femurs
| Phosphoprotein; nine phosphorylated
serine residues and a highly negatively
charged region including residues 41-77
|
|
|
|
| 1. Spuergin, P., Mueller, H., Walter, M., Schiltz, E., & Forster, J. (1996). Allergenic epitopes of bovine alpha S1-casein recognized by human IgE and IgG. Allergy, 51(5), 306–312. https://doi.org/10.1111/j.1398-9995.1996.tb04614.x.
2. Masoodi, T. A., & Shafi, G. (2010). Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation, 4(9), 430.
3. Farrell, H. M., Malin, E. L., Brown, E. M., & Mora-Gutierrez, A. (2009). Review of the chemistry of αS2-casein and the generation of a homologous molecular model to explain its properties. Journal of Dairy Science, 92(4), 1338–1353. https://doi.org/10.3168/jds.2008-1711.
4. Minervini F, Algaron F, Rizzello CG, Fox PF, Monnet V, Gobbetti M. Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Appl Environ Microbiol [Internet]. 2003 Sep [cited 2019 Nov 26];69(9):5297–305. Available from: http://www.ncbi.nlm.nih.gov/pubmed/12957917.
5. Hideaki K, Kunio D, Shigeru S, Hideyo U, Ryuji S, Umeji M, et al. Antihypertensive effect of tryptic hydrolysate of milk casein in spontaneously hypertensive rats. Comp Biochem Physiol Part C, Comp. 1990;96(2):367–71.
6. Loukas S, Varoucha D, Zioudrou C, Streaty RA, Klee WA. Opioid Activities and Structures of α-Casein-Derived Exorphins. Biochemistry. 1983;22(19):4567–73.
7. Maruyama S, Suzuki H. Agricultural and Biological Chemistry A Peptide Inhibitor of Angiotensin I Converting Enzyme in the Tryptic Hydrolysate of Casein. 2014 [cited 2019 Nov 26]; Available from: https://www.tandfonline.com/action/journalInformation?journalCode=tbbb20
|
| Bomi1032
| Vacuolar protein sorting 13 homolog D
| Bos taurus
| E1BIF6
| https://www.uniprot.org/uniprot/E1BIF6
| Whey, Exosome
|
|
| 4364
| 488366
| https://www.uniprot.org/uniprot/E1BIF6.fasta
| VPS13D
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi104
| Alpha-S2-casein
| Bos taurus
| P02663
| https://www.uniprot.org/uniprot/P02663
| Whey
| NP_776953.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776953.1
| 222
| 26019
| https://www.uniprot.org/uniprot/P02663.fasta
| CSN1S2
| 282209
| https://www.ncbi.nlm.nih.gov/gene/282209
| Reviewed: Experimental evidence at protein level
|
| Have unique
antibacterial properties; angiotensin-
I enzyme inhibitor; serve
to dampen allergenic responses; formation of health-promoting dairy products; inhibit
calmodulin-activation of cyclic nucleotide phosphodiesterase; may be involved in promoting
intestinal health and well being ; caprine caseins rich in αS2-CN offer
enhanced sites for interactions with the common food
additive κ-carrageenan
| Have unique
antibacterial properties; angiotensin-
I enzyme inhibitor; serve
to dampen allergenic responses; formation of health-promoting dairy products; inhibit
calmodulin-activation of cyclic nucleotide phosphodiesterase; may be involved in promoting
intestinal health and well being ; caprine caseins rich in αS2-CN offer
enhanced sites for interactions with the common food
additive κ-carrageenan
| found to enhance
calcium absorption resulted in the production of greater
bone mass and correspondingly increased resistance to
bone fracture in the rat femurs
| Phosphorylated; 11 phosphorylated serine residues; phosphorylated
residues varies from 10 to 13 minor degrees of intermolecular
disulfide bonding
|
| 6FS4, 6FS5
|
|
| 1. Spuergin, P., Mueller, H., Walter, M., Schiltz, E., & Forster, J. (1996). Allergenic epitopes of bovine alpha S1-casein recognized by human IgE and IgG. Allergy, 51(5), 306–312. https://doi.org/10.1111/j.1398-9995.1996.tb04614.x.
2. Masoodi, T. A., & Shafi, G. (2010). Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation, 4(9), 430.
3. Farrell, H. M., Malin, E. L., Brown, E. M., & Mora-Gutierrez, A. (2009). Review of the chemistry of αS2-casein and the generation of a homologous molecular model to explain its properties. Journal of Dairy Science, 92(4), 1338–1353. https://doi.org/10.3168/jds.2008-1711.
4. Srinivas S, Prakash V. Bioactive peptides from bovine milk α-casein: Isolation, characterization and multifunctional properties. Int J Pept Res Ther. 2010 Mar;16(1):7–15.
|
| Bomi1042
| Claspin
| Bos taurus
| E1BIR1
| https://www.uniprot.org/uniprot/E1BIR1
| Whey
|
|
| 1247
| 140274
| https://www.uniprot.org/uniprot/E1BIR1.fasta
| CLSPN
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1045
| Protein tyrosine phosphatase, non-receptor type 23
| Bos taurus
| E1BIU7
| https://www.uniprot.org/uniprot/E1BIU7
| Whey, Exosome
|
|
| 1617
| 176321
| https://www.uniprot.org/uniprot/E1BIU7.fasta
| PTPN23
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi105
| Beta-casein
| Bos taurus
| P02666
| https://www.uniprot.org/uniprot/P02666
| Whey
|
|
| 224
| 25107
| https://www.uniprot.org/uniprot/P02666.fasta
| CSN2
|
|
| Reviewed: Experimental evidence at protein level
|
| ß-caseinomorph stimulate human
lymphocyte T proliferation in vitro; ha cytomodulatory properties; enhances nutritional quality in food becausenof high lysine content; film-forming properties of casein may also be used, either as coatings or to reduce oil absorption during the cooking/frying stage in preparing the food
| ß-caseinomorph stimulate human
lymphocyte T proliferation in vitro; ha cytomodulatory properties; enhances nutritional quality in food becausenof high lysine content; film-forming properties of casein may also be used, either as coatings or to reduce oil absorption during the cooking/frying stage in preparing the food
| prime source of calcium and phosphorus for the
neonate; antigen capable of inducing a prolonged immune response. Increased levels of casein antibodies have been found in individuals with schizophrenia before and after diagnosis
| Phosphorylated; presence of 5 phosphates in bovine; site of phosphorylation: Ser-Xxx-Glu/pSer; of 12 genetic
variants of β -casein in bovine only two variants appear to have
altered phosphorylation; Equine β -casein shows variation in phosphorylation, with typically 3 to 7
phosphates on full-length β -casein; the β -casein
of human milk exists as six different forms with 0 to 5 phosphates; Ovine β -casein has variable phosphorylation, with 0 to 7
phosphates
|
|
|
|
| 1. Niebuhr, D. W., Li, Y., Cowan, D. N., Weber, N. S., Fisher, J. A., Ford, G. M., & Yolken, R. (2011). Association between bovine casein antibody and new onset schizophrenia among US military personnel. Schizophrenia Research, 128(1–3), 51–55. https://doi.org/10.1016/j.schres.2011.02.005.
2. Ferranti, P., Pizzano, R., Garro, G., Caira, S., Chianese, L., & Addeo, F. (2001). Mass spectrometry-based procedure for the identification of ovine casein heterogeneity. Journal of Dairy Research, 68(1), 35–51. https://doi.org/10.1017/S0022029900004611.
3. Greenberg, R., Groves, M. L., & Dower, H. J. (1984). Human beta-casein. Amino acid sequence and identification of phosphorylation sites. The Journal of Biological Chemistry, 259(8), 5132–5138. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/6715339.
4. Sato R, Shindo M, Gunshin H, Noguchi T, Naito H. Characterization of phosphopeptide derived from bovine β-casein: an inhibitor to intra-intestinal precipitation of calcium phosphate. Biochim Biophys Acta (BBA)/Protein Struct Mol. 1991 Apr 29;1077(3):413–5.
5. Hayes M, Stanton C, Slattery H, O’Sullivan O, Hill C, Fitzgerald GF, et al. Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors. Appl Environ Microbiol. 2007 Jul;73(14):4658–67.
6. Kitazawa H, Yonezawa K, Tohno M, Shimosato T, Kawai Y, Saito T, et al. Enzymatic digestion of the milk protein β-casein releases potent chemotactic peptide(s) for monocytes and macrophages. Int Immunopharmacol. 2007 Sep;7(9):1150–9.
7. Migliore-Samour D, Floc’h F, Jollès P. Biologically active casein peptides implicated in immunomodulation. J Dairy Res [Internet]. 1989 [cited 2019 Nov 26];56(3):357–62. Available from: http://www.ncbi.nlm.nih.gov/pubmed/2668358.
8. Cieślińska A, Kostyra E, Kostyra H, Oleński K, Fiedorowicz E, Kamiński S. Milk from cows of different β-casein genotypes as a source of β-casomorphin-7. Int J Food Sci Nutr. 2012 Jun;63(4):426–30.
9. Maeno M, Yamamoto N, Takano T. Identification of an Antihypertensive Peptide from Casein Hydrolysate Produced by a Proteinase from Lactobacillus helveticus CP790. J Dairy Sci. 1996;79(8):1316–21.
10. Maruyama S, Suzuki H. A Peptide Inhibitor of Angiotensin I Converting Enzyme in the Tryptic Hydrolysate of Casein. Agric Biol Chem [Internet]. 1982 May 9 [cited 2019 Nov 26];46(5):1393–4. Available from: http://www.tandfonline.com/doi/full/10.1080/00021369.1982.10865255.
11. Maruyama S, Nakagomi K, Tomizuka N, Suzuki H. Angiotensin i-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. Ii. isolation and bradykinin-potentiating activity on the uterus and the ileum of rats. Agric Biol Chem. 1985;49(5):1405–9.
12. Meisel H. Chemical characterization and opioid activity of an exorphin isolated from in vivo digests of casein. FEBS Lett. 1986 Feb 17;196(2):223–7.
|
| Bomi1052
| Cadherin EGF LAG seven-pass G-type receptor 2
| Bos taurus
| E1BJ11
| https://www.uniprot.org/uniprot/E1BJ11
| Whey, MFGM, Exosome
| NP_001179860.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179860.1
| 2920
| 316840
| https://www.uniprot.org/uniprot/E1BJ11.fasta
| CELSR2
| 538194
| https://www.ncbi.nlm.nih.gov/gene/538194
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1057
| DExH-box helicase 34
| Bos taurus
| E1BJ90
| https://www.uniprot.org/uniprot/E1BJ90
| Whey, MFGM, Exosome
|
|
| 1146
| 128790
| https://www.uniprot.org/uniprot/E1BJ90.fasta
| DHX34
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi106
| Fibrinogen beta chain
| Bos taurus
| P02676
| https://www.uniprot.org/uniprot/P02676
| Whey
|
|
| 468
| 53340
| https://www.uniprot.org/uniprot/P02676.fasta
| FGB
|
|
| Reviewed: Experimental evidence at protein level
| Plasma; seminal plasma
| Participates in blood clotting; sperm protection from proteolysis; acts as agglutination factor to regulate capacitation
| Participates in blood clotting; sperm protection from proteolysis; acts as agglutination factor to regulate capacitation
| Regulated clotting of milk; high in cinical and subclinical mastitis
| Glycosylated; biantennary oligosaccharides; sialic acids vary in the normal subpopulation of fibrinogen polypeptide as found in humans; sialic acids linkage in monosialylated sugars is either on 90% Manα(l -3) side and 10% on the Manα(1-6) side ;
|
| 1deq, 1jy2, 1jy3, 2z4e, 3h32
|
|
| 1. Rego, J. P. A., Crisp, J. M., Moura, A. A., Nouwens, A. S., Li, Y., Venus, B., Corbet, N. J., Corbet, D. H., Burns, B. M., Boe-Hansen, G. B., and McGowan, M. R. (2014) Seminal plasma proteome of electroejaculated Bos indicus bulls. Anim. Reprod. Sci. 148, 1–17.
2. Prunkard, D., Cottingham, I., Garner, I., Bruce, S., Dalrymple, M., Lasser, G., Bishop, P., and Foster, D. (1996) High-level expression of recombinant human fibrinogen in the milk of transgenic mice. Nat. Biotechnol. 14, 867–871.
3. Hermans, J. and McDonagh, J. (1982) Fibrin: Structure and Interactions. Semin. Thromb. Hemost. 8, 11–24.
4. Hessel, B., Makino, M., Iwanaga, S., and Blombäck, B. (1979) Primary structure of human fibrinogen and fibrin. Structural studies on NH2-terminal part of B beta chain. Eur. J. Biochem. 98, 521–534.
. 5. Martinez, J., Palascak, J. E., and Kwasniak, D. (1978) Abnormal sialic acid content of the dysfibrinogenemia associated with liver disease. J. Clin. Invest. 61, 535–538.
6. Palascak, J. E. and Martinez, J. (1977) Dysfibrinogenemia Associated with Liver Disease. J. Clin. Invest. 60, 89–95.
7. Gralnick, H. R., Givelber, H., and Abrams, E. (1978) Dysfibrinogenemia Associated with Hepatoma. N. Engl. J. Med. 299, 221–226.
8. Martinez, J., MacDonald, K. A., and Palascak, J. E. (1983) The role of sialic acid in the dysfibrinogenemia associated with liver disease: distribution of sialic acid on the constituent chains. Blood 61, 1196–1202.
9. Marguerie, G., Chagniel, G., and Suscillon, M. (1977) The binding of calcium to bovine fibrinogen. Biochim. Biophys. Acta 490, 94–103.
10. Van Ruijven-Vermeer, I. A. M., Nieuwenhuizen, W., and Nooijen, W. J. (1978) Ca binding of rat fibrinogen and fibrin(ogen) degradation products. FEBS Lett. 93, 177–180
|
| Bomi1061
| Tau tubulin kinase 2
| Bos taurus
| E1BJC2
| https://www.uniprot.org/uniprot/E1BJC2
| Whey
| NP_001193000.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193000.1
| 1243
| 137284
| https://www.uniprot.org/uniprot/E1BJC2.fasta
| TTBK2
| 541215
| https://www.ncbi.nlm.nih.gov/gene/541215
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1066
| Uncharacterized protein
| Bos taurus
| E1BJH3
| https://www.uniprot.org/uniprot/E1BJH3
| Whey, Exosome
|
|
| 456
| 52648
| https://www.uniprot.org/uniprot/E1BJH3.fasta
| CNTRL
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1067
| Myotubularin related protein 6
| Bos taurus
| E1BJH8
| https://www.uniprot.org/uniprot/E1BJH8
| Whey
|
|
| 621
| 71602
| https://www.uniprot.org/uniprot/E1BJH8.fasta
| MTMR6
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1068
| Axonemal dynein light chain domain containing 1
| Bos taurus
| E1BJH9
| https://www.uniprot.org/uniprot/E1BJH9
| Whey
|
|
| 997
| 115957
| https://www.uniprot.org/uniprot/E1BJH9.fasta
| AXDND1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi107
| Beta-lactoglobulin
| Bos taurus
| P02754
| https://www.uniprot.org/uniprot/P02754
| Whey
|
|
| 178
| 19883
| https://www.uniprot.org/uniprot/P02754.fasta
| LGB
| 280838
| https://www.ncbi.nlm.nih.gov/gene/280838
| Reviewed: Experimental evidence at protein level
|
| Role in molecular transport or possibly some form of modulator; binds both fatty
acids and retinol
| Role in molecular transport or possibly some form of modulator; binds both fatty
acids and retinol
| Dominant bovine milk allergen;
|
|
| 1B0O, 1B8E, 1BEB, 1BSO, 1BSQ, 1BSY, 1CJ5, 1DV9, 1GX8, 1GX9, 1GXA, 1QG5, 1UZ2, 1YUP, 2AKQ, 2BLG, 2GJ5, 2Q2M, 2Q2P, 2Q39, 2R56, 3BLG, 3KZA, 3NPO, 3NQ3, 3NQ9, 3PH5, 3PH6, 3UEU, 3UEV, 3UEW, 3UEX, 4DQ3, 4DQ4, 4GNY, 4IB6, 4IB7, 4IB8, 4IB9, 4IBA, 4KII, 4LZU, 4LZV, 4Y0P, 4Y0Q, 4Y0R, 5EEE, 5HTD, 5HTE, 5IO5, 5IO7, 5K06, 5LKE, 5LKF, 5NUJ, 5NUK, 5NUM, 5NUN, 5Y5C, 6FXB, 6GE7, 6GF9, 6GFS, 6GHH, 6NKQ, 6QI6, 6QI7, 6QPD, 6QPE, 6RWP, 6RWQ, 6RWR, 6rys, 6ryt
|
|
| 1. Duan, C., Li, A., Yang, L., Zhao, R., Fan, W., and Huo, G. (2014) Comparison of immunomodulating properties of Beta-lactoglobulin and its hydrolysates. Iran. J. Allergy. Asthma. Immunol. 13, 26–32.
2. de Jongh, H. H. J., Gröneveld, T., and de Groot, J. (2001) Mild Isolation Procedure Discloses New Protein Structural Properties of β-Lactoglobulin. J. Dairy Sci. 84, 562–571.
3. Prioult, G., Pecquet, S., and Fliss, I. (2005) Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes. Int. Dairy J. 15, 439–448.
4. Kontopidis, G., Holt, C., and Sawyer, L. (2004) Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function. J. Dairy Sci. 87, 785–796.
5. Kontopidis, G., Holt, C., and Sawyer, L. (2002) The Ligand-binding Site of Bovine β-Lactoglobulin: Evidence for a Function? J. Mol. Biol. 318, 1043–1055.
6. Fogliano, V., Monti, S. M., Visconti, A., Randazzo, G., Facchiano, A. M., Colonna, G., and Ritieni, A. (1998) Identification of a beta-lactoglobulin lactosylation site. Biochim. Biophys. Acta 1388, 295–304.
7. Morgan, F., Léonil, J., Mollé, D., and Bouhallab, S. (1997) Nonenzymatic lactosylation of bovine beta-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 236, 413–417.
8. Yamauchi R, Ohinata K, Yoshikawa M. β-Lactotensin and neurotensin rapidly reduce serum cholesterol via NT2 receptor. Peptides. 2003;24(12):1955–61.
9. Mullally MM, Meisel H, FitzGerald RJ. Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β-lactoglobulin. FEBS Lett [Internet]. 1997 Jan 27 [cited 2019 Nov 26];402(2–3):99–101. Available from: http://doi.wiley.com/10.1016/S0014-5793%2896%2901503-7.
10. FitzGerald RJ, Meisel H. Lactokinins: Whey protein-derived ACE inhibitory peptides. Nahrung - Food. 1999 Jun;43(3):165–7.
|
| Bomi1073
| Zinc finger protein 618
| Bos taurus
| E1BJV7
| https://www.uniprot.org/uniprot/E1BJV7
| Whey, Exosome
| XP_015328190.1
| https://www.ncbi.nlm.nih.gov/protein/XP_015328190.1
| 943
| 104084
| https://www.uniprot.org/uniprot/E1BJV7.fasta
| ZNF618
| 528603
| https://www.ncbi.nlm.nih.gov/gene/528603
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1076
| Signal peptide, CUB domain and EGF like domain containing 3
| Bos taurus
| E1BJX6
| https://www.uniprot.org/uniprot/E1BJX6
| Whey
|
|
| 993
| 109182
| https://www.uniprot.org/uniprot/E1BJX6.fasta
| SCUBE3
| 100300124
| https://www.ncbi.nlm.nih.gov/gene/100300124
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1077
| Interferon induced with helicase C domain 1
| Bos taurus
| E1BJZ0
| https://www.uniprot.org/uniprot/E1BJZ0
| Whey
|
|
| 1021
| 115341
| https://www.uniprot.org/uniprot/E1BJZ0.fasta
| IFIH1
| 535490
| https://www.ncbi.nlm.nih.gov/gene/535490
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1078
| GRIP and coiled-coil domain containing 1
| Bos taurus
| E1BJZ4
| https://www.uniprot.org/uniprot/E1BJZ4
| Whey
| NP_001192673.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192673.1
| 775
| 87603
| https://www.uniprot.org/uniprot/E1BJZ4.fasta
| GCC1
| 539985
| https://www.ncbi.nlm.nih.gov/gene/539985
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi108
| Cathepsin Z
| Bos taurus
| P05689
| https://www.uniprot.org/uniprot/P05689
| Whey
| NP_001071303.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001071303.1
| 304
| 33886
| https://www.uniprot.org/uniprot/P05689.fasta
| CTSZ
| 404187
| https://www.ncbi.nlm.nih.gov/gene/404187
| Reviewed: Experimental evidence at transcript level
| monocytes/macrophages,
dendritic cells, endothelial cells and certain
cancers,
| Involvement
in inflammatory processes and
immune functions; may participate in signaling through its interaction
with integrins and/or cell surface proteoglycans; facilitates cellular adhesion and migration processes;
| Involvement
in inflammatory processes and
immune functions; may participate in signaling through its interaction
with integrins and/or cell surface proteoglycans; facilitates cellular adhesion and migration processes;
|
|
|
|
|
|
| 1. Nägler, D. K., Zhang, R., Tam, W., Sulea, T., Purisima, E. O., & Ménard, R. (1999). Human cathepsin X: A cysteine protease with unique carboxypeptidase activity. Biochemistry, 38(39), 12648–12654. https://doi.org/10.1021/bi991371z.
2. Klemencic, I., Carmona, A. K., Cezari, M. H., Juliano, M. A., Juliano, L., Guncar, G., … Turk, B. (2000). Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. European Journal of Biochemistry, 267(17), 5404–5412. https://doi.org/10.1046/j.1432-1327.2000.01592.x.
3. Devanathan, G., Turnbull, J. L., Ziomek, E., Purisima, E. O., Ménard, R., & Sulea, T. (2005). Carboxy-monopeptidase substrate specificity of human cathepsin X. Biochemical and Biophysical Research Communications, 329(2), 445–452. https://doi.org/10.1016/j.bbrc.2005.01.150.
4. Puzer, L., Cotrin, S. S., Cezari, M. H. S., Hirata, I. Y., Juliano, M. A., Stefe, I., … Carmona, A. K. (2005). Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L. Biological Chemistry, 386(11), 1191–1195. https://doi.org/10.1515/BC.2005.136.
5. Staudt, N. D., Aicher, W. K., Kalbacher, H., Stevanovic, S., Carmona, A. K., Bogyo, M., & Klein, G. (2010). Cathepsin X is secreted by human osteoblasts, digests CXCL-12 and impairs adhesion of hematopoietic stem and progenitor cells to osteoblasts. Haematologica, 95(9), 1452–1460. https://doi.org/10.3324/haematol.2009.018671.
6. Nägler, D. K., Kraus, S., Feierler, J., Mentele, R., Lottspeich, F., Jochum, M., & Faussner, A. (2010). A cysteine-type carboxypeptidase, cathepsin X, generates peptide receptor agonists. International Immunopharmacology, 10(1), 134–139. https://doi.org/10.1016/j.intimp.2009.09.018.
7. Obermajer, N., Svajger, U., Bogyo, M., Jeras, M., & Kos, J. (2008). Maturation of dendritic cells depends on proteolytic cleavage by cathepsin X. Journal of Leukocyte Biology, 84(5), 1306–1315. https://doi.org/10.1189/jlb.0508285.
8. Krueger, S., Kalinski, T., Hundertmark, T., Wex, T., Küster, D., Peitz, U., … Roessner, A. (2005). Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer. The Journal of Pathology, 207(1), 32–42. https://doi.org/10.1002/path.1820.
|
| Bomi1082
| Uncharacterized protein (Fragment)
| Bos taurus
| E1BK38
| https://www.uniprot.org/uniprot/E1BK38
| Whey, Exosome
|
|
| 4971
| 559908
| https://www.uniprot.org/uniprot/E1BK38.fasta
| ABCA13
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1088
| Nipped-B protein
| Bos taurus
| E1BKC4
| https://www.uniprot.org/uniprot/E1BKC4
| Whey, MFGM, Exosome
| NP_001193513.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193513.1
| 2804
| 316227
| https://www.uniprot.org/uniprot/E1BKC4.fasta
| NIPBL
| 539566
| https://www.ncbi.nlm.nih.gov/gene/539566
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi109
| Angiogenin1
| Bos taurus
| P10152
| https://www.uniprot.org/uniprot/P10152
| Whey
|
|
| 148
| 16970
| https://www.uniprot.org/uniprot/P10152.fasta
| ANG1
|
|
| Reviewed: Experimental evidence at protein level
| liver, placenta, epthelial cells, fibroblasts, blood cells, serum
| Active inductor of vessel growth; maintenance of homeostasis in living organisms; regulates immune system
| Active inductor of vessel growth; maintenance of homeostasis in living organisms; regulates immune system
| Induced production of cytokines in leukocytes;
|
|
| 1AGI, 1GIO
|
|
| 1. Maes, P., Damart, D., Rommens, C., Montreuil, J., Spik, G., & Tartar, A. (1988). The complete amino acid sequence of bovine milk angiogenin. FEBS Letters, 241(1–2), 41–45. https://doi.org/10.1016/0014-5793(88)81027-5.
2. Shcheglovitova, O. N., Maksyanina, E. V., Ionova, I. I., Rustam’yan, Y. L., & Komolova, G. S. (2003). Cow milk angiogenin induces cytokine production in human blood leukocytes. Bulletin of Experimental Biology and Medicine, 135(2), 158–160. https://doi.org/10.1023/A:1023871931764.
|
| Bomi1090
| Inositol 1,4,5-trisphosphate receptor type 3
| Bos taurus
| E1BKE7
| https://www.uniprot.org/uniprot/E1BKE7
| Whey, MFGM, Exosome
|
|
| 2664
| 303284
| https://www.uniprot.org/uniprot/E1BKE7.fasta
| ITPR3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1092
| RNA polymerase III subunit E
| Bos taurus
| E1BKG7
| https://www.uniprot.org/uniprot/E1BKG7
| Whey
|
|
| 711
| 79944
| https://www.uniprot.org/uniprot/E1BKG7.fasta
| POLR3E
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1098
| Transcription factor E2F8
| Bos taurus
| E1BKK0
| https://www.uniprot.org/uniprot/E1BKK0
| Whey
| NP_001178163.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001178163.1
| 866
| 94043
| https://www.uniprot.org/uniprot/E1BKK0.fasta
| E2F8
| 786629
| https://www.ncbi.nlm.nih.gov/gene/786629
| Reviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi11
| Cathelicidin-2
| Bos taurus
| P19660
| https://www.uniprot.org/uniprot/P19660
| Whey
| NP_777251.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777251.1
| 176
| 20030
| https://www.uniprot.org/uniprot/P19660.fasta
| CATHL2
| 282165
| https://www.ncbi.nlm.nih.gov/gene/282165
| Reviewed: Experimental evidence at protein level
| bovine neutrophil
| almost exclusively
active against Gram-negative bacteria; non-lytic and is efficiently internalized by bacterial cells without
membrane disruption, enabling access to intracellular targets
| almost exclusively
active against Gram-negative bacteria; non-lytic and is efficiently internalized by bacterial cells without
membrane disruption, enabling access to intracellular targets
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
|
| pig leukocyte protein named cathelin shared similar
size and higher than70% sequence
identity to bovine cathelicidin 2
|
| 1. Smith, W. L., Sunaga, O., and Cullor, J. S. (1999) An evaluation of the tissue expression of a bovine dodecapeptide bactenecin in the adult and fetal animal. Comp. Haematol. Int. 9, 132–138.
2. 1. Tomasinsig, L., Scocchi, M., Di Loreto, C., Artico, D., and Zanetti, M. (2002) Inducible expression of an antimicrobial peptide of the innate immunity in polymorphonuclear leukocytes. J. Leukoc. Biol. 72, 1003–1010
|
| Bomi110
| Alpha-2-HS-glycoprotein
| Bos taurus
| P12763
| https://www.uniprot.org/uniprot/P12763
| Whey
| NP_776409.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776409.1
| 359
| 38419
| https://www.uniprot.org/uniprot/P12763.fasta
| AHSG
| 280988
| https://www.ncbi.nlm.nih.gov/gene/280988
| Reviewed: Experimental evidence at protein level
| Serum;
| Role in bone formation, opsonization, cellular immunity; modulate the inflammatory potential of
basic calcium phosphate crystals associated with various
clinical manifestations of inflammation; chondrocyte
differentiation ; negative acute phase proteins; free fatty acid transporter; enhances cellular lipid uptake and lipogenesis
| Role in bone formation, opsonization, cellular immunity; modulate the inflammatory potential of
basic calcium phosphate crystals associated with various
clinical manifestations of inflammation; chondrocyte
differentiation ; negative acute phase proteins; free fatty acid transporter; enhances cellular lipid uptake and lipogenesis
| Abundant in mastitic milk; enhances lipid uptake and lipogenesis in milk
| three potential N-glycosylation
sites identified in mouse AHSG are conserved
in bovine fetuin, while only two of them are conserved
in human AHSG; in humans A-chain of a2HS
contains 2 biantennary N- and 2 O-linked glycans; N-glycan has a2-6
NeuAc residues, 4
Gal, αMan, N glycans are partially (~90%) sialylated; O-glycans have partially sialylated 2.5 α2-3-linked NeuAc; 3 0-trisaccharides
have the structure NeuAcα2-3Gal01-3GalNAcαl-
0
|
|
|
|
| 1. Yang, F., Chen, Z. L., Bergeron, J. M., Cupples, R. L., & Friedrichs, W. E. (1992). Human alpha 2-HS-glycoprotein/bovine fetuin homologue in mice: identification and developmental regulation of the gene. Biochimica et Biophysica Acta, 1130(2), 149–156. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1373325.
Watzlawick, H., Walsh, M. T., Yoshioka, Y., Schmid, K., & Brossmer, R. (1992). Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases. Biochemistry, 31(48), 12198–12203. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1457416.
3. Strieder-Barboza, C., de Souza, J., Raphael, W., Lock, A. L., & Contreras, G. A. (2018). Fetuin-A: A negative acute-phase protein linked to adipose tissue function in periparturient dairy cows. Journal of Dairy Science, 101(3), 2602–2616. https://doi.org/10.3168/jds.2017-13644.
|
| Bomi1104
| Centrosomal protein 250
| Bos taurus
| E1BKP6
| https://www.uniprot.org/uniprot/E1BKP6
| Whey, MFGM, Exosome
|
|
| 2434
| 279170
| https://www.uniprot.org/uniprot/E1BKP6.fasta
| CEP250
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1106
| Myosin XVIIIA
| Bos taurus
| E1BKQ6
| https://www.uniprot.org/uniprot/E1BKQ6
| Whey, Exosome
|
|
| 953
| 111063
| https://www.uniprot.org/uniprot/E1BKQ6.fasta
| MYO18A
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi111
| Fibrinogen gamma B
| Bos taurus
| P12799
| https://www.uniprot.org/uniprot/P12799
| Whey
| NP_776336.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776336.1
| 444
| 50244
| https://www.uniprot.org/uniprot/P12799.fasta
| FGG
| 280792
| https://www.ncbi.nlm.nih.gov/gene/280792
| Reviewed: Experimental evidence at protein level
|
| fibrin polymerization
and cross-linking, role in the initiation of
fibrinolysis, binding and regulation of factor XIII activity,
interactions with platelets and other cells, and role in
mediating thrombin binding to fibrin, a thrombin inhibitory
function termed ‘antithrombin I
| fibrin polymerization
and cross-linking, role in the initiation of
fibrinolysis, binding and regulation of factor XIII activity,
interactions with platelets and other cells, and role in
mediating thrombin binding to fibrin, a thrombin inhibitory
function termed ‘antithrombin I
| Acute phase proteins; potential marker of mastitis
|
|
| 1DEQ, 1JY2, 1JY3
|
|
| 1. Kanaide, H., & Shainoff, J. R. (1975). Cross-linking of fibrinogen and fibrin by fibrin-stablizing factor (factor XIIIa). The Journal of Laboratory and Clinical Medicine, 85(4), 574–597. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1168234.
2. McKee, P. A., Mattock, P., & Hill, R. L. (1970). Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proceedings of the National Academy of Sciences of the United States of America, 66(3), 738–744. https://doi.org/10.1073/pnas.66.3.738.
3. Siebenlist, K. R., Meh, D. A., & Mosesson, M. W. (2001). Protransglutaminase (factor XIII) mediated crosslinking of fibrinogen and fibrin. Thrombosis and Haemostasis, 86(5), 1221–1228. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11816711.
4. Mosesson, M. W., Siebenlist, K. R., Hainfeld, J. F., & Wall, J. S. (1995). The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. Journal of Structural Biology, 115(1), 88–101. https://doi.org/10.1006/jsbi.1995.1033.
5. Hoeprich, P. D., & Doolittle, R. F. (1983). Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation. Biochemistry, 22(9), 2049–2055. https://doi.org/10.1021/bi00278a003.
6. Zhang, J. Z., & Redman, C. M. (1992). Identification of B beta chain domains involved in human fibrinogen assembly. The Journal of Biological Chemistry, 267(30), 21727–21732. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1400483.
7. Huang, S., Cao, Z., & Davie, E. W. (1993). The role of amino-terminal disulfide bonds in the structure and assembly of human fibrinogen. Biochemical and Biophysical Research Communications, 190(2), 488–495. https://doi.org/10.1006/bbrc.1993.1074.
8. Blombäck, B., Hessel, B., & Hogg, D. (1976). Disulfide bridges in nh2 -terminal part of human fibrinogen. Thrombosis Research, 8(5), 639–658. https://doi.org/10.1016/0049-3848(76)90245-0.
|
| Bomi1110
| Desmoplakin
| Bos taurus
| E1BKT9
| https://www.uniprot.org/uniprot/E1BKT9
| Whey, MFGM, Exosome
|
|
| 2889
| 332408
| https://www.uniprot.org/uniprot/E1BKT9.fasta
| DSP
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1112
| SEC23 interacting protein
| Bos taurus
| E1BKW5
| https://www.uniprot.org/uniprot/E1BKW5
| Whey, Exosome
| XP_005225831.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005225831.1
| 1006
| 111887
| https://www.uniprot.org/uniprot/E1BKW5.fasta
| SEC23IP
| 508557
| https://www.ncbi.nlm.nih.gov/gene/508557
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1115
| Intersectin 1
| Bos taurus
| E1BKY4
| https://www.uniprot.org/uniprot/E1BKY4
| Whey, Exosome
|
|
| 1716
| 194799
| https://www.uniprot.org/uniprot/E1BKY4.fasta
| ITSN1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1118
| Golgin B1
| Bos taurus
| E1BKZ5
| https://www.uniprot.org/uniprot/E1BKZ5
| Whey, Exosome
|
|
| 3228
| 372439
| https://www.uniprot.org/uniprot/E1BKZ5.fasta
| GOLGB1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1119
| Sortilin
| Bos taurus
| E1BKZ9
| https://www.uniprot.org/uniprot/E1BKZ9
| Whey
|
|
| 876
| 96446
| https://www.uniprot.org/uniprot/E1BKZ9.fasta
| SORT1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi112
| Apolipoprotein A-I
| Bos taurus
| P15497
| https://www.uniprot.org/uniprot/P15497
| Whey
| NP_776667.2
| https://www.ncbi.nlm.nih.gov/protein/NP_776667.2
| 265
| 30276
| https://www.uniprot.org/uniprot/P15497.fasta
| APOA1
| 281631
| https://www.ncbi.nlm.nih.gov/gene/281631
| Reviewed: Experimental evidence at protein level
| Serum,
| Role in reverse cholesterol transport; formation and stabilization of the HDL particle structure, interacting with the ABCA-I transporter; activating lecithin cholesterol acyl transferase; acting as a ligand for the hepatic scavenger receptor
| Role in reverse cholesterol transport; formation and stabilization of the HDL particle structure, interacting with the ABCA-I transporter; activating lecithin cholesterol acyl transferase; acting as a ligand for the hepatic scavenger receptor
|
| Lipoprotein; forty-four residue consensus sequence peptides (ABAB), real sequence peptides, RSP-1 (H4–5) and RSP-2 (H5–H6) were studied in plasma. RSP-1 exhibited higher lipid affinity than RSP-2 in terms of helical structure induced by detergent, suggesting that H4 has higher lipid-binding affinity than H6; little difference was seen in the α-helical content or lipid affinity of the larger vs. the 22-mer peptides, indicating that the individual domains do not fold/bind lipid cooperatively;
|
|
|
|
| 1. Lee, J.-Y. and Parks, J. S. (2005) ATP-binding cassette transporter AI and its role in HDL formation. Curr. Opin. Lipidol. 16, 19–25.
2. Fielding, C. J., Shore, V. G., and Fielding, P. E. (1972) A protein cofactor of lecithin:cholesterol acyltransferase. Biochem. Biophys. Res. Commun. 46, 1493–1498.
3. Acton, S., Rigotti, A., Landschulz, K. T., Xu, S., Hobbs, H. H., and Krieger, M. (1996) Identification of scavenger receptor SR-BI as a high density lipoprotein receptor. Science 271, 518–520.
4. Gorshkova, I. N., Liu, T., Zannis, V. I., and Atkinson, D. (2002) Lipid-free structure and stability of apolipoprotein A-I: probing the central region by mutation. Biochemistry 41, 10529–10539.
5. Palgunachari, M. N., Mishra, V. K., Lund-Katz, S., Phillips, M. C., Adeyeye, S. O., Alluri, S., Anantharamaiah, G. M., and Segrest, J. P. (1996) Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly. Arterioscler. Thromb. Vasc. Biol. 16, 328–338.
6. Zhu, H. L. and Atkinson, D. (2007) Conformation and Lipid Binding of a C-Terminal (198−243) Peptide of Human Apolipoprotein A-I †. Biochemistry 46, 1624–1634.
|
| Bomi1120
| Xin actin binding repeat containing 2
| Bos taurus
| E1BL04
| https://www.uniprot.org/uniprot/E1BL04
| Whey, MFGM, Exosome
|
|
| 3307
| 375583
| https://www.uniprot.org/uniprot/E1BL04.fasta
| XIRP2
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1122
| Aldehyde oxidase 4
| Bos taurus
| E1BL62
| https://www.uniprot.org/uniprot/E1BL62
| Whey, MFGM
| NP_001268848.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001268848.1
| 1335
| 148142
| https://www.uniprot.org/uniprot/E1BL62.fasta
| AOX4
| 518393
| https://www.ncbi.nlm.nih.gov/gene/518393
| Unreveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1126
| Dynein axonemal heavy chain 17
| Bos taurus
| E1BLB4
| https://www.uniprot.org/uniprot/E1BLB4
| Whey, MFGM, Exosome
|
|
| 4453
| 508122
| https://www.uniprot.org/uniprot/E1BLB4.fasta
| DNAH17
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1127
| Protein kinase, DNA-activated, catalytic subunit
| Bos taurus
| E1BLB6
| https://www.uniprot.org/uniprot/E1BLB6
| Whey, MFGM, Exosome
|
|
| 4124
| 464589
| https://www.uniprot.org/uniprot/E1BLB6.fasta
| PRKDC
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1129
| Eukaryotic translation initiation factor 4 gamma 3
| Bos taurus
| E1BLC8
| https://www.uniprot.org/uniprot/E1BLC8
| Whey, MFGM
|
|
| 1545
| 171805
| https://www.uniprot.org/uniprot/E1BLC8.fasta
| EIF4G3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi113
| Butyrophilin subfamily 1 member A1
| Bos taurus
| P18892
| https://www.uniprot.org/uniprot/P18892
| Whey
| NP_776933.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776933.1
| 526
| 59277
| https://www.uniprot.org/uniprot/P18892.fasta
| BTN1A1
| 282157
| https://www.ncbi.nlm.nih.gov/gene/282157
| Reviewed: Experimental evidence at protein level
| Abundant in milk fat globule membrane,
| butyrophilin mRNA correlates with the onset of milk fat secretion toward the end of pregnancy and is maintained throughout lactation; acts as a receptor, facilitating the
interaction between cytoplasmic lipid droplets
and the apical plasma membrane; the major component of a proteinaceous layer
between the plasma membrane and lipid droplet
surface; associated with complex immunological phenomena; regulate the function of T cells by engaging poorly defined receptors on both αβ and γδ T cells
| butyrophilin mRNA correlates with the onset of milk fat secretion toward the end of pregnancy and is maintained throughout lactation; acts as a receptor, facilitating the
interaction between cytoplasmic lipid droplets
and the apical plasma membrane; the major component of a proteinaceous layer
between the plasma membrane and lipid droplet
surface; associated with complex immunological phenomena; regulate the function of T cells by engaging poorly defined receptors on both αβ and γδ T cells
| protein associated in large
amounts with MFGM and has
function in the secretion of milk fat globules
| N linked glycosylation in the exoplasmic domain; presence of mannaose, galactose and N-acetylglucosamine; 3 potential N-glycosylation sites - 2 in the -NH2 terminal and 1 in -COOH terminal; Acylation with myristate, stearate, palmitate and oleate
|
| 4hh8
|
|
| 1. Franke, W. W., Heid, H. W., Grund, C., Winter, S., Freudenstein, C., Schmid, E., Jarasch, E. D., and Keenan, T. W. (1981) Antibodies to the major insoluble milk fat globule membrane-associated protein: specific location in apical regions of lactating epithelial cells. J. Cell Biol. 89, 485–494.
2. Franke, W. W., Lüder, M. R., Kartenbeck, J., Zerban, H., and Keenan, T. W. (1976) Involvement of vesicle coat material in casein secretion and surface regeneration. J. Cell Biol. 69, 173–195.
3. Gavel, Y. and von Heijne, G. (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3, 433–442.
4. Hirano, H., Parkhouse, B., Nicolson, G. L., Lennox, E. S., and Singer, S. J. (1972) Distribution of saccharide residues on membrane fragments from a myeloma-cell homogenate: its implications for membrane biogenesis. Proc. Natl. Acad. Sci. U. S. A. 69, 2945–2949.
5. Keenan, T. W., Heid, H. W., Stadler, J., Jarasch, E. d, and Franke, W. W. (1982) Tight attachment of fatty acids to proteins associated with milk lipid globule membrane. Eur. J. Cell Biol. 26, 270–276.
6. Freudenstein, C., Keenan, T. W., Eigel, W. N., Sasaki, M., Stadler, J., and Franke, W. W. (1979) Preparation and characterization of the inner coat material associated with fat globule membranes from bovine and human milk. Exp. Cell Res. 118, 277–294
|
| Bomi1130
| HECT domain E3 ubiquitin protein ligase 1
| Bos taurus
| E1BLD1
| https://www.uniprot.org/uniprot/E1BLD1
| Whey, MFGM, Exosome
|
|
| 2610
| 289338
| https://www.uniprot.org/uniprot/E1BLD1.fasta
| HECTD1
| 536240
| https://www.ncbi.nlm.nih.gov/gene/536240
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1134
| Synaptonemal complex protein 1
| Bos taurus
| E1BLN1
| https://www.uniprot.org/uniprot/E1BLN1
| Whey
|
|
| 915
| 106886
| https://www.uniprot.org/uniprot/E1BLN1.fasta
| SYCP1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1138
| Caspase 8 associated protein 2
| Bos taurus
| E1BLU4
| https://www.uniprot.org/uniprot/E1BLU4
| Whey, Exosome
| XP_010806816.1
| https://www.ncbi.nlm.nih.gov/protein/XP_010806816.1
| 1973
| 221236
| https://www.uniprot.org/uniprot/E1BLU4.fasta
| CASP8AP2
| 505138
| https://www.ncbi.nlm.nih.gov/gene/505138
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi114
| Cathelicidin-3
| Bos taurus
| P19661
| https://www.uniprot.org/uniprot/P19661
| Whey
| NP_776426.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776426.1
| 190
| 21567
| https://www.uniprot.org/uniprot/P19661.fasta
| CATHL3
| 281037
| https://www.ncbi.nlm.nih.gov/gene/281037
| Reviewed: Experimental evidence at protein level
| bovine neutrophil
| antimicrobial activity
against Gram-negative bacteria; internalized into the cell where it inactivates intracellular
targets; micropinocytosis; has cytolytic activity,
involving membrane disruption and necrosis of host mammalian
cells; In terms of fungicidal activity,
Bac7 is active against Cryptococcus neoformans, which infects the
lungs and central nervous system; displays activity against several Chlamydia strains; inhibit biofilms; prevents bacterial metabolism,
likely disrupting biofilm formation
| antimicrobial activity
against Gram-negative bacteria; internalized into the cell where it inactivates intracellular
targets; micropinocytosis; has cytolytic activity,
involving membrane disruption and necrosis of host mammalian
cells; In terms of fungicidal activity,
Bac7 is active against Cryptococcus neoformans, which infects the
lungs and central nervous system; displays activity against several Chlamydia strains; inhibit biofilms; prevents bacterial metabolism,
likely disrupting biofilm formation
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
| 4JWC, 4JWD, 5F8K, 5HAU
|
|
| 1. Donati, M., Di Francesco, A., Gennaro, R., Benincasa, M., Magnino, S., Pignanelli, S., Shurdhi, A., Moroni, A., Mazzoni, C., Merialdi, G., Baldelli, R., and Cevenini, R. (2007) Sensitivity of Chlamydia suis to cathelicidin peptides. Vet. Microbiol. 123, 269–273.
2. Pompilio, A., Scocchi, M., Pomponio, S., Guida, F., Di Primio, A., Fiscarelli, E., Gennaro, R., and Di Bonaventura, G. (2011) Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients. Peptides 32, 1807–1814. >br/> 3.Tomasinsig, L., Benincasa, M., Scocchi, M., Skerlavaj, B., Tossi, A., Zanetti, M., and Gennaro, R. (2010) Role of Cathelicidin Peptides in Bovine Host Defense and Healing. Probiotics Antimicrob. Proteins 2, 12–20.
4. Frank, R. W., Gennaro, R., Schneider, K., Przybylski, M., and Romeo, D. (1990) Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J. Biol. Chem. 265, 18871–18874.
5. Pelillo, C., Benincasa, M., Scocchi, M., Gennaro, R., Tossi, A., and Pacor, S. (2014) Cellular internalization and cytotoxicity of the antimicrobial proline-rich peptide Bac7(1-35) in monocytes/macrophages, and its activity against phagocytosed Salmonella typhimurium. Protein Pept. Lett. 21, 382–390.
|
| Bomi1144
| Ras protein specific guanine nucleotide releasing factor 1
| Bos taurus
| E1BM01
| https://www.uniprot.org/uniprot/E1BM01
| Whey
| NP_001178386.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001178386.1
| 1257
| 143089
| https://www.uniprot.org/uniprot/E1BM01.fasta
| RASGRF1
| 520039
| https://www.ncbi.nlm.nih.gov/gene/520039
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi115
| Conglutinin
| Bos taurus
| P23805
| https://www.uniprot.org/uniprot/P23805
| Whey
| NP_783630.2
| https://www.ncbi.nlm.nih.gov/protein/NP_783630.2
| 371
| 37995
| https://www.uniprot.org/uniprot/P23805.fasta
| CGN1
| 281068
| https://www.ncbi.nlm.nih.gov/gene/281068
| Reviewed: Experimental evidence at protein level
|
| conglutinin in the serum of dairy cows depends on many factors such as breeding, the
season of the year, the stage of the reproductive cycle and infection
| conglutinin in the serum of dairy cows depends on many factors such as breeding, the
season of the year, the stage of the reproductive cycle and infection
| effector molecules in innate immunity; . Conglutinin does not appear in the
serum of calves until after it has received colostrum;
then its concentration gradually increases up to the
80th week of life, when it reaches the level characteristic
for adult cattle
| presence of O-linked
glycans of β(1-3)-GalNAc and α-(2-3) linked sialic
acid type. No N-linked glycans were detected
|
|
|
|
| 1. Dec, M., & Wernicki, A. (2006). Conglutinin, CL-43 and CL-46--three bovine collectins. Polish Journal of Veterinary Sciences, 9(4), 265–275. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/17203746.
2. Andersen, O., Nielsen, E. H., Storgaard, P., Højrup, P., Friis, P., Leslie, G., & Svehag, S. E. (n.d.). Biochemical and ultrastructural studies of the C-type lectin bovine conglutinin. Journal of Structural Biology, 109(3), 201–207. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1296754.
|
| Bomi1152
| Aminopeptidase
| Bos taurus
| E1BM61
| https://www.uniprot.org/uniprot/E1BM61
| Whey, MFGM
| NP_001193254.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193254.1
| 989
| 112546
| https://www.uniprot.org/uniprot/E1BM61.fasta
| LVRN
| 525695
| https://www.ncbi.nlm.nih.gov/gene/525695
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1154
| TOG array regulator of axonemal microtubules 1
| Bos taurus
| E1BM83
| https://www.uniprot.org/uniprot/E1BM83
| Whey, Exosome
|
|
| 1766
| 193991
| https://www.uniprot.org/uniprot/E1BM83.fasta
| TOGARAM1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1155
| Prominin 2
| Bos taurus
| E1BM92
| https://www.uniprot.org/uniprot/E1BM92
| Whey, MFGM, Exosome
|
|
| 833
| 91521
| https://www.uniprot.org/uniprot/E1BM92.fasta
| PROM2
| 520936
| https://www.ncbi.nlm.nih.gov/gene/520936
| Unreveeiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1158
| DNA polymerase theta
| Bos taurus
| E1BMC0
| https://www.uniprot.org/uniprot/E1BMC0
| Whey, Exosome
|
|
| 2712
| 303315
| https://www.uniprot.org/uniprot/E1BMC0.fasta
| POLQ
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi116
| Lactotransferrin
| Bos taurus
| P24627
| http://www.uniprot.org/uniprot/P24627
| Whey
| NP_851341.1
| https://www.ncbi.nlm.nih.gov/protein/NP_851341.1
| 708
| 78056
| http://www.uniprot.org/uniprot/P24627.fasta
| LTF
| 280846
| https://www.ncbi.nlm.nih.gov/gene/280846
| Reviewed: Experimental evidence at protein level
| saliva, tears, bile/pncreatic secretions, mucosal secretions of trachea, uterus, ovaries, seminal secretion, plasma, joint fluid
| Potent iron chelator; has antimicrobial, anti-tumor, anti-allergeic, anti-inflammatory activities; promotes innante and adaptive immunity and neutrophil migration; depresses endotoxemia; acts as tumor suppressor in multiple cancers; controls oxidative cell injury; inhibits pathological development during autoimmune disorder; prevents cell apoptosis; used as chemotherapeutic agent
| Potent iron chelator; has antimicrobial, anti-tumor, anti-allergeic, anti-inflammatory activities; promotes innante and adaptive immunity and neutrophil migration; depresses endotoxemia; acts as tumor suppressor in multiple cancers; controls oxidative cell injury; inhibits pathological development during autoimmune disorder; prevents cell apoptosis; used as chemotherapeutic agent
| Highest in colustrum; has biomodulatory properties and effects nutritional value of the milk; used as active ingredients in infant formula, prebiotic drinks and immune supplements; lactoferrin through pepsin digestion produces a more potent anti-microbial peptide, lactoferrisin that reaches the gut
| Glycosylated; 5 N-linked glycans; mixtures of high mannose, complex and hybrid type; 59 different structures have been identified till date; fucosylated and sialylated; presence of unusual motifs including N,N'-diacetyllactosamine as found in bovine milk
| Glycosylation changes at multiple points of lactation; glycosylation plays a role in the protein's bioactivity and its digestion profile in the infant gut; source of novel bioactives; stimulation of bone formation; anticancer; sialylation chelates loosed bound Ca2+ and prevent bacterial colonization
| 2dxr, 2dxy, 2dyx, 2e0s, 2e1s, 2fa7, 2g93, 2h4i, 2hca, 2md1, 2md2, 2md3, 2md4, 2nuv, 2nwj, 2o1l, 2o51, 2ocu, 2p1s, 2px1, 2q8j, 2qje, 2r71, 2r9j, 2zmb, 3cfl, 3ci8, 3crb, 3e9x, 3iaz, 3ib0, 3ib1, 3ib2, 3k0v, 3kj7, 3mjn, 3mjn, 3o97, 3rgy, 3sdf, 3taj, 3tod, 3tus, 3u72, 3u8q, 3ugw, 3uk4, 3usd, 3v5a,3vdf, 4dig, 4dxu, 4fim, 4fjp, 4for, 4g2z, 4g77, 4g8h, 4grk, 4n6p, 4ned, 4oqo, 5cry, 5hbc, 1blf, 1lfc, 1nkx, 1sdx, 1y58, 2alu, 2ays, 2b65, 2doj, 2dp8, 2dqv, 2ds9, 2dsf, 2dvc, 2dwa, 2dwh, 2dwi, 2dwj
|
|
| 1. Sreedhara, A., Flengsrud, R., Prakash, V., Krowarsch, D., Langsrud, T., Kaul, P., Devold, T. G., and Vegarud, G. E. (2010) A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin. Int. Dairy J. 20, 487–494.
2. Kawakami, H., Tanaka, M., Tatsumi, K., and Dosako, S. (1992) Effects of ionic strength and pH on the thermostability of lactoferrin. Int. Dairy J. 2, 287–298.
3. Zimecki, M., Kocieba, M., Chodaczek, G., Houszka, M., and Kruzel, M. L. (2007) Lactoferrin ameliorates symptoms of experimental encephalomyelitis in Lewis rats. J. Neuroimmunol. 182, 160–166.
4. Manzoni, P., Rinaldi, M., Cattani, S., Pugni, L., Romeo, M. G., Messner, H., Stolfi, I., Decembrino, L., Laforgia, N., Vagnarelli, F., Memo, L., Bordignon, L., Saia, O. S., Maule, M., Gallo, E., Mostert, M., Magnani, C., Quercia, M., Bollani, L., Pedicino, R., Renzullo, L., Betta, P., Mosca, F., Ferrari, F., Magaldi, R., Stronati, M., Farina, D., and Italian Task Force for the Study and Prevention of Neonatal Fungal Infections, Italian Society of Neonatology. (2009) Bovine Lactoferrin Supplementation for Prevention of Late-Onset Sepsis in Very Low-Birth-Weight NeonatesA Randomized Trial JAMA 302, 1421.
5. Wang, Y.-Z., Shan, T.-Z., Xu, Z.-R., Feng, J., and Wang, Z.-Q. (2007) Effects of the lactoferrin (LF) on the growth performance, intestinal microflora and morphology of weanling pigs. Anim. Feed Sci. Technol. 135, 263–272.
6. Hua, S., Nwosu, C. C., Strum, J. S., Seipert, R. R., An, H. J., Zivkovic, A. M., German, J. B., and Lebrilla, C. B. (2012) Site-specific protein glycosylation analysis with glycan isomer differentiation. Anal. Bioanal. Chem. 403, 1291–1302.
7. Yoshida, S., Wei, Z., Shinmura, Y., and Fukunaga, N. (2000) Separation of lactoferrin-a and -b from bovine colostrum. J. Dairy Sci. 83, 2211–2215.
8. Debbabi, H., Dubarry, M., Rautureau, M., and Tomé, D. (1998) Bovine lactoferrin induces both mucosal and systemic immune response in mice. J. Dairy Res. 65, 283–293.
9. Kreuß, M., Krause, I., and Kulozik, U. (2009) Influence of glycosylation on foaming properties of bovine caseinomacropeptide. Int. Dairy J. 19, 715–720.
10. Cornish, J., Callon, K. E., Naot, D., Palmano, K. P., Banovic, T., Bava, U., Watson, M., Lin, J.-M., Tong, P. C., Chen, Q., Chan, V. A., Reid, H. E., Fazzalari, N., Baker, H. M., Baker, E. N., Haggarty, N. W., Grey, A. B., and Reid, I. R. (2004) Lactoferrin Is a Potent Regulator of Bone Cell Activity and Increases Bone Formation in Vivo. Endocrinology 145, 4366–4374.
11. Ujita, M., Furukawa, K., Aoki, N., Sato, T., Noda, A., Nakamura, R., Greenwalt, D. E., and Matsuda, T. (1993) A change in soybean agglutinin binding patterns of bovine milk fat globule membrane glycoproteins during early lactation. FEBS Lett. 332, 119–122.
12. Wang, B., Yu, B., Karim, M., Hu, H., Sun, Y., McGreevy, P., Petocz, P., Held, S., and Brand-Miller, J. (2007) Dietary sialic acid supplementation improves learning and memory in piglets. Am. J. Clin. Nutr. 85, 561–569.
13. Takimori, S., Shimaoka, H., Furukawa, J.-I., Yamashita, T., Amano, M., Fujitani, N., Takegawa, Y., Hammarström, L., Kacskovics, I., Shinohara, Y., and Nishimura, S.-I. (2011) Alteration of the N-glycome of bovine milk glycoproteins during early lactation. FEBS J. 278, 3769–3781.
14. van Leeuwen, S. S., Schoemaker, R. J. W., Timmer, C. J. A. M., Kamerling, J. P., and Dijkhuizen, L. (2012) Use of Wisteria floribunda agglutinin affinity chromatography in the structural analysis of the bovine lactoferrin N-linked glycosylation. Biochim. Biophys. Acta - Gen. Subj. 1820, 1444–1455.
15. O’Riordan, N., Gerlach, J. Q., Kilcoyne, M., O’Callaghan, J., Kane, M., Hickey, R. M., and Joshi, L. (2014) Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays. Food Chem. 165, 388–396.
16. Puddu, P., Latorre, D., Carollo, M., Catizone, A., Ricci, G., Valenti, P., and Gessani, S. (2011) Bovine lactoferrin counteracts Toll-like receptor mediated activation signals in antigen presenting cells. PLoS One 6, e22504.
17. He, Y., Lawlor, N. T., and Newburg, D. S. (2016) Human Milk Components Modulate Toll-Like Receptor-Mediated Inflammation. Adv. Nutr. 7, 102–111.
18. He, S., McEuen, A. R., Blewett, S. A., Li, P., Buckley, M. G., Leufkens, P., and Walls, A. F. (2003) The inhibition of mast cell activation by neutrophil lactoferrin: uptake by mast cells and interaction with tryptase, chymase and cathepsin G. Biochem. Pharmacol. 65, 1007–1015.
19. Schaible, U. E., Collins, H. L., Priem, F., and Kaufmann, S. H. E. (2002) Correction of the iron overload defect in beta-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis. J. Exp. Med. 196, 1507–1513.
20. Bullen, J. J., Rogers, H. J., and Leigh, L. (1972) Iron-binding proteins in milk and resistance to Escherichia coli infection in infants. Br. Med. J. 1, 69–75.
21. Reiter, B., Brock, J. H., and Steel, E. D. (1975) Inhibition of Escherichia coli by bovine colostrum and post-colostral milk. II. The bacteriostatic effect of lactoferrin on a serum susceptible and serum resistant strain of E. coli. Immunology 28, 83–95.
22. Spik, G., Cheron, A., Montreuil, J., and Dolby, J. M. (1978) Bacteriostasis of a milk-sensitive strain of Escherichia coli by immunoglobulins and iron-binding proteins in association. Immunology 35, 663–671.
23. Masson, P. L., Heremans, J. F., Prignot, J. J., and Wauters, G. (1966) Immunohistochemical localization and bacteriostatic properties of an iron-binding protein from bronchial mucus. Thorax 21, 538–544.
24. 1. Bertuccini, L., Costanzo, M., Iosi, F., Tinari, A., Terruzzi, F., Stronati, L., Aloi, M., Cucchiara, S., and Superti, F. (2014) Lactoferrin prevents invasion and inflammatory response following E. coli strain LF82 infection in experimental model of Crohn’s disease. Dig. Liver Dis. 46, 496–504.
25. Yoo, Y. C., Watanabe, S., Watanabe, R., Hata, K., Shimazaki, K., and Azuma, I. (1997) Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice. Jpn. J. Cancer Res. 88, 184–190.
26. Janssen, P. T. and van Bijsterveld, O. P. (1983) Origin and biosynthesis of human tear fluid proteins. Invest. Ophthalmol. Vis. Sci. 24, 623–630.
27. Saito, K. and Nakanuma, Y. (1992) Lactoferrin and lysozyme in the intrahepatic bile duct of normal livers and hepatolithiasis. An immunohistochemical study. J. Hepatol. 15, 147–153.
28. Varadhachary, A., Wolf, J. S., Petrak, K., O’Malley, B. W., Spadaro, M., Curcio, C., Forni, G., and Pericle, F. (2004) Oral lactoferrin inhibits growth of established tumors and potentiates conventional chemotherapy. Int. J. Cancer 111, 398–403.
29. Saito, H., Miyakawa, H., Tamura, Y., Shimamura, S., and Tomita, M. (1991) Potent Bactericidal Activity of Bovine Lactoferrin Hydrolysate Produced by Heat Treatment at Acidic pH. J. Dairy Sci. 74, 3724–3730.
30. Zhang, J., Ling, T., Wu, H., and Wang, K. (2015) Re-expression of Lactotransferrin , a candidate tumor suppressor inactivated by promoter hypermethylation, impairs the malignance of oral squamous cell carcinoma cells. J. Oral Pathol. Med. 44, 578–584.
31. Meisel H, Bockelmann W. Bioactive peptides encrypted in milk proteins: proteolytic activation and thropho-functional properties. Antonie Van Leeuwenhoek [Internet]. [cited 2019 Nov 26];76(1–4):207–15. Available from: http://www.ncbi.nlm.nih.gov/pubmed/10532380
|
| Bomi1161
| Cilia and flagella associated protein 43
| Bos taurus
| E1BMD1
| https://www.uniprot.org/uniprot/E1BMD1
| Whey
| NP_001192778.3
| https://www.ncbi.nlm.nih.gov/protein/NP_001192778
| 1665
| 192505
| https://www.uniprot.org/uniprot/E1BMD1.fasta
| CFAP43
| 518801
| https://www.ncbi.nlm.nih.gov/gene/518801
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1163
| Dynein axonemal heavy chain 5
| Bos taurus
| E1BMG2
| https://www.uniprot.org/uniprot/E1BMG2
| Whey, MFGM, Exosome
|
|
| 4610
| 528363
| https://www.uniprot.org/uniprot/E1BMG2.fasta
| DNAH5
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1165
| 10-formyltetrahydrofolate dehydrogenase
| Bos taurus
| E1BMG9
| https://www.uniprot.org/uniprot/E1BMG9
| Whey
|
|
| 902
| 98753
| https://www.uniprot.org/uniprot/E1BMG9.fasta
| ALDH1L1
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1166
| Sodium channel protein
| Bos taurus
| E1BHR8
| https://www.uniprot.org/uniprot/E1BHR8
| Whey, MFGM
| NP_001137581.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001137581.1
| 2006
| 227827
| https://www.uniprot.org/uniprot/E1BHR8.fasta
| SCN2A
| 539718
| https://www.ncbi.nlm.nih.gov/gene/539718
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1169
| Centlein
| Bos taurus
| E1BMK9
| https://www.uniprot.org/uniprot/E1BMK9
| Whey, Exosome
|
|
| 1346
| 155454
| https://www.uniprot.org/uniprot/E1BMK9.fasta
| CNTLN
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi117
| Cathepsin L1
| Bos taurus
| P25975
| https://www.uniprot.org/uniprot/P25975
| Whey
| NP_776457.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776457.1
| 334
| 37347
| https://www.uniprot.org/uniprot/P25975.fasta
| CTSL
| 281108
| https://www.ncbi.nlm.nih.gov/gene/281108
| Reviewed: Experimental evidence at protein level
| Ubiquitously expressed, highly expressed in osteoclasts;
| regulation of cell-cycle progression; proteolytic processing of the N-terminus of
the histone H3 tail; cleaves elastin; special role in bone resorption under normal and pathological
conditions
| regulation of cell-cycle progression; proteolytic processing of the N-terminus of
the histone H3 tail; cleaves elastin; special role in bone resorption under normal and pathological
conditions
|
|
|
|
|
|
| 1. Turk, B., Dolenc, I., Turk, V., & Bieth, J. G. (1993). Kinetics of the pH-induced inactivation of human cathepsin L. Biochemistry, 32(1), 375–380. https://doi.org/10.1021/bi00052a046.
2. Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., & Brömme, D. (2004). Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. The Journal of Biological Chemistry, 279(35), 36761–36770. https://doi.org/10.1074/jbc.M403986200.
3. Brömme, D., Okamoto, K., Wang, B. B., & Biroc, S. (1996). Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. The Journal of Biological Chemistry, 271(4), 2126–2132. https://doi.org/10.1074/jbc.271.4.2126.
4. Drake, F. H., Dodds, R. A., James, I. E., Connor, J. R., Debouck, C., Richardson, S., … Gowen, M. (1996). Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. The Journal of Biological Chemistry, 271(21), 12511–12516. https://doi.org/10.1074/jbc.271.21.12511.
5. Goulet, B., Baruch, A., Moon, N.-S., Poirier, M., Sansregret, L. L., Erickson, A., … Nepveu, A. (2004). A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Molecular Cell, 14(2), 207–219. https://doi.org/10.1016/s1097-2765(04)00209-6.
6. Duncan, E. M., Muratore-Schroeder, T. L., Cook, R. G., Garcia, B. A., Shabanowitz, J., Hunt, D. F., & Allis, C. D. (2008). Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell, 135(2), 284–294. https://doi.org/10.1016/j.cell.2008.09.055.
7. Ceru, S., Konjar, S., Maher, K., Repnik, U., Krizaj, I., Bencina, M., … Kopitar-Jerala, N. (2010). Stefin B interacts with histones and cathepsin L in the nucleus. The Journal of Biological Chemistry, 285(13), 10078–10086. https://doi.org/10.1074/jbc.M109.034793.
|
| Bomi1174
| SANT domain-containing protein
| Bos taurus
| E1BMQ3
| https://www.uniprot.org/uniprot/E1BMQ3
| Whey, Exosome
|
|
| 1043
| 118830
| https://www.uniprot.org/uniprot/E1BMQ3.fasta
| MIS18BP1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1177
| AP-2 complex subunit alpha
| Bos taurus
| E1BMW2
| https://www.uniprot.org/uniprot/E1BMW2
| Whey, Exosome
|
|
| 969
| 106980
| https://www.uniprot.org/uniprot/E1BMW2.fasta
| AP2A1
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1178
| Uncharacterized protein
| Bos taurus
| E1BMW9
| https://www.uniprot.org/uniprot/E1BMW9
| Whey, Exosome
| NP_001192363.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192363.1
| 322
| 34881
| https://www.uniprot.org/uniprot/E1BMW9.fasta
| PURA
| 782746
| https://www.ncbi.nlm.nih.gov/gene/782746
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi118
| Spermadhesin-1
| Bos taurus
| P29392
| https://www.uniprot.org/uniprot/P29392
| Whey
| NP_777041.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777041.1
| 134
| 15036
| https://www.uniprot.org/uniprot/P29392.fasta
| SPADH1
| 282373
| https://www.ncbi.nlm.nih.gov/gene/282373
| Reviewed: Experimental evidence at protein level
| male genital
tract of pig, horse and bulls, seminal vescicles, peripherally associated to the sperm
surface,
| multifunctional
proteins; involved in different
steps of fertilization; represent
a novel class of lectins that may be involved in
sequential steps of fertilization; stimulates progesterone secretion and growth through cell division and in bovine granulosa cells in vitro
| multifunctional
proteins; involved in different
steps of fertilization; represent
a novel class of lectins that may be involved in
sequential steps of fertilization; stimulates progesterone secretion and growth through cell division and in bovine granulosa cells in vitro
| potential protein candidate biomarkers of bovine pregnancy;
|
|
| 1SFP
|
|
| 1. Johnston, D., Malo Estepa, I., Ebhardt, H. A., Crowe, M. A., & Diskin, M. G. (2018). Differences in the bovine milk whey proteome between early pregnancy and the estrous cycle. Theriogenology, 114, 301–307. https://doi.org/10.1016/j.theriogenology.2018.04.008.
2. Einspanier, R., Krause, I., Calvete, J. J., Töfper-Petersen, E., Klostermeyer, H., & Karg, H. (1994). Bovine seminal plasma aSFP: localization of disulfide bridges and detection of three different isoelectric forms. FEBS Letters, 344(1), 61–64. https://doi.org/10.1016/0014-5793(94)00362-9.
3. Romero, A., Romão, M. J., Varela, P. F., Kölln, I., Dias, J. M., Carvalho, A. L., … Calvete, J. J. (1997). The crystal structures of two spermadhesins reveal the CUB domain fold. Nature Structural Biology, 4(10), 783–788. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/9334740.
|
| Bomi1180
| MDS1 and EVI1 complex locus
| Bos taurus
| E1BMZ2
| https://www.uniprot.org/uniprot/E1BMZ2
| Whey
|
|
| 1011
| 114040
| https://www.uniprot.org/uniprot/E1BMZ2.fasta
| MECOM
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1183
| Coiled-coil domain containing 18
| Bos taurus
| E1BN16
| https://www.uniprot.org/uniprot/E1BN16
| Whey, MFGM, Exosome
| XP_005204380.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005204380.1
| 1456
| 169858
| https://www.uniprot.org/uniprot/E1BN16.fasta
| CCDC18
| 540863
| https://www.ncbi.nlm.nih.gov/gene/540863
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1184
| Zinc finger NFX1-type containing 1
| Bos taurus
| E1BN24
| https://www.uniprot.org/uniprot/E1BN24
| Whey, Exosome
|
|
| 1918
| 219979
| https://www.uniprot.org/uniprot/E1BN24.fasta
| ZNFX1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1189
| Mitogen-activated protein kinase 8 interacting protein 3
| Bos taurus
| E1BN82
| https://www.uniprot.org/uniprot/E1BN82
| Whey
|
|
| 1324
| 145540
| https://www.uniprot.org/uniprot/E1BN82.fasta
| MAPK8IP3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi119
| Osteopontin
| Bos taurus
| P31096
| https://www.uniprot.org/uniprot/P31096
| Whey
| NP_776612.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776612.1
| 278
| 30904
| https://www.uniprot.org/uniprot/P31096.fasta
| SPP1
| 281499
| https://www.ncbi.nlm.nih.gov/gene/281499
| Reviewed: Experimental evidence at protein level
| blood, urine, seminal fluid
| Inhibition
of ectopic calcification, bone remodelling, cancer metastasis and
immune modulatory functions; act as an opsonin, as it binds directly to several bacterial
strains leading to enhanced phagocytosis by macrophages; can induce Th1 type immunity by inducing
interleukin-12 expression in macrophages
| Inhibition
of ectopic calcification, bone remodelling, cancer metastasis and
immune modulatory functions; act as an opsonin, as it binds directly to several bacterial
strains leading to enhanced phagocytosis by macrophages; can induce Th1 type immunity by inducing
interleukin-12 expression in macrophages
| OPN plays a role in the development of the
infant and could provide an important immunological signal during
development; OPN, which
possess known cytokine-like properties, was the most abundantly
expressed when compared with the expression of 240 cytokine
related genes in human milk; involved in mammary gland
development and differentiation; bind and
form soluble complexes with calcium ions which together with especially the caseins, could inhibit unintentional precipitation of
amorphous calcium phosphate in milk; act as a transporter of these immunomodulating and
antimicrobial proteins to their site of action and to protect them
from proteolysis
| Phosphorylated glycoprotein; ~25 phosphates
distributed over 36 potential sites in human milk osteopontin; ~22 phosphates
distributed over 28 potential sites in bovine milk osteopontin; Bovine milk OPN contains three
O-glycosylated threonine residues close to the integrin binding
motifs; The glycan
structures on human milk OPN have been shown to consist of large
fucosylated N-acetyllactosamine units; the carbohydrates on bovine OPN consist of a disialylated
GalNAc-galactose cores
|
|
|
|
| 1. Bautista, D. S., Saad, Z., Chambers, A. F., Tonkin, K. S., O’Malley, F. P., Singhal, H., Tokmakejian, S., Bramwell, V., and Harris, J. F. (1996) Quantification of osteopontin in human plasma with an ELISA: basal levels in pre- and postmenopausal women. Clin. Biochem. 29, 231–239.
2. Senger, D. R., Perruzzi, C. A., Papadopoulos, A., and Tenen, D. G. (1989) Purification of a human milk protein closely similar to tumor-secreted phosphoproteins and osteopontin. Biochim. Biophys. Acta 996, 43–48.
3. Hoyer, J. R., Otvos, L., and Urge, L. (1995) Osteopontin in urinary stone formation. Ann. N. Y. Acad. Sci. 760, 257–265.
4. Cancel, A. M., Chapman, D. A., and Killian, G. J. (1999) Osteopontin localization in the Holstein bull reproductive tract. Biol. Reprod. 60, 454–460.
5. Anborgh, P. H., Mutrie, J. C., Tuck, A. B., and Chambers, A. F. (2011) Pre- and post-translational regulation of osteopontin in cancer. J. Cell Commun. Signal. 5, 111–122.
6. Schack, L., Stapulionis, R., Christensen, B., Kofod-Olsen, E., Skov Sorensen, U. B., Vorup-Jensen, T., Sorensen, E. S., and Hollsberg, P. (2009) Osteopontin Enhances Phagocytosis through a Novel Osteopontin Receptor, the X 2 Integrin. J. Immunol. 182, 6943–6950.
7. Schack, L., Stapulionis, R., Christensen, B., Kofod-Olsen, E., Skov Sorensen, U. B., Vorup-Jensen, T., Sorensen, E. S., and Hollsberg, P. (2009) Osteopontin Enhances Phagocytosis through a Novel Osteopontin Receptor, the X 2 Integrin. J. Immunol. 182, 6943–6950.
8. Chatterton, D. E. ., Rasmussen, J. ., Heegaard, C. ., Sørensen, E. ., and Petersen, T. . (2004) In vitro digestion of novel milk protein ingredients for use in infant formulas: Research on biological functions. Trends Food Sci. Technol. 15, 373–383.
9. Ashkar, S., Weber, G. F., Panoutsakopoulou, V., Sanchirico, M. E., Jansson, M., Zawaideh, S., Rittling, S. R., Denhardt, D. T., Glimcher, M. J., and Cantor, H. (2000) Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. Science 287, 860–864.
10. Agnihotri, R., Crawford, H. C., Haro, H., Matrisian, L. M., Havrda, M. C., and Liaw, L. (2001) Osteopontin, a Novel Substrate for Matrix Metalloproteinase-3 (Stromelysin-1) and Matrix Metalloproteinase-7 (Matrilysin). J. Biol. Chem. 276, 28261–28267.
11. Christensen, B., Kläning, E., Nielsen, M. S., Andersen, M. H., and Sørensen, E. S. (2012) C-terminal modification of osteopontin inhibits interaction with the αVβ3-integrin. J. Biol. Chem. 287, 3788–3797.
12. Boskey, A. L., Christensen, B., Taleb, H., and Sørensen, E. S. (2012) Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth. Biochem. Biophys. Res. Commun. 419, 333–338.
13. Sørensen, E. S., Petersen, T. E., and Højrup, P. (1995) Posttranslational modifications of bovine osteopontin: Identification of twenty-eight phosphorylation and three O -glycosylation sites. Protein Sci. 4, 2040–2049.
|
| Bomi1194
| Kin17 DNA and RNA binding protein
| Bos taurus
| E1BND1
| https://www.uniprot.org/uniprot/E1BND1
| Whey
|
|
| 392
| 45218
| https://www.uniprot.org/uniprot/E1BND1.fasta
| KIN
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1195
| LPS responsive beige-like anchor protein
| Bos taurus
| E1BND6
| https://www.uniprot.org/uniprot/E1BND6
| Whey, Exosome
|
|
| 2845
| 316088
| https://www.uniprot.org/uniprot/E1BND6.fasta
| LRBA
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1196
| PTPRF interacting protein alpha 2
| Bos taurus
| E1BND7
| https://www.uniprot.org/uniprot/E1BND7
| Whey
|
|
| 1237
| 141066
| https://www.uniprot.org/uniprot/E1BND7.fasta
| PPFIA2
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi12
| Transforming growth factor beta-2
| Bos taurus
| P21214
| https://www.uniprot.org/uniprot/P21214
| Whey
| NP_001106723.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001106723.1
| 414
| 47692
| https://www.uniprot.org/uniprot/P21214.fasta
| TGFB2
| 534069
| https://www.ncbi.nlm.nih.gov/gene/534069
| Reviewed: Experimental evidence at protein level
|
| maintenance of metabolic homeostasis in the bone tissue; leading role in the fracture healing process; induces chondrogenesis
and osteogenesis; potent inhibitor of
intestinal epithelial cell proliferation
| maintenance of metabolic homeostasis in the bone tissue; leading role in the fracture healing process; induces chondrogenesis
and osteogenesis; potent inhibitor of
intestinal epithelial cell proliferation
| have inhibitory
effects on [3H]thymidine uptake by concanavalin-A-stimulated
thymocytes; found in milk MFG and has immunosuppressive effects; important roles in the regulation of
growth and differentiation processes in the foetus, neonate
and adult and leads us to speculate on the function of these
molecules in milk; regulate growth and differentiation of
the intestinal epithelia from the lumenal surface of the neonatal
gut in the early days following birth
|
|
|
| TGFß2 RNAand TGFß3 RNA levels are the highest on the
7th day of the fracture
|
| 1. Daopin, S., Piez, K. A., Ogawa, Y., & Davies, D. R. (1992). Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. Science (New York, N.Y.), 257(5068), 369–373. https://doi.org/10.1126/science.1631557.
2. Joyce, M. E., Roberts, A. B., Sporn, M. B., & Bolander, M. E. (1990). Transforming growth factor-beta and the initiation of chondrogenesis and osteogenesis in the rat femur. The Journal of Cell Biology, 110(6), 2195–2207. https://doi.org/10.1083/jcb.110.6.2195.
3. Cho, T.-J., Gerstenfeld, L. C., & Einhorn, T. A. (2002). Differential temporal expression of members of the transforming growth factor beta superfamily during murine fracture healing. Journal of Bone and Mineral Research : The Official Journal of the American Society for Bone and Mineral Research, 17(3), 513–520. https://doi.org/10.1359/jbmr.2002.17.3.513.
4. Cox, D. A., & Bürk, R. R. (1991). Isolation and characterisation of milk growth factor, a transforming-growth-factor-beta 2-related polypeptide, from bovine milk. European Journal of Biochemistry, 197(2), 353–358. https://doi.org/10.1111/j.1432-1033.1991.tb15918.x.
5. Javelaud, D., & Mauviel, A. (2004). Mammalian transforming growth factor-betas: Smad signaling and physio-pathological roles. The International Journal of Biochemistry & Cell Biology, 36(7), 1161–1165. https://doi.org/10.1016/S1357-2725(03)00255-3
|
| Bomi120
| Cathelicidin-4
| Bos taurus
| P33046
| https://www.uniprot.org/uniprot/P33046
| Whey
| NP_777252.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777252.1
| 144
| 16479
| https://www.uniprot.org/uniprot/P33046.fasta
| CATHL4
| 282166
| https://www.ncbi.nlm.nih.gov/gene/282166
| Reviewed: Experimental evidence at protein level
|
| smallest natural bovine
cathelicidin; intermediate antibacterial activity with
minimum inhibitory concentrations; inhibitory activity against P.
aeruginosa biofilm formation at 16 μg/mL; anti-endotoxin activities, including inhibition
of LPS-induced cytokine synthesis in leukocytes; At high concentrations, indolicidin becomes
membranolytic, translocating across mammalian membranes to interact
with internal cellular targets; potent
fungicidal activity, including against C. neoformans, C. albicans;
| smallest natural bovine
cathelicidin; intermediate antibacterial activity with
minimum inhibitory concentrations; inhibitory activity against P.
aeruginosa biofilm formation at 16 μg/mL; anti-endotoxin activities, including inhibition
of LPS-induced cytokine synthesis in leukocytes; At high concentrations, indolicidin becomes
membranolytic, translocating across mammalian membranes to interact
with internal cellular targets; potent
fungicidal activity, including against C. neoformans, C. albicans;
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
| 1G89, 1G8C, 1HR1, 1QX9, 1QXQ
|
|
| 1. Falla, T. J., Karunaratne, D. N., and Hancock, R. E. (1996) Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271, 19298–19303.
2. Pompilio, A., Scocchi, M., Pomponio, S., Guida, F., Di Primio, A., Fiscarelli, E., Gennaro, R., and Di Bonaventura, G. (2011) Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients. Peptides 32, 1807–1814.
3. Sahoo, B. R. and Fujiwara, T. (2016) Membrane Mediated Antimicrobial and Antitumor Activity of Cathelicidin 6: Structural Insights from Molecular Dynamics Simulation on Multi-Microsecond Scale. PLoS One 11, e0158702.
4. Das, H., Sharma, B., and Kumar, A. (2006) Cloning and characterization of novel cathelicidin cDNA sequence of Bubalus bubalis homologous to Bos taurus cathelicidin-4. DNA Seq. 17, 407–414.
5. Falla, T. J., Karunaratne, D. N., and Hancock, R. E. (1996) Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271, 19298–19303.
6. Bowdish, D. M. E., Davidson, D. J., Scott, M. G., and Hancock, R. E. W. (2005) Immunomodulatory Activities of Small Host Defense Peptides. Antimicrob. Agents Chemother. 49, 1727–1732.
7. Benincasa, M., Scocchi, M., Pacor, S., Tossi, A., Nobili, D., Basaglia, G., Busetti, M., and Gennaro, R. (2006) Fungicidal activity of five cathelicidin peptides against clinically isolated yeasts. J. Antimicrob. Chemother. 58, 950–959
|
| Bomi1203
| Polybromo 1
| Bos taurus
| E1BNH8
| https://www.uniprot.org/uniprot/E1BNH8
| Whey, MFGM
|
|
| 1688
| 192667
| https://www.uniprot.org/uniprot/E1BNH8.fasta
| PBRM1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1206
| Protease, serine, 22-like
| Bos taurus
| E1BNJ9
| https://www.uniprot.org/uniprot/E1BNJ9
| Whey
|
|
| 296
| 32255
| https://www.uniprot.org/uniprot/E1BNJ9.fasta
| PRSS22
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1207
| Zinc finger protein 142
| Bos taurus
| E1BNL0
| https://www.uniprot.org/uniprot/E1BNL0
| Whey, MFGM, Exosome
| XP_002685618.2
| https://www.ncbi.nlm.nih.gov/protein/XP_002685618.2
| 1838
| 204177
| https://www.uniprot.org/uniprot/E1BNL0.fasta
| ZNF142
| 511573
| https://www.ncbi.nlm.nih.gov/gene/511573
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1208
| Integrin subunit alpha 8
| Bos taurus
| E1BNM2
| https://www.uniprot.org/uniprot/E1BNM2
| Whey
|
|
| 1012
| 111654
| https://www.uniprot.org/uniprot/E1BNM2.fasta
| ITGA8
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1209
| Kinesin family member 27
| Bos taurus
| E1BNN5
| https://www.uniprot.org/uniprot/E1BNN5
| Whey
|
|
| 1395
| 159861
| https://www.uniprot.org/uniprot/E1BNN5.fasta
| KIF27
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi121
| Alpha-1-antiproteinase
| Bos taurus
| P34955
| https://www.uniprot.org/uniprot/P34955
| Whey
| NP_776307.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776307.1
| 416
| 46104
| https://www.uniprot.org/uniprot/P34955.fasta
| SERPINA1
| 280699
| https://www.ncbi.nlm.nih.gov/gene/280699
| Reviewed: Experimental evidence at protein level
| saliva, tears, breast milk, urine, semen, bronchoalveolar lavage fluid
| serine protease inhibitor; major anti-elastase of the
lower respiratory tract; modulate both
infl ammation and apoptosis;
| serine protease inhibitor; major anti-elastase of the
lower respiratory tract; modulate both
infl ammation and apoptosis;
| Acute phase proteins; elevated levels in milk during subclinical mastitis due to bacterial inection
| glycosylation at three distinct asparagine residues; These asparagine-linked side chains are composed of
N-acetylglucosamine, mannose, galactose, and sialic acid arranged as a core with
two to three branching “antennae”
| help maintain solubility and
allow attachment of protein-processing enzymes; contribute to the antiinflammatory capacity of the protein through negative regulation of IL-8-induced
neutrophil chemotaxis
|
|
|
| 1. Guha, A., Guha, R., and Gera, S. (2013) Comparison of α1-Antitrypsin, α1-Acid Glycoprotein, Fibrinogen and NOx as Indicator of Subclinical Mastitis in Riverine Buffalo (Bubalus bubalis). Asian-Australasian J. Anim. Sci. 26, 788–794.
2. Huber, R. and Carrell, R. W. (1989) Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951–8966.
3. Burnouf, T., Constans, J., Clerc, A., Descamps, J., Martinache, L., and Goudemand, M. (1987) Biochemical and Biological Properties of an α 1 -Antitrypsin Concentrate. Vox Sang. 52, 291–297.
4. Ekeowa, U. I., Gooptu, B., Belorgey, D., Hägglöf, P., Karlsson-Li, S., Miranda, E., Pérez, J., MacLeod, I., Kroger, H., Marciniak, S. J., Crowther, D. C., and Lomas, D. A. (2009) α 1 -Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies. Clin. Sci. 116, 837–850.
5. Gadek, J. E., Fells, G. A., Zimmerman, R. L., Rennard, S. I., and Crystal, R. G. (1981) Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema. J. Clin. Invest. 68, 889–898.
6. Petrache, I., Fijalkowska, I., Medler, T. R., Skirball, J., Cruz, P., Zhen, L., Petrache, H. I., Flotte, T. R., and Tuder, R. M. (2006) alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis. Am. J. Pathol. 169, 1155–1166.
7. Berman, M. B., Barber, J. C., Talamo, R. C., and Langley, C. E. (1973) Corneal ulceration and the serum antiproteases. I. Alpha 1-antitrypsin. Invest. Ophthalmol. 12, 759–770.
8. Poortmans, J. and Jeanloz, R. W. (1968) Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise. J. Clin. Invest. 47, 386–393.
9. American Thoracic Society and European Respiratory Society. (2003) American Thoracic Society/European Respiratory Society Statement. Am. J. Respir. Crit. Care Med. 168, 818–900.
10. Hu, C. and Perlmutter, D. H. (2002) Cell-specific involvement of HNF-1β in α 1 -antitrypsin gene expression in human respiratory epithelial cells. Am. J. Physiol. Cell. Mol. Physiol. 282, L757–L765.
11. Brantly, M., Nukiwa, T., and Crystal, R. G. (1988) Molecular basis of alpha-1-antitrypsin deficiency. Am. J. Med. 84, 13–31.
12. Sifers, R. N. (2010) Intracellular Processing of 1-Antitrypsin. Proc. Am. Thorac. Soc. 7, 376–380.
13. Bergin, D. A., Reeves, E. P., Meleady, P., Henry, M., McElvaney, O. J., Carroll, T. P., Condron, C., Chotirmall, S. H., Clynes, M., O’Neill, S. J., and McElvaney, N. G. (2010) α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8. J. Clin. Invest. 120, 4236–4250.
|
| Bomi1213
| Apolipoprotein B
| Bos taurus
| E1BNR0
| https://www.uniprot.org/uniprot/E1BNR0
| Whey, MFGM, Exosome
|
|
| 4567
| 515516
| https://www.uniprot.org/uniprot/E1BNR0.fasta
| APOB
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1216
| L-lactate dehydrogenase
| Bos taurus
| E1BNS9
| https://www.uniprot.org/uniprot/E1BNS9
| Whey, Exosome
| NP_001106720.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001106720.1
| 332
| 36015
| https://www.uniprot.org/uniprot/E1BNS9.fasta
| LDHC
| 537256
| https://www.ncbi.nlm.nih.gov/gene/537256
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi122
| Serum amyloid A protein
| Bos taurus
| P35541
| https://www.uniprot.org/uniprot/P35541
| Whey
| NP_001068728.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068728.1
| 130
| 14516
| https://www.uniprot.org/uniprot/P35541.fasta
| SAA1
| 506412
| https://www.ncbi.nlm.nih.gov/gene/506412
| Reviewed: Experimental evidence at protein level
|
| Acute phase proteins; role in increased
cholesterol efflux from macrophages at sites of tissue
injury; pro-inflammatory
and anti-inflammatory; suggested roles of alkaline SAA is upregulation
of mucin expression in newborn calf intestinal mucosa and
enhanced mucosal immunity of the newborn
| Acute phase proteins; role in increased
cholesterol efflux from macrophages at sites of tissue
injury; pro-inflammatory
and anti-inflammatory; suggested roles of alkaline SAA is upregulation
of mucin expression in newborn calf intestinal mucosa and
enhanced mucosal immunity of the newborn
| markers of subclinical
inflammation in ruminants; two acidic serum SAA isoforms (pI 5.5 and 4.5) in the subclinical
mastitis;
|
|
|
|
|
| 1. Kovačević-Filipović, M., Ilić, V., Vujčić, Z., Dojnov, B., Stevanov-Pavlović, M., Mijačević, Z., and Božić, T. (2012) Serum amyloid A isoforms in serum and milk from cows with Staphylococcus aureus subclinical mastitis. Vet. Immunol. Immunopathol. 145, 120–128.
2. Cabana, V. G., Siegel, J. N., and Sabesin, S. M. (1989) Effects of the acute phase response on the concentration and density distribution of plasma lipids and apolipoproteins. J. Lipid Res. 30, 39–49.
3. Uhlar, C. M. and Whitehead, A. S. (1999) Serum amyloid A, the major vertebrate acute-phase reactant. Eur. J. Biochem. 265, 501–523.
4. Eckersall, P. D., Young, F. J., McComb, C., Hogarth, C. J., Safi, S., Weber, A., McDonald, T., Nolan, A. M., and Fitzpatrick, J. L. (2001) Acute phase proteins in serum and milk from dairy cows with clinical mastitis. Vet. Rec. 148, 35–41.
5. Jacobsen, S., Andersen, P. H., Toelboell, T., and Heegaard, P. M. H. (2004) Dose Dependency and Individual Variability of the Lipopolysaccharide-Induced Bovine Acute Phase Protein Response. J. Dairy Sci. 87, 3330–3339.
6. McDonald, T. L., Larson, M. A., Mack, D. R., and Weber, A. (2001) Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum. Vet. Immunol. Immunopathol. 83, 203–211.
|
| Bomi1221
| Family with sequence similarity 13 member B
| Bos taurus
| E1BNY2
| https://www.uniprot.org/uniprot/E1BNY2
| Whey
|
|
| 916
| 104494
| https://www.uniprot.org/uniprot/E1BNY2.fasta
| FAM13B
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1222
| General transcription factor IIIC subunit 1
| Bos taurus
| E1BNY8
| https://www.uniprot.org/uniprot/E1BNY8
| Whey, Exosome
|
|
| 2096
| 236187
| https://www.uniprot.org/uniprot/E1BNY8.fasta
| GTF3C1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1223
| HECT, UBA and WWE domain containing 1, E3 ubiquitin protein ligase
| Bos taurus
| E1BNY9
| https://www.uniprot.org/uniprot/E1BNY9
| Whey, Exosome
| NP_001103474.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001103474.1
| 4375
| 482191
| https://www.uniprot.org/uniprot/E1BNY9.fasta
| HUWE1
| 511826
| https://www.ncbi.nlm.nih.gov/gene/511826
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1224
| Myosin IIIA
| Bos taurus
| E1BP01
| https://www.uniprot.org/uniprot/E1BP01
| Whey
| XP_015329509.1
| https://www.ncbi.nlm.nih.gov/protein/XP_015329509.1
| 1623
| 186059
| https://www.uniprot.org/uniprot/E1BP01.fasta
| MYO3A
| 535824
| https://www.ncbi.nlm.nih.gov/gene/535824
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1225
| Slit guidance ligand 1
| Bos taurus
| E1BP10
| https://www.uniprot.org/uniprot/E1BP10
| Whey
| XP_002698459.1
| https://www.ncbi.nlm.nih.gov/protein/XP_002698459.1
| 1534
| 167504
| https://www.uniprot.org/uniprot/E1BP10.fasta
| SLIT1
| 510761
| https://www.ncbi.nlm.nih.gov/gene/510761
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1226
| Serine/threonine-protein kinase PLK
| Bos taurus
| E1BP17
| https://www.uniprot.org/uniprot/E1BP17
| Whey
| NP_001179174.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179174.1
| 685
| 78260
| https://www.uniprot.org/uniprot/E1BP17.fasta
| PLK2
| 539449
| https://www.ncbi.nlm.nih.gov/gene/539449
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi123
| Collectin-43
| Bos taurus
| P42916
| https://www.uniprot.org/uniprot/P42916
| Whey
| NP_001002237.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001002237.1
| 321
| 33616
| https://www.uniprot.org/uniprot/P42916.fasta
| CL43
| 431784
| https://www.ncbi.nlm.nih.gov/gene/431784
| Reviewed: Experimental evidence at protein level
|
| collagen containing C type lectin; CL-43 is synthesized only in the bovine liver; involved in the innate immune defense; bind to microbial surface carbohydrates
inducing aggregation and, thereby, impeding infectivity; binds to the
collectin receptor (C1qR) localized on many types of cells identified as a surface variant of calreticulin; show antiviral activities towards influenza A virus and rotaviruses ; displays protective activity against bacterial infections
| collagen containing C type lectin; CL-43 is synthesized only in the bovine liver; involved in the innate immune defense; bind to microbial surface carbohydrates
inducing aggregation and, thereby, impeding infectivity; binds to the
collectin receptor (C1qR) localized on many types of cells identified as a surface variant of calreticulin; show antiviral activities towards influenza A virus and rotaviruses ; displays protective activity against bacterial infections
| Antimicrobial proteins - exclusively detected
in the colostrum fluid phase
| CL -43 does
not posses N-linked carbohydrate, but it contains hydroxylysine
residues in the collagen-like region that
are potential O-glycosylation sites
|
|
|
|
| 1. Nissen, A., Andersen, P. H., Bendixen, E., Ingvartsen, K. L., and Røntved, C. M. (2017) Colostrum and milk protein rankings and ratios of importance to neonatal calf health using a proteomics approach. J. Dairy Sci. 100, 2711–2728.
2. Lu, J. (1997) Collectins: Collectors of microorganisms for the innate immune system. BioEssays 19, 509–518.
3. Hansen, S., Holm, D., Moeller, V., Vitved, L., Bendixen, C., Reid, K. B. M., Skjoedt, K., and Holmskov, U. (2002) CL-46, a novel collectin highly expressed in bovine thymus and liver. J. Immunol. 169, 5726–5734.
4. Holmskov, U., Laursen, S. B., Malhotra, R., Wiedemann, H., Timpl, R., Stuart, G. R., Tornøe, I., Madsen, P. S., Reid, K. B., and Jensenius, J. C. (1995) Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Biochem. J. 305 ( Pt 3), 889–896.
5. Lim, B. L., Willis, A. C., Reid, K. B., Lu, J., Laursen, S. B., Jensenius, J. C., and Holmskov, U. (1994) Primary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-D. J. Biol. Chem. 269, 11820–11824.
6. Haurum, J. S., Thiel, S., Haagsman, H. P., Laursen, S. B., Larsen, B., and Jensenius, J. C. (1993) Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: mannan-binding protein and conglutinin. Biochem. J. 293 ( Pt 3), 873–878.
7. Holmskov, U., Teisner, B., Willis, A. C., Reid, K. B., and Jensenius, J. C. (1993) Purification and characterization of a bovine serum lectin (CL-43) with structural homology to conglutinin and SP-D and carbohydrate specificity similar to mannan-binding protein. J. Biol. Chem. 268, 10120–10125.
8. Loveless, R. W., Holmskov, U., and Feizi, T. (1995) Collectin-43 is a serum lectin with a distinct pattern of carbohydrate recognition. Immunology 85, 651–659.
|
| Bomi124
| Vimentin
| Bos taurus
| P48616
| https://www.uniprot.org/uniprot/P48616
| Whey
| NP_776394.2
| https://www.ncbi.nlm.nih.gov/protein/NP_776394.2
| 466
| 53728
| https://www.uniprot.org/uniprot/P48616.fasta
| VIM
| 280955
| https://www.ncbi.nlm.nih.gov/gene/280955
| Reviewed: Experimental evidence at protein level
|
| Vimentin is a cytoskeletal type III intermediate filament protein; contributes to epithelial to mesenchymal
transition progression; provides mechanical stability; regulation of signalling, protein trafficking and
gene expression;
| Vimentin is a cytoskeletal type III intermediate filament protein; contributes to epithelial to mesenchymal
transition progression; provides mechanical stability; regulation of signalling, protein trafficking and
gene expression;
| Role in mammary gland development; mammary gland development is delayed in the absence of vimentin;
| Sumoylation by ubc9; glycosylation by OGT, O-linked β-N-acetylglucosamine; ADP ribosylation by ADP-ribosyl transferase SpyA; numerous phosphorylation sites
| phosphorylation is strongly associated with promoting cell migration; phosphorylation induces interaction with 14-3-3 which influences cell growth and tumorigenesis, autophagy and promotes Akt-mediated tumorigenesisl phosphorylation sites appear to promote its pro-migratory function; late M phase phosphorylation was altered with increased GlcNAcylation in vimentin
|
|
|
| 1. Ku, N.-O., Michie, S., Resurreccion, E. Z., Broome, R. L., & Omary, M. B. (2002). Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression. Proceedings of the National Academy of Sciences of the United States of America, 99(7), 4373–4378. https://doi.org/10.1073/pnas.072624299.
2. Kim, S., Wong, P., & Coulombe, P. A. (2006). A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature, 441(7091), 362–365. https://doi.org/10.1038/nature04659.
3. Hyder, C. L., Pallari, H.-M., Kochin, V., & Eriksson, J. E. (2008). Providing cellular signposts--post-translational modifications of intermediate filaments. FEBS Letters, 582(14), 2140–2148. https://doi.org/10.1016/j.febslet.2008.04.064.
4. Peuhu, E., Virtakoivu, R., Mai, A., Wärri, A., & Ivaska, J. (2017). Epithelial vimentin plays a functional role in mammary gland development. Development (Cambridge, England), 144(22), 4103–4113. https://doi.org/10.1242/dev.154229.
5. Premchandar, A., Mücke, N., Poznański, J., Wedig, T., Kaus-Drobek, M., Herrmann, H., & Dadlez, M. (2016). Structural Dynamics of the Vimentin Coiled-coil Contact Regions Involved in Filament Assembly as Revealed by Hydrogen-Deuterium Exchange. The Journal of Biological Chemistry, 291(48), 24931–24950. https://doi.org/10.1074/jbc.M116.748145.
|
| Bomi1241
| Coiled-coil domain containing 81
| Bos taurus
| E1BPJ2
| https://www.uniprot.org/uniprot/E1BPJ2
| Whey
|
|
| 590
| 69419
| https://www.uniprot.org/uniprot/E1BPJ2.fasta
| CCDC81
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1244
| ATP binding cassette subfamily B member 7
| Bos taurus
| E1BPL3
| https://www.uniprot.org/uniprot/E1BPL3
| Whey, MFGM, Exosome
| NP_001179712.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001179712
| 752
| 82928
| https://www.uniprot.org/uniprot/E1BPL3.fasta
| ABCB7
| 533669
| https://www.ncbi.nlm.nih.gov/gene/533669
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1247
| Chromodomain helicase DNA binding protein 7
| Bos taurus
| E1BPM4
| https://www.uniprot.org/uniprot/E1BPM4
| Whey, Exosome
|
|
| 2786
| 310383
| https://www.uniprot.org/uniprot/E1BPM4.fasta
| CHD7
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi125
| Calreticulin
| Bos taurus
| P52193
| https://www.uniprot.org/uniprot/P52193
| Whey
| NP_776425.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776425.1
| 417
| 48039
| https://www.uniprot.org/uniprot/P52193.fasta
| CALR
| 281036
| https://www.ncbi.nlm.nih.gov/gene/281036
| Reviewed: Experimental evidence at protein level
|
| unique ER luminal resident protein; affects many cellular functions, both in the ER
lumen and outside of the ER environment ; performs two major functions: chaperoning and
regulation of Ca2+ homoeostasis; highly versatile
lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors,
integrins and transporters; affects intracellular
Ca2+ homoeostasis by modulation of ER Ca2+ storage and transport;
| unique ER luminal resident protein; affects many cellular functions, both in the ER
lumen and outside of the ER environment ; performs two major functions: chaperoning and
regulation of Ca2+ homoeostasis; highly versatile
lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors,
integrins and transporters; affects intracellular
Ca2+ homoeostasis by modulation of ER Ca2+ storage and transport;
| Associated with lipid droplets in milk as found in rat; calcium binding protein in milk
| Depending on species, calreticulin may have one or
more potential N-linked glycosylation sites; The
glycosylation pattern of the protein seems to be heterogeneous
and does not appear to be a conserved property of the protein.
The glycosylation of calreticulin is more common in plants than
in animal cells; bovine liver calreticulin appears to be glycosylated with two potential N-linked glycosylation sites; carbohydrate composition, GlcNac2Man4 -9 with
GlcNAc2Man5 being most abundant in bovine brain calreticulum; rat liver protein is glycosylated with complex hybrid type of oligosaccharide with a
terminal galactose residue
| glycosylation is species specific and ppossibly a tissue-specific event, and may not be involved directly
in its function.
| _
|
|
| 1. Matsuoka, K., Seta, K., Yamakawa, Y., Okuyama, T., Shinoda, T., and Isobe, T. (1994) Covalent structure of bovine brain calreticulin. Biochem. J. 298 ( Pt 2), 435–442.
2. Navazio, L., Baldan, B., Mariani, P., Gerwig, G. J., and Vliegenthart, J. F. (1996) Primary structure of the N-linked carbohydrate chains of Calreticulin from spinach leaves. Glycoconj. J. 13, 977–983.
3. Ostwald, T. J. and MacLennan, D. H. (1974) Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J. Biol. Chem. 249, 974–979.
4. Fliegel, L., Burns, K., MacLennan, D. H., Reithmeier, R. A., and Michalak, M. (1989) Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 264, 21522–21528.
5. Smith, M. J. and Koch, G. L. (1989) Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J. 8, 3581–3586.
6. Lewis, M. J., Mazzarella, R. A., and Green, M. (1985) Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes. J. Biol. Chem. 260, 3050–3057.
7. Ghosal, D., Shappell, N. W., and Keenan, T. W. (1994) Endoplasmic reticulum lumenal proteins of rat mammary gland. Potential involvement in lipid droplet assembly during lactation. Biochim. Biophys. Acta 1200, 175–181
|
| Bomi1256
| Zinc finger homeobox 3
| Bos taurus
| E1BPV9
| https://www.uniprot.org/uniprot/E1BPV9
| Whey, Exosome
|
|
| 3704
| 403728
| https://www.uniprot.org/uniprot/E1BPV9.fasta
| ZFHX3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1259
| Vacuolar protein sorting 13 homolog C
| Bos taurus
| E1BPX1
| https://www.uniprot.org/uniprot/E1BPX1
| Whey, MFGM, Exosome
|
|
| 3735
| 421253
| https://www.uniprot.org/uniprot/E1BPX1.fasta
| VPS13C
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi126
| Cathelicidin-6
| Bos taurus
| P54228
| https://www.uniprot.org/uniprot/P54228
| Whey
| NP_777257.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777257.1
| 158
| 17852
| https://www.uniprot.org/uniprot/P54228.fasta
| CATHL6
| 317651
| https://www.ncbi.nlm.nih.gov/gene/317651
| Reviewed: Experimental evidence at protein level
|
| Scrambled BMAP–27 has reduced
antimicrobial action against S. aureus, S. uberis and E. coli compared
with unmodified BMAP-27, confirming the specificity of this
peptide; Scrambled BMAP-27 did not retain its original conformation,
but had the same net charge (+10), indicating that structure
is significant to maintaining its antimicrobial activity; has immunomodulatory roles desirable for treatment
of infectious disorders; reduces cytotoxicity of mammalian cells and
inhibit-LPS induced TNF-α secretion;
| Scrambled BMAP–27 has reduced
antimicrobial action against S. aureus, S. uberis and E. coli compared
with unmodified BMAP-27, confirming the specificity of this
peptide; Scrambled BMAP-27 did not retain its original conformation,
but had the same net charge (+10), indicating that structure
is significant to maintaining its antimicrobial activity; has immunomodulatory roles desirable for treatment
of infectious disorders; reduces cytotoxicity of mammalian cells and
inhibit-LPS induced TNF-α secretion;
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
| 2KET
|
|
| 1. Baumann, A., Kiener, M. S., Haigh, B., Perreten, V., and Summerfield, A. (2017) Differential Ability of Bovine Antimicrobial Cathelicidins to Mediate Nucleic Acid Sensing by Epithelial Cells. Front. Immunol. 8, 59.
2. Mookherjee, N., Wilson, H. L., Doria, S., Popowych, Y., Falsafi, R., Yu, J. J., Li, Y., Veatch, S., Roche, F. M., Brown, K. L., Brinkman, F. S. L., Hokamp, K., Potter, A., Babiuk, L. A., Griebel, P. J., and Hancock, R. E. W. (2006) Bovine and human cathelicidin cationic host defense peptides similarly suppress transcriptional responses to bacterial lipopolysaccharide. J. Leukoc. Biol. 80, 1563–1574.
3. Haines, L. R., Thomas, J. M., Jackson, A. M., Eyford, B. A., Razavi, M., Watson, C. N., Gowen, B., Hancock, R. E. W., and Pearson, T. W. (2009) Killing of Trypanosomatid Parasites by a Modified Bovine Host Defense Peptide, BMAP-18. PLoS Negl. Trop. Dis. 3, e373.
|
| Bomi1260
| Myosin heavy chain 7B
| Bos taurus
| E1BPX8
| https://www.uniprot.org/uniprot/E1BPX8
| Whey, Exosome
|
|
| 1928
| 219935
| https://www.uniprot.org/uniprot/E1BPX8.fasta
| MYH7B
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1261
| REV3 like, DNA directed polymerase zeta catalytic subunit
| Bos taurus
| E1BPY8
| https://www.uniprot.org/uniprot/E1BPY8
| Whey, MFGM
|
|
| 3133
| 353091
| https://www.uniprot.org/uniprot/E1BPY8.fasta
| REV3L
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1263
| Cytoplasmic linker associated protein 2
| Bos taurus
| E1BQ15
| https://www.uniprot.org/uniprot/E1BQ15
| Whey, Exosome
| NP_001178130.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001178130.2
| 1514
| 165785
| https://www.uniprot.org/uniprot/E1BQ15.fasta
| CLASP2
| 531418
| https://www.ncbi.nlm.nih.gov/gene/531418
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1269
| CAP-Gly domain containing linker protein 1
| Bos taurus
| E3W9A2
| https://www.uniprot.org/uniprot/E3W9A2
| Whey, Exosome
| NP_001179752.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179752.1
| 1427
| 160624
| https://www.uniprot.org/uniprot/E3W9A2.fasta
| CLIP1
| 534624
| https://www.ncbi.nlm.nih.gov/gene/534624
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi127
| Cathelicidin-5
| Bos taurus
| P54229
| https://www.uniprot.org/uniprot/P54229
| Whey
| NP_776935.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776935.1
| 159
| 17616
| https://www.uniprot.org/uniprot/P54229.fasta
| CATHL5
| 282167
| https://www.ncbi.nlm.nih.gov/gene/282167
| Reviewed: Experimental evidence at protein level
|
| the effect
of BMAP-28 on S. aureus may be complex and include promoting
bacterial pathogenesis; increased
adherence of S. aureus to host fibronectin, collagen type I and collagen
type IV; spirochetes are susceptible to BMAP-28; antiparasitic activity against two strains
of L. major; caused greater inhibition of release of lipoteichoic acid
(LTA)-induced TNF-α, IL-6 and nitric oxide from Gram-positive bacteria; can induce immunomodulatory effects on leukocytes depending
on the pathogen and surrounding cytokine milieu
| the effect
of BMAP-28 on S. aureus may be complex and include promoting
bacterial pathogenesis; increased
adherence of S. aureus to host fibronectin, collagen type I and collagen
type IV; spirochetes are susceptible to BMAP-28; antiparasitic activity against two strains
of L. major; caused greater inhibition of release of lipoteichoic acid
(LTA)-induced TNF-α, IL-6 and nitric oxide from Gram-positive bacteria; can induce immunomodulatory effects on leukocytes depending
on the pathogen and surrounding cytokine milieu
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
| 2NDC, 2NDE
|
|
| 1. Giacometti, A., Cirioni, O., Ghiselli, R., Bergnach, C., Orlando, F., D’Amato, G., Mocchegiani, F., Silvestri, C., Del Prete, M. S., Skerlavaj, B., Saba, V., Zanetti, M., and Scalise, G. (2004) The antimicrobial peptide BMAP-28 reduces lethality in mouse models of staphylococcal sepsis. Crit. Care Med. 32, 2485–2490.
2. 1. Lynn, M. A., Kindrachuk, J., Marr, A. K., Jenssen, H., Panté, N., Elliott, M. R., Napper, S., Hancock, R. E., and McMaster, W. R. (2011) Effect of BMAP-28 Antimicrobial Peptides on Leishmania major Promastigote and Amastigote Growth: Role of Leishmanolysin in Parasite Survival. PLoS Negl. Trop. Dis. 5, e1141.
3. 1. Takagi, S., Bai, L., Ozeki, T., Miyagi, H., Kuroda, K., Hayashi, S., Yoneyama, H., Ando, T., and Isogai, E. (2014) A bovine myeloid antimicrobial peptide (BMAP-28) kills methicillin-resistant Staphylococcus aureus but promotes adherence of the bacteria. Anim. Sci. J. 85, 342–346.
|
| Bomi1277
| EF-hand domain-containing protein D2
| Bos taurus
| A5D7A0
| https://www.uniprot.org/uniprot/A5D7A0
| Whey, Exosome
| NP_001096715.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001096715.1
| 242
| 26918
| https://www.uniprot.org/uniprot/A5D7A0.fasta
| EFHD2
| 514259
| https://www.ncbi.nlm.nih.gov/gene/514259
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi128
| Cathelicidin-7
| Bos taurus
| P56425
| https://www.uniprot.org/uniprot/P56425
| Whey
| NP_777256.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777256.1
| 165
| 18848
| https://www.uniprot.org/uniprot/P56425.fasta
| CATHL7
| 317650
| https://www.ncbi.nlm.nih.gov/gene/317650
| Reviewed: Experimental evidence at transcript level
|
| broad–
spectrum activity against fungi and Gram-negative and Grampositive
bacteria, including MRSA and P. aeruginosa; is inactive against eukaryotic cells
| broad–
spectrum activity against fungi and Gram-negative and Grampositive
bacteria, including MRSA and P. aeruginosa; is inactive against eukaryotic cells
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
| _
|
|
| 1. Tomasinsig, L., Benincasa, M., Scocchi, M., Skerlavaj, B., Tossi, A., Zanetti, M., and Gennaro, R. (2010) Role of Cathelicidin Peptides in Bovine Host Defense and Healing. Probiotics Antimicrob. Proteins 2, 12–20.
2. Baumann, A., Kiener, M. S., Haigh, B., Perreten, V., and Summerfield, A. (2017) Differential Ability of Bovine Antimicrobial Cathelicidins to Mediate Nucleic Acid Sensing by Epithelial Cells. Front. Immunol. 8, 59.
3. 1. Gennaro, R., Scocchi, M., Merluzzi, L., and Zanetti, M. (1998) Biological characterization of a novel mammalian antimicrobial peptide. Biochim. Biophys. Acta 1425, 361–368.
4. 1. Scocchi, M., Wang, S., and Zanetti, M. (1997) Structural organization of the bovine cathelicidin gene family and identification of a novel member. FEBS Lett. 417, 311–315.
|
| Bomi1280
| Eukaryotic translation initiation factor 3 subunit C
| Bos taurus
| Q3SYW6
| https://www.uniprot.org/uniprot/Q3SYW6
| Whey, MFGM, Exosome
| NP_001029790.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029790.1
| 912
| 105366
| https://www.uniprot.org/uniprot/Q3SYW6.fasta
| EIF3C
| 534882
| https://www.ncbi.nlm.nih.gov/gene/534882
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1285
| Endoplasmin
| Bos taurus
| Q95M18
| https://www.uniprot.org/uniprot/Q95M18
| Whey, MFGM, Exosome
| NP_777125.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777125.1
| 804
| 92427
| https://www.uniprot.org/uniprot/Q95M18.fasta
| HSP90B1
| 282646
| https://www.ncbi.nlm.nih.gov/gene/282646
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi129
| Ras-related C3 botulinum toxin substrate 1
| Bos taurus
| P62998
| https://www.uniprot.org/uniprot/P62998
| Whey
| NP_776588.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776588.1
| 192
| 21450
| https://www.uniprot.org/uniprot/P62998.fasta
| RAC1
| 281440
| https://www.ncbi.nlm.nih.gov/gene/281440
| Reviewed: Experimental evidence at protein level
| Rac1 and Rac3 are ubiquitously expressed and therefore
regulate a wide variety of cellular processes, whereas Rac2 is predominantly
expressed in cells of the hematopoietic lineage; Rac1b was
discovered in human tumors;
| act as molecular switches cycling
between an active GTP‐bound and an inactive GDP‐bound form through
nucleotide exchange and hydrolysis; three distinct
mammalian Rac isoforms, Rac1, 2 and 3, share a very high sequence identity; Rac2 is proposed to be responsible for the regulation of the
oxidative burst in hematopoietic cells; serum‐inducible and hyperactive in breast cancer cells;
| act as molecular switches cycling
between an active GTP‐bound and an inactive GDP‐bound form through
nucleotide exchange and hydrolysis; three distinct
mammalian Rac isoforms, Rac1, 2 and 3, share a very high sequence identity; Rac2 is proposed to be responsible for the regulation of the
oxidative burst in hematopoietic cells; serum‐inducible and hyperactive in breast cancer cells;
|
|
|
|
|
|
| 1. Jordan, P., Brazão, R., Boavida, M. G., Gespach, C., & Chastre, E. (1999). Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene, 18(48), 6835–6839. https://doi.org/10.1038/sj.onc.1203233.
2. Haeusler, L. C., Blumenstein, L., Stege, P., Dvorsky, R., & Ahmadian, M. R. (2003). Comparative functional analysis of the Rac GTPases. FEBS Letters, 555(3), 556–560. https://doi.org/10.1016/S0014-5793(03)01351-6.
3. Fiegen, D., Haeusler, L.-C., Blumenstein, L., Herbrand, U., Dvorsky, R., Vetter, I. R., & Ahmadian, M. R. (2004). Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase. The Journal of Biological Chemistry, 279(6), 4743–4749. https://doi.org/10.1074/jbc.M310281200.
4. Haataja, L., Groffen, J., & Heisterkamp, N. (1997). Characterization of RAC3, a novel member of the Rho family. The Journal of Biological Chemistry, 272(33), 20384–20388. https://doi.org/10.1074/jbc.272.33.20384.
|
| Bomi1290
| Ewing's tumor-associated antigen 1 homolog
| Bos taurus
| Q08DI1
| https://www.uniprot.org/uniprot/Q08DI1
| Whey, Exosome
| NP_001068596.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068596.1
| 899
| 99859
| https://www.uniprot.org/uniprot/Q08DI1.fasta
| ETAA1
| 282224
| https://www.ncbi.nlm.nih.gov/gene/282224
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1297
| Factor XIIa inhibitor
| Bos taurus
| P50448
| https://www.uniprot.org/uniprot/P50448
| Whey
| NP_777246.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777246.1
| 468
| 51723
| https://www.uniprot.org/uniprot/P50448.fasta
|
| 281035
| https://www.ncbi.nlm.nih.gov/gene/281035
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi13
| Cathelicidin-1
| Bos taurus
| P22226
| https://www.uniprot.org/uniprot/P22226
| Whey
| NP_777250.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777250.1
| 155
| 17600
| https://www.uniprot.org/uniprot/P22226.fasta
| CATHL1
| 282164
| https://www.ncbi.nlm.nih.gov/gene/282164
| Reviewed: Experimental evidence at protein level
| neutrophils present in peripheral blood, bone marrow, spleen, or liver
| bactericidal activity against both Escherichia coli and Staphylococcus aureus;
| bactericidal activity against both Escherichia coli and Staphylococcus aureus;
| initial response of the mammary epithelium to microbial infection
|
| Antimicrobial peptides and upregulated in mastitis
|
| Stored in neutrophil granules in inactive forms; enzymatically cleaved into active peptides by neutrophil granule contents; bactenecin’s expression is
concomitant with granulopoiesis during fetal life
|
| 1. Romeo, D., Skerlavaj, B., Bolognesi, M., and Gennaro, R. (1988) Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263, 9573–9575.
2. 1. Smith, W. L., Sunaga, O., and Cullor, J. S. (1999) An evaluation of the tissue expression of a bovine dodecapeptide bactenecin in the adult and fetal animal. Comp. Haematol. Int. 9, 132–138
|
| Bomi130
| Protein S100-A12
| Bos taurus
| P79105
| https://www.uniprot.org/uniprot/P79105
| Whey
| NP_777076.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777076.1
| 92
| 10685
| https://www.uniprot.org/uniprot/P79105.fasta
| S100A12
| 282467
| https://www.ncbi.nlm.nih.gov/gene/282467
| Reviewed: Experimental evidence at protein level
| neutrophils, monocytes, smooth muscle cells;
| important mediators in many different cellular
functions involving immunity, inflammation, cell proliferation, apoptosis
and other activities; expression of S100A12 increased at some
cases of human inflammatory diseases; modulate interactions between cytoskeletal
elements and membranes; inhibits aggregation of aldolase and GAPDH and
may have Ca2+-dependent chaperone/anti-chaperone-like functions; play a role
in vascular remodeling
| important mediators in many different cellular
functions involving immunity, inflammation, cell proliferation, apoptosis
and other activities; expression of S100A12 increased at some
cases of human inflammatory diseases; modulate interactions between cytoskeletal
elements and membranes; inhibits aggregation of aldolase and GAPDH and
may have Ca2+-dependent chaperone/anti-chaperone-like functions; play a role
in vascular remodeling
| S100A12 was positively associated
with the somatic cell count and the sodium and chloride concentrations of milk; a negative correlation was found between S100A12 and the potassium concentration
and pH of milk; S100A12 level in milk may serve as a diagnostic
tool for subclinical mastitis in cows without obvious clinical signs
|
|
|
|
|
| 1. Zhong, K., Zhang, C.-Y., Zha, G.-M., Wang, X.-J., Jiao, X.-Q., Zhu, H.-S., & Wang, Y.-Y. (2018). S100 calcium-binding protein A12 as a diagnostic index for subclinical mastitis in cows. Reproduction in Domestic Animals = Zuchthygiene, 53(6), 1442–1447. https://doi.org/10.1111/rda.13273.
2. Hofmann Bowman, M., Wilk, J., Heydemann, A., Kim, G., Rehman, J., Lodato, J. A., … McNally, E. M. (2010). S100A12 mediates aortic wall remodeling and aortic aneurysm. Circulation Research, 106(1), 145–154. https://doi.org/10.1161/CIRCRESAHA.109.209486.
3. Hatakeyama, T., Okada, M., Shimamoto, S., Kubota, Y., & Kobayashi, R. (2004). Identification of intracellular target proteins of the calcium-signaling protein S100A12. European Journal of Biochemistry, 271(18), 3765–3775. https://doi.org/10.1111/j.1432-1033.2004.04318.
4. Vogl, T., Pröpper, C., Hartmann, M., Strey, A., Strupat, K., van den Bos, C., … Roth, J. (1999). S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14. The Journal of Biological Chemistry, 274(36), 25291–25296. https://doi.org/10.1074/jbc.274.36.25291.
|
| Bomi1307
| Coiled-coil domain containing 88A
| Bos taurus
| F1MAY4
| https://www.uniprot.org/uniprot/F1MAY4
| Whey, MFGM, Exosome
|
|
| 1842
| 212919
| https://www.uniprot.org/uniprot/F1MAY4.fasta
| CCDC88A
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi131
| Lactoperoxidase
| Bos taurus
| P80025
| http://www.uniprot.org/uniprot/P80025
| Whey
| NP_776358.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776358.1
| 712
| 80642
| http://www.uniprot.org/uniprot/P80025.fasta
| LPO
| 280844
| https://www.ncbi.nlm.nih.gov/gene/280844
| Reviewed: Experimental evidence at protein level
| saliva, airway mucus, tears
| Promotes host defence against microbes in milk saliva and airways; controlled catalysis of oxidation of certain molecules;
| Promotes host defence against microbes in milk saliva and airways; controlled catalysis of oxidation of certain molecules;
| Biocidal activity, efficient antibiotics and antiviral agents against a wide spectrum of bacteria, fungi, and viruses; activated lactoperoxidase by peroxide can preserve raw milk during transportation, reduces refrigeration and pasteurization requirement;
| glycoprotein; four to five N-glycosylation sites and are characterizedby a carbohydrate content of about 10 %;
|
| 2ips, 2nqx, 2pt3, 2pum, 2qpk, 2qqt, 2qrb, 3bxi, 3eri, 3gc1, 3gcj, 3gck, 3gcl, 3i6n, 3krq, 3nyh, 3ogw, 3py4, 3q9k, 3ql6, 3r4x, 3r5o, 3s4f, 3tgy, 3uba, 3v6q, 4gm7, 4gn6, 4ksz, 4njb, 4nt3, 4pnx, 5b72, 5gh0, 5gls, 5wv3, 5zgs, 5zww, 6a4y
|
|
| 1. Salathe, M., Holderby, M., Forteza, R., Abraham, W. M., Wanner, A., and Conner, G. E. (1997) Isolation and Characterization of a Peroxidase from the Airway. Am. J. Respir. Cell Mol. Biol. 17, 97–105.
2. Wijkstrom-Frei, C., El-Chemaly, S., Ali-Rachedi, R., Gerson, C., Cobas, M. A., Forteza, R., Salathe, M., and Conner, G. E. (2003) Lactoperoxidase and Human Airway Host Defense. Am. J. Respir. Cell Mol. Biol. 29, 206–212.
3. Singh, P. K., Iqbal, N., Sirohi, H. V., Bairagya, H. R., Kaur, P., Sharma, S., and Singh, T. P. (2018) Structural basis of activation of mammalian heme peroxidases. Prog. Biophys. Mol. Biol. 133, 49–55.
4. Reiter, B., Marshall, V. M., BjörckL, and Rosén, C. G. (1976) Nonspecific bactericidal activity of the lactoperoxidases-thiocyanate-hydrogen peroxide system of milk against Escherichia coli and some gram-negative pathogens. Infect. Immun. 13, 800–807.
5. Reiter, B., Marshall, V. M., and Philips, S. M. (1980) The antibiotic activity of the lactoperoxidase-thiocyanate-hydrogen peroxide system in the calf abomasum. Res. Vet. Sci. 28, 116–122.
6. Klebanoff, S. J. and Luebke, R. G. (1965) The Antilactobacillus System of Saliva. Role of Salivary Peroxidase. Exp. Biol. Med. 118, 483–486.
7. Kussendrager, K. D. and van Hooijdonk, A. C. (2000) Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 84 Suppl 1, S19-25.
8. Kamau, D. N., Doores, S., and Pruitt, K. M. (1990) Enhanced thermal destruction of Listeria monocytogenes and Staphylococcus aureus by the lactoperoxidase system. Appl. Environ. Microbiol. 56, 2711–2716.
9. Arqués, J. L., Rodríguez, E., Nuñez, M., and Medina, M. (2008) Antimicrobial Activity of Nisin, Reuterin, and the Lactoperoxidase System on Listeria monocytogenes and Staphylococcus aureus in Cuajada, a Semisolid Dairy Product Manufactured in Spain. J. Dairy Sci. 91, 70–75.
10. Furtmüller, P. G., Jantschko, W., Regelsberger, G., Jakopitsch, C., Arnhold, J., and Obinger, C. (2002) Reaction of lactoperoxidase compound I with halides and thiocyanate. Biochemistry 41, 11895–11900.
11. Redwan, E. M., EL-Fakharany, E. M., Uversky, V. N., and Linjawi, M. H. (2014) Screening the anti infectivity potentials of native N- and C-lobes derived from the camel lactoferrin against hepatitis C virus. BMC Complement. Altern. Med. 14, 219.
12. Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., and Obinger, C. (2006) Active site structure and catalytic mechanisms of human peroxidases. Arch. Biochem. Biophys. 445, 199–213
|
| Bomi1310
| Rho guanine nucleotide exchange factor 40
| Bos taurus
| F1MB21
| https://www.uniprot.org/uniprot/F1MB21
| Whey
| NP_001192870.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192870.1
| 1520
| 164934
| https://www.uniprot.org/uniprot/F1MB21.fasta
| ARHGEF40
| 527362
| https://www.ncbi.nlm.nih.gov/gene/527362
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1311
| Alpha-2-macroglobulin like 1
| Bos taurus
| F1MB32
| https://www.uniprot.org/uniprot/F1MB32
| Whey
| NP_001178230.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001178230.1
| 1396
| 155559
| https://www.uniprot.org/uniprot/F1MB32.fasta
| A2ML1
| 516769
| https://www.ncbi.nlm.nih.gov/gene/516769
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1315
| SMG1, nonsense mediated mRNA decay associated PI3K related kinase
| Bos taurus
| F1MBL6
| https://www.uniprot.org/uniprot/F1MBL6
| Whey, Exosome
| NP_001192844.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192844.1
| 3658
| 410232
| https://www.uniprot.org/uniprot/F1MBL6.fasta
| SMG1
| 525143
| https://www.ncbi.nlm.nih.gov/gene/525143
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1318
| Gamma-secretase activating protein
| Bos taurus
| F1MBQ5
| https://www.uniprot.org/uniprot/F1MBQ5
| Whey, Exosome
|
|
| 814
| 93572
| https://www.uniprot.org/uniprot/F1MBQ5.fasta
| GSAP
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi132
| Angiogenin2
| Bos taurus
| P80929
| https://www.uniprot.org/uniprot/P80929
| Whey
|
|
| 123
| 14522
| https://www.uniprot.org/uniprot/P80929.fasta
| ANG2
|
|
| Reviewed: Experimental evidence at protein level
|
| cell adhesion , nuclear translocation
, actin binding , inhibition of cell-free translation or
hydrolysis of tRNA; highly active in inducing blood-vessel
growth
| cell adhesion , nuclear translocation
, actin binding , inhibition of cell-free translation or
hydrolysis of tRNA; highly active in inducing blood-vessel
growth
| Milk contains considerably more bovine angiogenin than
does serum; binds to PRI but had very little RNase
activit
| cross-linked by three disulfide bonds, is glycosylated at Asn33; contained 5 - 6 mannose, 2- 3 glucosamine,
1-2 galactosamine, up to one xylose and no sialic acid
residues;
| modification of bovine angiogenin-2 is on
Am33 and should physically cover a large surface area of bovine
angiogenin-2, as on RNase B, some
modulation of nuclear translocation may be possible, even
though bovine angiogenin-2 is an active angiogenic molecule
|
|
|
| 1. Strydom, D. J., Bond, M. D., & Vallee, B. L. (1997). An angiogenic protein from bovine serum and milk--purification and primary structure of angiogenin-2. European Journal of Biochemistry, 247(2), 535–544. https://doi.org/10.1111/j.1432-1033.1997.00535.
|
| Bomi1320
| Transforming growth factor-beta-induced protein ig-h3
| Bos taurus
| F1MBS3
| https://www.uniprot.org/uniprot/F1MBS3
| Whey
|
|
| 649
| 70792
| https://www.uniprot.org/uniprot/F1MBS3.fasta
| TGFBI
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1326
| Keratin, type I cytoskeletal 14
| Bos taurus
| F1MC11
| https://www.uniprot.org/uniprot/F1MC11
| Whey, MFGM, Exosome
|
|
| 515
| 55895
| https://www.uniprot.org/uniprot/F1MC11.fasta
| KRT14
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1327
| Laminin subunit alpha 5
| Bos taurus
| F1MC13
| https://www.uniprot.org/uniprot/F1MC13
| Whey, Exosome
|
|
| 2649
| 285446
| https://www.uniprot.org/uniprot/F1MC13.fasta
| LAMA5
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1328
| Stromal antigen 1
| Bos taurus
| F1MC39
| https://www.uniprot.org/uniprot/F1MC39
| Whey
|
|
| 998
| 115030
| https://www.uniprot.org/uniprot/F1MC39.fasta
| STAG1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi133
| Complement factor B
| Bos taurus
| P81187
| https://www.uniprot.org/uniprot/P81187
| Whey
| NP_001035616.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001035616.1
| 761
| 85366
| https://www.uniprot.org/uniprot/P81187.fasta
| CFB
| 514076
| https://www.ncbi.nlm.nih.gov/gene/514076
| Reviewed: Experimental evidence at protein level
|
| key glycoprotein in the alternative
pathway of complement activation; role in assembly of the C3 convertase complex by association
with a C3b molecule; unusual type of
serine proteinase
| key glycoprotein in the alternative
pathway of complement activation; role in assembly of the C3 convertase complex by association
with a C3b molecule; unusual type of
serine proteinase
| immune protection
against environmental pathogens
| Glycosylated; glucose is covalently attached; sialylated complex biantennary
sugars
| N-linked oligosaccharide may be involved in the regulation of FB binding to C3b
|
|
|
| 1. Christie, D. L., & Gagnon, J. (1983). Amino acid sequence of the Bb fragment from complement factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment. Biochemical Journal, 209(1), 61–70. https://doi.org/10.1042/bj2090061.
2. Niemann, M. A., Bhown, A. S., & Miller, E. J. (1991). The principal site of glycation of human complement Factor B. Biochemical Journal, 274(2), 473–480. https://doi.org/10.1042/bj2740473.
3. Rainard, P. (2002). Complement factor B and the alternative pathway of complement activation in bovine milk. The Journal of Dairy Research, 69(1), 1–12. https://doi.org/10.1017/s0022029901005337.
4. Davrinche, C., Abbal, M., & Clerc, A. (1990). Molecular characterization of human complement factor B subtypes. Immunogenetics, 32(5), 309–312. https://doi.org/10.1007/bf00211644.
|
| Bomi1333
| FAT atypical cadherin 3
| Bos taurus
| F1MC84
| https://www.uniprot.org/uniprot/F1MC84
| Whey, MFGM
|
|
| 4555
| 499745
| https://www.uniprot.org/uniprot/F1MC84.fasta
| FAT3
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1334
| Zinc finger protein 106
| Bos taurus
| F1MC90
| https://www.uniprot.org/uniprot/F1MC90
| Whey
| XP_002690856.2
| https://www.ncbi.nlm.nih.gov/protein/XP_002690856.2
| 1903
| 211513
| https://www.uniprot.org/uniprot/F1MC90.fasta
| ZNF106
| 788468
| https://www.ncbi.nlm.nih.gov/gene/788468
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1336
| Leucine-rich repeat-containing protein 7
| Bos taurus
| F1MCA7
| https://www.uniprot.org/uniprot/F1MCA7
| Whey, MFGM, Exosome
|
|
| 1536
| 172407
| https://www.uniprot.org/uniprot/F1MCA7.fasta
| LRRC7
|
|
| Reviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi134
| Polymeric immunoglobulin receptor
| Bos taurus
| P81265
| http://www.uniprot.org/uniprot/P81265
| Whey
| NP_776568.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776568.1
| 757
| 82435
| http://www.uniprot.org/uniprot/P81265.fasta
| PIGR
| 281401
| https://www.ncbi.nlm.nih.gov/gene/281401
| Reviewed: Experimental evidence at transcript level
| saliva, intestinal secretions, bile, respiratory
secretions, and tears
| Transcytosed in intestinal epithelial cells, proteolytically cleaved at apical plasma membrane into secretory component and transmembrane segment; binds to IgA and IgM and protect them from proteolytic degradation; promotes internal neutralization of some viruses; binds to bacterial components of Streptococcus pneumonia and prevent their invasion on respiratory epithelial cells
| Transcytosed in intestinal epithelial cells, proteolytically cleaved at apical plasma membrane into secretory component and transmembrane segment; binds to IgA and IgM and protect them from proteolytic degradation; promotes internal neutralization of some viruses; binds to bacterial components of Streptococcus pneumonia and prevent their invasion on respiratory epithelial cells
| Important for the establishment of intestinal microbiota
| Heavily N-glycosylated; contains glucose, N-acetylglucosamine, N-acetylgalactosamine.
and N-acetylneuraminic acid as detected in human colustrum
|
|
|
|
| 1. Lu, L., Lamm, M. E., Li, H., Corthesy, B., and Zhang, J.-R. (2003) The human polymeric immunoglobulin receptor binds to Streptococcus pneumoniae via domains 3 and 4. J. Biol. Chem. 278, 48178–48187.
2. Tomana, M., Niedermeier, W., and Spivey, C. (1978) Microdetermination of monosaccharides in glycoproteins by gas-liquid chromatography. Anal. Biochem. 89, 110–118.
|
| Bomi1343
| Endoribonuclease Dicer
| Bos taurus
| F1MCQ5
| https://www.uniprot.org/uniprot/F1MCQ5
| Whey, MFGM
| XP_010815510.1
| https://www.ncbi.nlm.nih.gov/protein/XP_010815510.1
| 1922
| 218408
| https://www.uniprot.org/uniprot/F1MCQ5.fasta
| DICER1
| 337871
| https://www.ncbi.nlm.nih.gov/gene/337871
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi135
| Annexin A5
| Bos taurus
| P81287
| https://www.uniprot.org/uniprot/P81287
| Whey
|
|
| 321
| 36089
| https://www.uniprot.org/uniprot/P81287.fasta
| ANXA5
|
|
| Reviewed: Experimental evidence at protein level
|
| regulating membrane-cytoskeleton
dynamics; an association with the platelet membrane
of cytosolic phospholipase A2, suggests an interaction
between this phospholipase and annexin A5
| regulating membrane-cytoskeleton
dynamics; an association with the platelet membrane
of cytosolic phospholipase A2, suggests an interaction
between this phospholipase and annexin A5
|
|
|
|
|
|
| 1. Zhang, M., Chen, D., Zhen, Z., Ao, J., Yuan, X., & Gao, X. (2018). Annexin A2 positively regulates milk synthesis and proliferation of bovine mammary epithelial cells through the mTOR signaling pathway. Journal of Cellular Physiology, 233(3), 2464–2475. https://doi.org/10.1002/jcp.26123.
2. Rosengarth, A., Gerke, V., & Luecke, H. (2001). X-ray structure of full-length annexin 1 and implications for membrane aggregation. Journal of Molecular Biology, 306(3), 489–498. https://doi.org/10.1006/jmbi.2000.4423.
3. Rescher, U., Zobiack, N., & Gerke, V. (2000). Intact Ca(2+)-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells. Journal of Cell Science, 113 ( Pt 22), 3931–3938. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11058080.
|
| Bomi1356
| Laminin subunit gamma 1
| Bos taurus
| F1MD77
| https://www.uniprot.org/uniprot/F1MD77
| Whey, Exosome
|
|
| 1608
| 177693
| https://www.uniprot.org/uniprot/F1MD77.fasta
| LAMC1
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi136
| Nucleobindin 2
| Bos taurus
| Q0IIH5
| http://www.uniprot.org/uniprot/Q0IIH5
| Whey
| NP_001068849.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068849.1
| 415
| 49188
| http://www.uniprot.org/uniprot/Q0IIH5.fasta
| NUCB2
| 509003
| https://www.ncbi.nlm.nih.gov/gene/509003
| Unreviewed: Experimental evidence at protein level
| Serum
| Regulates appetite; production of body fat; role in glucose metabolism; acts as a substrate for caspase 3, 6 and 8
| Regulates appetite; production of body fat; role in glucose metabolism; acts as a substrate for caspase 3, 6 and 8
| Important for growth, bone formation, energy regulation and maturation of the gastrointestinal system in neonates
| Phosphorylated as found in gastric mucosa; might be glycosylated
|
|
|
|
| 1. Miura, K., Kurosawa, Y., and Kanai, Y. (1994) Calcium-Binding Activity of Nucleobindin Mediated by an EF Hand Moiety. Biochem. Biophys. Res. Commun. 199, 1388–1393.
2. Kroll, K. A., Otte, S., Hirschfeld, G., Barnikol-Watanabe, S., Götz, H., Sternbach, H., Kratzin, H. D., Barnikol, H. U., and Hilschmann, N. (1999) Heterologous overexpression of human NEFA and studies on the two EF-hand calcium-binding sites. Biochem. Biophys. Res. Commun. 260, 1–8.
3. Valencia, C. A., Cotten, S. W., Duan, J., and Liu, R. (2008) Modulation of nucleobindin-1 and nucleobindin-2 by caspases. FEBS Lett. 582, 286–290.
4. Kalnina, Z., Silina, K., Bruvere, R., Gabruseva, N., Stengrevics, A., Barnikol-Watanabe, S., Leja, M., and Line, A. Molecular characterisation and expression analysis of SEREX-defined antigen NUCB2 in gastric epithelium, gastritis and gastric cancer. Eur. J. Histochem. 53, 7–18.
5. Aydin, S. (2010) The presence of the peptides apelin, ghrelin and nesfatin-1 in the human breast milk, and the lowering of their levels in patients with gestational diabetes mellitus. Peptides 31, 2236–2240
|
| Bomi1360
| Transforming acidic coiled-coil containing protein 2
| Bos taurus
| F1MDB9
| https://www.uniprot.org/uniprot/F1MDB9
| Whey
|
|
| 2518
| 264441
| https://www.uniprot.org/uniprot/F1MDB9.fasta
| TACC2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1362
| Diacylglycerol kinase
| Bos taurus
| A6QPL5
| https://www.uniprot.org/uniprot/A6QPL5
| Whey, MFGM, Exosome
| NP_001030359.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001030359.2
| 1215
| 133974
| https://www.uniprot.org/uniprot/A6QPL5.fasta
| DGKD
| 513389
| https://www.ncbi.nlm.nih.gov/gene/513389
| Unreveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1366
| Fms related tyrosine kinase 1
| Bos taurus
| F1MDD9
| https://www.uniprot.org/uniprot/F1MDD9
| Whey, Exosome
| NP_001178061.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001178061.2
| 1337
| 149706
| https://www.uniprot.org/uniprot/F1MDD9.fasta
| FLT1
| 503620
| https://www.ncbi.nlm.nih.gov/gene/503620
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi137
| RNASET2 protein (Fragment)
| Bos taurus
| Q0III8
| https://www.uniprot.org/uniprot/Q0III8
| Whey
| NP_001193266.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193266.1
| 291
| 32830
| https://www.uniprot.org/uniprot/Q0III8.fasta
| RNASET2
| 508245
| https://www.ncbi.nlm.nih.gov/gene/508245
| Unreviewed: Experimental evidence at transcript level
| typically secreted from the cell, or localized to internal
compartments such as the lysosome or vacuole
| Endoribonucleases that cleave single stranded
RNA through a 2′,3′–cyclic phosphate intermediate, producing
mono- or oligonucleotides with a terminal 3′-phosphate; scavenger of nucleic acids; degradates self-
RNA; modulates host immune responses and serve as extra- or intracellular cytotoxins
| Endoribonucleases that cleave single stranded
RNA through a 2′,3′–cyclic phosphate intermediate, producing
mono- or oligonucleotides with a terminal 3′-phosphate; scavenger of nucleic acids; degradates self-
RNA; modulates host immune responses and serve as extra- or intracellular cytotoxins
| mediate an extracellular protective role; can participate in the
host response against infection both by direct antimicrobial action
and immune response activation; induces cytokine release in leukocytes
| glycosylated in eukaryotic cells- glucose, mannose, glucosamine, galactose and xylose
|
|
|
|
| 1. Inokuchi, N., Saitoh, S., Kobayashi, H., Itagaki, T., Koyama, T., Uchiyama, S., & Irie, M. (1999). Comparison of base specificity and other enzymatic properties of two protozoan ribonucleases from Physarum polycephalum and Dictyostelium discoideum. Bioscience, Biotechnology, and Biochemistry, 63(1), 141–145. https://doi.org/10.1271/bbb.63.141.
2. Uchida, T. (1966). Purification and properties of RNase T2. Journal of Biochemistry, 60(2), 115–132. https://doi.org/10.1093/oxfordjournals.jbchem.a128410.
3. Shimada, H., Inokuchi, N., Okuwaki, H., Koyama, T., & Irie, M. (1991). Purification and characterization of a base non-specific and adenylic acid preferring ribonuclease from the fruit bodies of Lentinus edodes. Agricultural and Biological Chemistry, 55(4), 1167–1169. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1368676.
4. Inada, Y., Watanabe, H., Ohgi, K., & Irie, M. (1991). Isolation, characterization, and primary structure of a base non-specific and adenylic acid preferential ribonuclease with higher specific activity from Trichoderma viride. Journal of Biochemistry, 110(6), 896–904. https://doi.org/10.1093/oxfordjournals.jbchem.a123686.
5. Inokuchi, N., Koyama, T., Sawada, F., & Irie, M. (1993). Purification, some properties, and primary structure of base non-specific ribonucleases from Physarum polycephalum. Journal of Biochemistry, 113(4), 425–432. https://doi.org/10.1093/oxfordjournals.jbchem.a124062.
6. Thompson, D. M., & Parker, R. (2009). The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae. The Journal of Cell Biology, 185(1), 43–50. https://doi.org/10.1083/jcb.200811119.
7. Irie, M. (1999). Structure-function relationships of acid ribonucleases: lysosomal, vacuolar, and periplasmic enzymes. Pharmacology & Therapeutics, 81(2), 77–89. https://doi.org/10.1016/s0163-7258(98)00035-7.
|
| Bomi1376
| Uncharacterized protein
| Bos taurus
| F1MDR5
| https://www.uniprot.org/uniprot/F1MDR5
| Whey
|
|
| 810
| 92324
| https://www.uniprot.org/uniprot/F1MDR5.fasta
| MIA2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1377
| DnaJ heat shock protein family (Hsp40) member C13
| Bos taurus
| F1MDR7
| https://www.uniprot.org/uniprot/F1MDR7
| Whey, MFGM, Exosome
|
|
| 2243
| 254413
| https://www.uniprot.org/uniprot/F1MDR7.fasta
| DNAJC13
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1379
| Histone-lysine N-methyltransferase
| Bos taurus
| F1MDT8
| https://www.uniprot.org/uniprot/F1MDT8
| Whey, Exosome
|
|
| 2539
| 284215
| https://www.uniprot.org/uniprot/F1MDT8.fasta
| SETD2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi138
| 78 kDa glucose-regulated protein
| Bos taurus
| Q0VCX2
| https://www.uniprot.org/uniprot/Q0VCX2
| Whey
| NP_001068616.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068616.1
| 655
| 72400
| https://www.uniprot.org/uniprot/Q0VCX2.fasta
| HSPA5
| 415113
| https://www.ncbi.nlm.nih.gov/gene/415113
| Reviewed: Experimental evidence at transcript level
|
| immunoglobulin heavy chain binding protein1 and as
the glucose regulated protein; ER-located
member of the family of HSP70 molecular chaperones; binds transiently to newly-synthesized proteins
in the ER and more permanently to misfolded,
underglycosylated or unassembled proteins whose
transport from the ER is blocked; assists the folding and assembly of newly-synthesized
proteins by recognising unfolded polypeptides and,
by inhibiting intra- or intermolecular aggregation,
maintaining them in a state competent for subsequent
folding and oligomerisation; maintain the permeability barrier of the ER membrane
by sealing the lumenal end of the translocon
pore before and early in translocation; required
during ara cell mating for the stage of karyogamy
that involves fusion of the nuclear membranes of Saccharomyces cerevisiae
| immunoglobulin heavy chain binding protein1 and as
the glucose regulated protein; ER-located
member of the family of HSP70 molecular chaperones; binds transiently to newly-synthesized proteins
in the ER and more permanently to misfolded,
underglycosylated or unassembled proteins whose
transport from the ER is blocked; assists the folding and assembly of newly-synthesized
proteins by recognising unfolded polypeptides and,
by inhibiting intra- or intermolecular aggregation,
maintaining them in a state competent for subsequent
folding and oligomerisation; maintain the permeability barrier of the ER membrane
by sealing the lumenal end of the translocon
pore before and early in translocation; required
during ara cell mating for the stage of karyogamy
that involves fusion of the nuclear membranes of Saccharomyces cerevisiae
| required for
mammary gland development; contributes to the regulation of Cripto signaling in mammary
stem cells; . Grp78 heterozygosity
impeded transgene-induced mammary tumor development,
with the tumors showing reduced proliferation, increased
apoptosis, and dramatic reduction of tumor angiogenesis
| mammalian BiP exists in interconvertible
monomeric and oligomeric forms and can
be post-translationally modified by phosphorylation and by ADP ribosylation
| important in regulating the
synthesis and polypeptide binding activity of the
molecule; conditions that increase
the levels of unfolded polypeptides in the ER lumen
cause a decrease in the extent of modification of
BiP and an increase in the proportion of monomeric species; post-translational
modification of BiP appears to provide a
storage pool of BiP that can be recruited back to the
active form in response to need
|
|
|
| 1. Panayi, G. S. and Corrigall, V. M. (2014) Immunoglobulin heavy-chain-binding protein (BiP): a stress protein that has the potential to be a novel therapy for rheumatoid arthritis. Biochem. Soc. Trans. 42, 1752–1755.
2. Pouysségur, J., Shiu, R. P., and Pastan, I. (1977) Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation. Cell 11, 941–947.
3. Munro, S. and Pelham, H. R. (1986) An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291–300.
4. McKay, D. B. (1993) Structure and mechanism of 70-kDa heat-shock-related proteins. Adv. Protein Chem. 44, 67–98.
5. Flynn, G. C., Chappell, T. G., and Rothman, J. E. (1989) Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245, 385–390.
6. Blond-Elguindi, S., Cwirla, S. E., Dower, W. J., Lipshutz, R. J., Sprang, S. R., Sambrook, J. F., and Gething, M. J. (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717–728.
7. Blond-Elguindi, S., Fourie, A. M., Sambrook, J. F., and Gething, M. J. (1993) Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J. Biol. Chem. 268, 12730–12735.
8. Fourie, A. M., Sambrook, J. F., and Gething, M. J. (1994) Common and divergent peptide binding specificities of hsp70 molecular chaperones. J. Biol. Chem. 269, 30470–30478.
9. Knarr, G., Gething, M. J., Modrow, S., and Buchner, J. (1995) BiP binding sequences in antibodies. J. Biol. Chem. 270, 27589–27594.
10. Flaherty, K. M., DeLuca-Flaherty, C., and McKay, D. B. (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623–628.
11. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., and Hendrickson, W. A. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606–1614.
12. Nishikawa, S. and Endo, T. (1997) The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion. J. Biol. Chem. 272, 12889–12892.
13. Brodsky, J. L. and Schekman, R. (1993) A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123, 1355–1363.
14. Lyman, S. K. and Schekman, R. (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88, 85–96.
15. Carlsson, L. and Lazarides, E. (1983) ADP-ribosylation of the Mr 83,000 stress-inducible and glucose-regulated protein in avian and mammalian cells: modulation by heat shock and glucose starvation. Proc. Natl. Acad. Sci. U. S. A. 80, 4664–4668.
|
| Bomi139
| Carboxypeptidase Q
| Bos taurus
| Q17QK3
| https://www.uniprot.org/uniprot/Q17QK3
| Whey
| NP_001069716.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001069716.1
| 472
| 51679
| https://www.uniprot.org/uniprot/Q17QK3.fasta
| CPQ
| 540923
| https://www.ncbi.nlm.nih.gov/gene/540923
| Reviewed: Experimental evidence at transcript level
| highest expression levels found in the nervous and prostatic tissue;
| membrane-bound binuclear zinc metallopeptidase ; involved in the neuron-neuron and neuron-glia
signaling via the hydrolysis of N-acetylaspartylglutamate (NAAG); facilitate integrin signaling in epithelial cells; associated with the anaphase promoting
complex in prostate cancer cells; activate the NF-κB signaling
pathway promoting cell proliferation; plays an important role in
folate absorption in humans
| membrane-bound binuclear zinc metallopeptidase ; involved in the neuron-neuron and neuron-glia
signaling via the hydrolysis of N-acetylaspartylglutamate (NAAG); facilitate integrin signaling in epithelial cells; associated with the anaphase promoting
complex in prostate cancer cells; activate the NF-κB signaling
pathway promoting cell proliferation; plays an important role in
folate absorption in humans
| belong to the protease system in milk
| heavily N- and Oglycosylated - ten N-glycosylation sites predicted within the primary sequence of human
GCPII
| N-glycosylation is indispensable for GCPII enzymatic activity and stability; glycosylation of the protein is implicated in apical sorting, proteolytic
resistance and its association with lipid rafts
|
|
|
| 1. Barinka, C., Sácha, P., Sklenár, J., Man, P., Bezouska, K., Slusher, B. S., & Konvalinka, J. (2004). Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity. Protein Science : A Publication of the Protein Society, 13(6), 1627–1635. https://doi.org/10.1110/ps.04622104.
2. Schülke, N., Varlamova, O. A., Donovan, G. P., Ma, D., Gardner, J. P., Morrissey, D. M., … Olson, W. C. (2003). The homodimer of prostate-specific membrane antigen is a functional target for cancer therapy. Proceedings of the National Academy of Sciences of the United States of America, 100(22), 12590–12595. https://doi.org/10.1073/pnas.1735443100.
3. Barinka, C., Rinnová, M., Sácha, P., Rojas, C., Majer, P., Slusher, B. S., & Konvalinka, J. (2002). Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II. Journal of Neurochemistry, 80(3), 477–487. https://doi.org/10.1046/j.0022-3042.2001.00715.
4. Kozikowski, A. P., Zhang, J., Nan, F., Petukhov, P. A., Grajkowska, E., Wroblewski, J. T., … Neale, J. H. (2004). Synthesis of urea-based inhibitors as active site probes of glutamate carboxypeptidase II: efficacy as analgesic agents. Journal of Medicinal Chemistry, 47(7), 1729–1738. https://doi.org/10.1021/jm0306226.
5. Jackson, P. F., Cole, D. C., Slusher, B. S., Stetz, S. L., Ross, L. E., Donzanti, B. A., & Trainor, D. A. (1996). Design, synthesis, and biological activity of a potent inhibitor of the neuropeptidase N-acetylated alpha-linked acidic dipeptidase. Journal of Medicinal Chemistry, 39(2), 619–622. https://doi.org/10.1021/jm950801q.
|
| Bomi1390
| Laminin subunit alpha 1
| Bos taurus
| F1MEG3
| https://www.uniprot.org/uniprot/F1MEG3
| Whey, Exosome
|
|
| 3032
| 330637
| https://www.uniprot.org/uniprot/F1MEG3.fasta
| LAMA1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1394
| Heparan sulfate proteoglycan 2
| Bos taurus
| F1MER7
| https://www.uniprot.org/uniprot/F1MER7
| Whey, MFGM, Exosome
|
|
| 4356
| 464021
| https://www.uniprot.org/uniprot/F1MER7.fasta
| HSPG2
|
|
| Unreviewed: Experimental evidence at protein leve
|
|
|
|
|
|
|
|
|
|
|
| Bomi14
| Cathepsin S
| Bos taurus
| P25326
| https://www.uniprot.org/uniprot/P25326
| Whey
| NP_001028787.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001028787.1
| 331
| 37176
| https://www.uniprot.org/uniprot/P25326.fasta
| CTSS
| 327711
| https://www.ncbi.nlm.nih.gov/gene/327711
| Reviewed: Experimental evidence at protein level
| Serum, synovial fluid, lymph nodes, spleen
| Plays several roles
in the disease process of RA; stable at physiological pH and is
involved in the major histocompatibility complex class II
(MHC II)-mediated antigen presentation, degradation of
the extracellular matrix in atherosclerosis, and other
inflammatory diseases as well as in tumor progression;
| Plays several roles
in the disease process of RA; stable at physiological pH and is
involved in the major histocompatibility complex class II
(MHC II)-mediated antigen presentation, degradation of
the extracellular matrix in atherosclerosis, and other
inflammatory diseases as well as in tumor progression;
|
| potential glycosylation
sites are located in the propeptide at position Asn104 in the
human enzyme; Asn100 as well as Asn110 in
the rat enzyme; Human cathepsin S contains three disulfide bonds
(Cys136-Cys180, Cys170-Cys213, Cys272-Cys320).
Cys139, His278 and Asn298
| Disulfide bonds are directed towards catalytic activity
|
| Cathepsin S is an endopeptidase with no detected exopeptidase
activities. The substrate specificity is similar to
that of cathepsins B, K, and L;
|
| 1. Weitoft, T., Larsson, A., Manivel, V. A., Lysholm, J., Knight, A., & Rönnelid, J. (2015). Cathepsin S and cathepsin L in serum and synovial fluid in rheumatoid arthritis with and without autoantibodies. Rheumatology (Oxford, England), 54(10), 1923–1928. https://doi.org/10.1093/rheumatology/keu486.
2. Wiederanders, B., Brömme, D., Kirschke, H., von Figura, K., Schmidt, B., & Peters, C. (1992). Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S. The Journal of Biological Chemistry, 267(19), 13708–13713. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1377692.
3. Shi, G. P., Munger, J. S., Meara, J. P., Rich, D. H., & Chapman, H. A. (1992). Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. The Journal of Biological Chemistry, 267(11), 7258–7262. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1373132.
4. Brömme, D., & Demuth, H. U. (1994). N,O-diacyl hydroxamates as selective and irreversible inhibitors of cysteine proteinases. Methods in Enzymology, 244, 671–685. https://doi.org/10.1016/0076-6879(94)44050-6.
5. Turk, B., Colić, A., Stoka, V., & Turk, V. (1994). Kinetics of inhibition of bovine cathepsin S by bovine stefin B. FEBS Letters, 339(1–2), 155–159. https://doi.org/10.1016/0014-5793(94)80405-2.
6. Kirschke, H., Wiederanders, B., Brömme, D., & Rinne, A. (1989). Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. The Biochemical Journal, 264(2), 467–473. https://doi.org/10.1042/bj2640467.
7. Xin, X. Q., Gunesekera, B., & Mason, R. W. (1992). The specificity and elastinolytic activities of bovine cathepsins S and H. Archives of Biochemistry and Biophysics, 299(2), 334–339. https://doi.org/10.1016/0003-9861(92)90283-3.
8. Turnsek, T., Kregar, I., & Lebez, D. (1975). Acid sulphydryl protease from calf lymph nodes. Biochimica et Biophysica Acta, 403(2), 514–520. https://doi.org/10.1016/0005-2744(75)90079-0.
|
| Bomi140
| Thrombospondin-1
| Bos taurus
| Q28178
| https://www.uniprot.org/uniprot/Q28178
| Whey
| NP_776621.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776621.1
| 1170
| 129534
| https://www.uniprot.org/uniprot/Q28178.fasta
| THBS1
| 281530
| https://www.ncbi.nlm.nih.gov/gene/281530
| Reviewed: Experimental evidence at transcript level
| Plasma, monocytes, α-granules of platelets,
| induces endothelial cell actin reorganization and focal
adhesion disassembly and influences multiple endothelial cell functions; influences cell
attachment to and spreading on substrates; cell motility; interacts with TGFß and modulates wound healing and proliferation; anti-angiogenic;
| induces endothelial cell actin reorganization and focal
adhesion disassembly and influences multiple endothelial cell functions; influences cell
attachment to and spreading on substrates; cell motility; interacts with TGFß and modulates wound healing and proliferation; anti-angiogenic;
| kinetics
of thrombospondin accumulation in human and goat milk has shown temporal variations which could be due to hormonal regulation. TSP
was detected in the initial aqueous phase of milk secretion
and its levels subsequently fell during the transition to mature
milk
| Glycosylated; contains neutral sugars, amino sugars, sialic acids;
|
|
|
|
| 1. Goldblum, S. E., Young, B. A., Wang, P., & Murphy-Ullrich, J. E. (1999). Thrombospondin-1 Induces Tyrosine Phosphorylation of Adherens Junction Proteins and Regulates an Endothelial Paracellular Pathway. Molecular Biology of the Cell, 10(5), 1537–1551. https://doi.org/10.1091/mbc.10.5.1537.
2. Dawes, J., Clezardin, P., & Pratt, D. (1987). Thrombospondin in Milk, Other Breast Secretions, and Breast Tissue. Seminars in Thrombosis and Hemostasis, 13(03), 378–384. https://doi.org/10.1055/s-2007-1003514.
3. Lawler, J. W., Slayter, H. S., & Coligan, J. E. (1978). Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. The Journal of Biological Chemistry, 253(23), 8609–8616. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/101549.
|
| Bomi1400
| Rho-associated protein kinase
| Bos taurus
| F1MF50
| https://www.uniprot.org/uniprot/F1MF50
| Whey, Exosome
|
|
| 1356
| 158648
| https://www.uniprot.org/uniprot/F1MF50.fasta
| ROCK1
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1403
| [F-actin]-monooxygenase MICAL2
| Bos taurus
| F1MF74
| https://www.uniprot.org/uniprot/F1MF74
| Whey, Exosome
| XP_005216149.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005216149.1
| 1101
| 124013
| https://www.uniprot.org/uniprot/F1MF74.fasta
| MICAL2
| 534041
| https://www.ncbi.nlm.nih.gov/gene/534041
| Reviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1404
| Spectrin repeat containing nuclear envelope protein 2
| Bos taurus
| F1MF78
| https://www.uniprot.org/uniprot/F1MF78
| Whey, MFGM, Exosome
| NP_001193515.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193515.1
| 6.919
| 797779
| https://www.uniprot.org/uniprot/F1MF78.fasta
| SYNE2
| 540504
| https://www.ncbi.nlm.nih.gov/gene/540504
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi141
| Serotransferrin
| Bos taurus
| Q29443
| http://www.uniprot.org/uniprot/Q29443
| Whey
| NP_803450.2
| https://www.ncbi.nlm.nih.gov/protein/NP_803450.2
| 704
| 77753
| http://www.uniprot.org/uniprot/Q29443.fasta
| TF
| 280705
| https://www.ncbi.nlm.nih.gov/gene/280705
| Reviewed: Experimental evidence at transcript level
| serum, milk
| Role in iron metabolism; delivers iron to cells via receptor mediated endocytosis; remove toxic free iron from blood; antibacterial;
| Role in iron metabolism; delivers iron to cells via receptor mediated endocytosis; remove toxic free iron from blood; antibacterial;
| Resistant to gastric hydrolysis; render biological activity in gastrointestinal tract
| Glycosylated; carbohydrate content varies from 3 to 11.8% of total protein weight; biantennary structure; presence of branched, hetero N-glycan chains; each glycan consists of two sialic acid, two galactose, three mannose and four N-acetylglucosamine residues;
|
|
|
|
| 1. Britton, J. R. and Koldovský, O. (1989) Gastric luminal digestion of lactoferrin and transferrin by preterm infants. Early Hum. Dev. 19, 127–135.
2. 1. Britton, J. R. and Koldovský, O. (1989) Gastric luminal digestion of lactoferrin and transferrin by preterm infants. Early Hum. Dev. 19, 127–135.
3. 1. MacGillivray, R. T., Mendez, E., Sinha, S. K., Sutton, M. R., Lineback-Zins, J., and Brew, K. (1982) The complete amino acid sequence of human serum transferrin. Proc. Natl. Acad. Sci. U. S. A. 79, 2504–2508.
4. 1. Kerckaert, J. P. and Bayard, B. (1982) Glycan uniformity within molecular variants of transferrin with distinct affinity for concanavalin A. Biochem. Biophys. Res. Commun. 105, 1023–1030.
5. 1. Aisen, P. and Listowsky, I. (1980) Iron transport and storage proteins. Annu. Rev. Biochem. 49, 357–393.
6. 1. Princiotto, J. V and Zapolski, E. J. (1975) Difference between the two iron-binding sites of transferrin. Nature 255, 87–88.
7. 1. Thakurta, P. G., Choudhury, D., Dasgupta, R., and Dattagupta, J. K. (2004) Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study. Biochem. Biophys. Res. Commun. 316, 1124–1131.
|
| Bomi1415
| HFM1, ATP dependent DNA helicase homolog
| Bos taurus
| F1MFR1
| https://www.uniprot.org/uniprot/F1MFR1
| Whey, Exosome
| NP_001192505.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192505.1
| 1437
| 162637
| https://www.uniprot.org/uniprot/F1MFR1.fasta
| HFM1
| 505814
| https://www.ncbi.nlm.nih.gov/gene/505814
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1417
| CUB and Sushi multiple domains 3
| Bos taurus
| F1MFS1
| https://www.uniprot.org/uniprot/F1MFS1
| Whey
|
|
| 3497
| 383092
| https://www.uniprot.org/uniprot/F1MFS1.fasta
| CSMD3
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1418
| Potassium channel tetramerization domain containing 9
| Bos taurus
| F1MFU2
| https://www.uniprot.org/uniprot/F1MFU2
| Whey
|
|
| 389
| 42524
| https://www.uniprot.org/uniprot/F1MFU2.fasta
| KCTD9
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi142
| Leucine-rich alpha-2-glycoprotein
| Bos taurus
| Q2KIF2
| https://www.uniprot.org/uniprot/Q2KIF2
| Whey
| NP_001039642.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001039642.1
| 346
| 38348
| https://www.uniprot.org/uniprot/Q2KIF2.fasta
| LRG1
| 514663
| https://www.ncbi.nlm.nih.gov/gene/514663
| Unreviewed: Experimental evidence at protein level
| serum, hepatocytes
| a serum protein which has been
implicated in angiogenesis and tumor promotion; expression increases in response to mediators of the
acute-phase response and bacterial infections; roles in cell survival, migration, invasion, and apoptosis
| a serum protein which has been
implicated in angiogenesis and tumor promotion; expression increases in response to mediators of the
acute-phase response and bacterial infections; roles in cell survival, migration, invasion, and apoptosis
| Found in whey; Has a role in inflammation
| has two
intrachain disulfide bonds; one galactosamine and four glucosamine
oligosaccharides attached;
| disulfide bond and the carbohydrate suggest that LRG is a membrane-derived or
membrane-associated protein containing a series of domains
capable of bipolar surface orientation
|
|
|
| 1. Druhan, L. J., Lance, A., Li, S., Price, A. E., Emerson, J. T., Baxter, S. A., … Avalos, B. R. (2017). Leucine Rich α-2 Glycoprotein: A Novel Neutrophil Granule Protein and Modulator of Myelopoiesis. PloS One, 12(1), e0170261. https://doi.org/10.1371/journal.pone.0170261.
2. Takahashi, N., Takahashi, Y., & Putnam, F. W. (1985). Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich alpha 2-glycoprotein of human serum. Proceedings of the National Academy of Sciences of the United States of America, 82(7), 1906–1910. https://doi.org/10.1073/pnas.82.7.1906.
3. Sun, D.-C., Shi, Y., Wang, L.-X., Lv, Y., Han, Q.-L., Wang, Z.-K., & Dai, G.-H. (2017). Leucine-rich alpha-2-glycoprotein-1, relevant with microvessel density, is an independent survival prognostic factor for stage III colorectal cancer patients: a retrospective analysis. Oncotarget, 8(39), 66550–66558. https://doi.org/10.18632/oncotarget.16289.
|
| Bomi1422
| Signal peptide peptidase like 2A
| Bos taurus
| F1MG08
| https://www.uniprot.org/uniprot/F1MG08
| Whey, MFGM, Exosome
|
|
| 541
| 60186
| https://www.uniprot.org/uniprot/F1MG08.fasta
| SPPL2A
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1428
| CDK5 regulatory subunit associated protein 2
| Bos taurus
| F1MGF7
| https://www.uniprot.org/uniprot/F1MGF7
| Whey, MFGM, Exosome
|
|
| 1924
| 215045
| https://www.uniprot.org/uniprot/F1MGF7.fasta
| CDK5RAP2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi143
| Carboxypeptidase B2
| Bos taurus
| Q2KIG3
| https://www.uniprot.org/uniprot/Q2KIG3
| Whey
| NP_001039462.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001039462.1
| 423
| 48822
| https://www.uniprot.org/uniprot/Q2KIG3.fasta
| CPB2
| 508222
| https://www.ncbi.nlm.nih.gov/gene/508222
| Reviewed: Experimental evidence at protein level
|
| enzyme that
selectively catalyzes the release of the carboxyl-terminal basic
amino acids, arginine and lysine, from proteins and peptides; possess esterase
activity toward hippuryl-n-argininic acid
| enzyme that
selectively catalyzes the release of the carboxyl-terminal basic
amino acids, arginine and lysine, from proteins and peptides; possess esterase
activity toward hippuryl-n-argininic acid
| belong to the protease system in milk
|
|
| 3D4U, 3DGV, 3OSL
|
|
| 1. FOLK, J. E., WOLFF, E. C., & SCHIRMER, E. W. (1962). The kinetics of carboxypeptidase B activity. II. Kinetic parameters of the cobalt and cadmium enzymes. The Journal of Biological Chemistry, 237, 3100–3104. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/13945772
|
| Bomi1430
| Oncostatin M receptor
| Bos taurus
| F1MGK8
| https://www.uniprot.org/uniprot/F1MGK8
| Whey, MFGM, Exosome
|
|
| 366
| 42167
| https://www.uniprot.org/uniprot/F1MGK8.fasta
| OSMR
|
|
| Unreveiwed:-Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1433
| Semaphorin 3F
| Bos taurus
| F1MGN0
| https://www.uniprot.org/uniprot/F1MGN0
| Whey, Exosome
|
|
| 792
| 89097
| https://www.uniprot.org/uniprot/F1MGN0.fasta
| SEMA3F
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi144
| Tetranectin
| Bos taurus
| Q2KIS7
| https://www.uniprot.org/uniprot/Q2KIS7
| Whey
| NP_001039677.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001039677.1
| 202
| 22144
| https://www.uniprot.org/uniprot/Q2KIS7.fasta
| CLEC3B
| 515783
| https://www.ncbi.nlm.nih.gov/gene/515783
| Reviewed: Experimental evidence at transcript level
| including monocytes, neutrophils, fibroblasts, osteoblasts, extracellular matrix of certain human carcinomas
(breast, colonic, and ovarian tumors
| role in
the invasive process, in
mineralization during osteogenesis; target plasminogen to specific carbohydrate ligands
on cell surfaces, in the extracellular matrix or to fibrin
| role in
the invasive process, in
mineralization during osteogenesis; target plasminogen to specific carbohydrate ligands
on cell surfaces, in the extracellular matrix or to fibrin
| Expression increases during mammary involution process
| contains
a long-form carbohydrate recognition domain with three disulfide bridges
|
|
|
|
| 1. Boggs, I., Hine, B., Smolenski, G., Hettinga, K., Zhang, L., & Wheeler, T. T. (2015). Changes in the repertoire of bovine milk proteins during mammary involution. EuPA Open Proteomics, 9, 65–75. https://doi.org/10.1016/j.euprot.2015.09.001.
2. Nielsen, B. B., Kastrup, J. S., Rasmussen, H., Holtet, T. L., Graversen, J. H., Etzerodt, M., … Larsen, I. K. (1997). Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil. FEBS Letters, 412(2), 388–396. https://doi.org/10.1016/s0014-5793(97)00664-9.
|
| Bomi1441
| Exophilin 5
| Bos taurus
| F1MGW8
| https://www.uniprot.org/uniprot/F1MGW8
| Whey
|
|
| 1933
| 216124
| https://www.uniprot.org/uniprot/F1MGW8.fasta
| EXPH5
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1443
| Uncharacterized protein (Fragment)
| Bos taurus
| F1MGY6
| https://www.uniprot.org/uniprot/F1MGY6
| Whey, Exosome
|
|
| 2864
| 324572
| https://www.uniprot.org/uniprot/F1MGY6.fasta
| TEX15
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1446
| Histone-lysine N-methyltransferase
| Bos taurus
| F1MHA1
| https://www.uniprot.org/uniprot/F1MHA1
| Whey, MFGM, Exosome
|
|
| 3710
| 405267
| https://www.uniprot.org/uniprot/F1MHA1.fasta
| KMT2A
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1447
| SET binding protein 1
| Bos taurus
| F1MHB3
| https://www.uniprot.org/uniprot/F1MHB3
| Whey
|
|
| 1606
| 176259
| https://www.uniprot.org/uniprot/F1MHB3.fasta
| SETBP1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi145
| Alpha-1B-glycoprotein
| Bos taurus
| Q2KJF1
| https://www.uniprot.org/uniprot/Q2KJF1
| Whey
| NP_001039708.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001039708.1
| 503
| 53554
| https://www.uniprot.org/uniprot/Q2KJF1.fasta
| A1BG
| 518955
| https://www.ncbi.nlm.nih.gov/gene/518955
| Reviewed: Experimental evidence at protein level
| urine
| associated with bladder cancer, having been detected in all tumor-bearing patient samples; could be involved in cell recognition and the regulation of cell behavior
| associated with bladder cancer, having been detected in all tumor-bearing patient samples; could be involved in cell recognition and the regulation of cell behavior
| Helps in building immunity
| single polypeptide chain N-linked to four
glucosamine oligosaccharides; All four glucosamine oligosaccharides
are attached to asparagine in the obligate tripeptide
acceptor sequence Asn-Xaa-Ser/Thr, in which Xaa is almost
any amino acid; five
intrachain disulfide bonds
|
|
|
|
| 1. Ishioka, N., Takahashi, N., & Putnam, F. W. (1986). Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the immunoglobulin supergene family. Proceedings of the National Academy of Sciences of the United States of America, 83(8), 2363–2367. https://doi.org/10.1073/pnas.83.8.2363
|
| Bomi146
| Haptoglobin
| Bos taurus
| Q2TBU0
| https://www.uniprot.org/uniprot/Q2TBU0
| Whey
| NP_001035560.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001035560.1
| 401
| 44859
| https://www.uniprot.org/uniprot/Q2TBU0.fasta
| HP
| 280692
| https://www.ncbi.nlm.nih.gov/gene/280692
| Reviewed: Experimental evidence at transcript level
| serum, saliva, amniotic fluid, urine
| antioxidant, scavenger of free hemoglobin and carry them for
degradation in the liver and for iron recycling, has angiogenic, anti-inflammatory and immunomodulatory properties; binds to most CD4 and
CD8 T lymphocytes, directly inhibiting their proliferation and
further modifying the T helper 1/Th2 balance; haptoglobin polymorphism may play a role in susceptibility to
bacterial infections in patients with liver cirrhosis
| antioxidant, scavenger of free hemoglobin and carry them for
degradation in the liver and for iron recycling, has angiogenic, anti-inflammatory and immunomodulatory properties; binds to most CD4 and
CD8 T lymphocytes, directly inhibiting their proliferation and
further modifying the T helper 1/Th2 balance; haptoglobin polymorphism may play a role in susceptibility to
bacterial infections in patients with liver cirrhosis
| significant role in the early response of the
mammary gland to pathogenic bacteria;
| Acidic glycoprotein tetramer; β-chain contains four N-glycosylation sites at
Asn184, Asn207, Asn211 and Asn241; increased O-glycosylation like fucosylation was revealed in different diseases; fucosylation and sialylation
have been reported to influence ligand–receptor interactions as found in humans
|
|
|
|
| 1. Vitalis, Z., Altorjay, I., Tornai, I., Palatka, K., Kacska, S., Palyu, E., Tornai, D., Udvardy, M., Harsfalvi, J., Dinya, T., Veres, G., Lakatos, P. L., and Papp, M. (2011) Phenotypic polymorphism of haptoglobin: A novel risk factor for the development of infection in liver cirrhosis. Hum. Immunol. 72, 348–354.
2. Kalmus, P., Simojoki, H., Pyörälä, S., Taponen, S., Holopainen, J., and Orro, T. (2013) Milk haptoglobin, milk amyloid A, and N-acetyl-β-d-glucosaminidase activity in bovines with naturally occurring clinical mastitis diagnosed with a quantitative PCR test. J. Dairy Sci. 96, 3662–3670.
3. Melamed-Frank, M., Lache, O., Enav, B. I., Szafranek, T., Levy, N. S., Ricklis, R. M., and Levy, A. P. (2001) Structure-function analysis of the antioxidant properties of haptoglobin. Blood 98, 3693–3698.
4. Polticelli, F., Bocedi, A., Minervini, G., and Ascenzi, P. (2008) Human haptoglobin structure and function - a molecular modelling study. FEBS J. 275, 5648–5656.
5. Kαtnik, I. and Dobryszycka, W. (1990) Enzyme Immunoassay to Measure Low Levels of Haptoglobin in Biological Fluids. J. Immunoassay 11, 503–517.
6. Wang, Y., Kinzie, E., Berger, F. G., Lim, S.-K., and Baumann, H. (2001) Haptoglobin, an inflammation-inducible plasma protein. Redox Rep. 6, 379–385.
7. Wejman, J. C., Hovsepian, D., Wall, J. S., Hainfeld, J. F., and Greer, J. (1984) Structure and assembly of haptoglobin polymers by electron microscopy. J. Mol. Biol. 174, 343–368.
8. Eckersall, P. D., Young, F. J., Nolan, A. M., Knight, C. H., McComb, C., Waterston, M. M., Hogarth, C. J., Scott, E. M., and Fitzpatrick, J. L. (2006) Acute Phase Proteins in Bovine Milk in an Experimental Model of Staphylococcus aureus Subclinical Mastitis. J. Dairy Sci. 89, 1488–1501.
9. Andersen, C. B. F., Torvund-Jensen, M., Nielsen, M. J., de Oliveira, C. L. P., Hersleth, H.-P., Andersen, N. H., Pedersen, J. S., Andersen, G. R., and Moestrup, S. K. (2012) Structure of the haptoglobin–haemoglobin complex. Nature 489, 456–459.
10. Boonyapranai, K., Tsai, H.-Y., Chen, M. C.-M., Sriyam, S., Sinchaikul, S., Phutrakul, S., and Chen, S.-T. (2011) Glycoproteomic analysis and molecular modeling of haptoglobin multimers. Electrophoresis 32, 1422–1432.
11. Mann, A. C., Record, C. O., Self, C. H., and Turner, G. A. (1994) Monosaccharide composition of haptoglobin in liver diseases and alcohol abuse: large changes in glycosylation associated with alcoholic liver disease. Clin. Chim. Acta. 227, 69–78.
12. Matsumoto, K., Yokote, H., Arao, T., Maegawa, M., Tanaka, K., Fujita, Y., Shimizu, C., Hanafusa, T., Fujiwara, Y., and Nishio, K. (2008) N -Glycan fucosylation of epidermal growth factor receptor modulates receptor activity and sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor. Cancer Sci. 99, 1611–1617.
13. Arredouani, M., Matthijs, P., Van Hoeyveld, E., Kasran, A., Baumann, H., Ceuppens, J. L., and Stevens, E. (2003) Haptoglobin directly affects T cells and suppresses T helper cell type 2 cytokine release. Immunology 108, 144–151.
|
| Bomi1460
| Zinc finger MYM-type containing 4
| Bos taurus
| F1MHR5
| https://www.uniprot.org/uniprot/F1MHR5
| Whey, Exosome
|
|
| 1518
| 169408
| https://www.uniprot.org/uniprot/F1MHR5.fasta
| ZMYM4
| 529962
| https://www.ncbi.nlm.nih.gov/gene/529962
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1463
| CCR4-NOT transcription complex subunit 1
| Bos taurus
| F1MHU9
| https://www.uniprot.org/uniprot/F1MHU9
| Whey
| NP_001192968.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192968.1
| 2376
| 266875
| https://www.uniprot.org/uniprot/F1MHU9.fasta
| CNOT1
| 533968
| https://www.ncbi.nlm.nih.gov/gene/533968
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi147
| Complement C3
| Bos taurus
| Q2UVX4
| http://www.uniprot.org/uniprot/Q2UVX4
| Whey
| NP_001035559.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001035559.2
| 1661
| 187253
| http://www.uniprot.org/uniprot/Q2UVX4.fasta
| C3
| 280677
| https://www.ncbi.nlm.nih.gov/gene/280677
| Reviewed: Experimental evidence at protein level
| serum,
| Component of innate immune system; host mechanism for detection and clearance of potential pathogens; stimulates mast cell degranulation, plays an important role in chemotaxis and serves as a precursor of the acylation stimulating protein through its interaction with carboxypeptidase B; special marker of chronic
inflammation
| Component of innate immune system; host mechanism for detection and clearance of potential pathogens; stimulates mast cell degranulation, plays an important role in chemotaxis and serves as a precursor of the acylation stimulating protein through its interaction with carboxypeptidase B; special marker of chronic
inflammation
| Protection o mammary gland; increased resistance to breast-fed infants against infections; defeciency leads to an increased risk of mastitis;
| Glycosylated; N-linked high-mannose carbohydrate moieties are attached at residues 917 of the α-chain and 63 of the ß-chain
|
| 2b39
|
|
| 1. Hase, S., Kikuchi, N., Ikenaka, T., and Inoue, K. (1985) Structures of sugar chains of the third component of human complement. J. Biochem. 98, 863–874.
2. Prentice, A., Prentice, A. M., and Lamb, W. H. (1985) Mastitis in rural Gambian mothers and the protection of the breast by milk antimicrobial factors. Trans. R. Soc. Trop. Med. Hyg. 79, 90–95.
3. Buescher, E. S. (2001) Anti-inflammatory characteristics of human milk: how, where, why. Adv. Exp. Med. Biol. 501, 207–222.
4. Széplaki, G., Prohászka, Z., Duba, J., Rugonfalvi-Kiss, S., Karádi, I., Kókai, M., Kramer, J., Füst, G., Kleiber, M., Romics, L., and Varga, L. (2004) Association of high serum concentration of the third component of complement (C3) with pre-existing severe coronary artery disease and new vascular events in women. Atherosclerosis 177, 383–389.
5. Hirani, S., Lambris, J. D., and Müller-Eberhard, H. J. (1986) Structural analysis of the asparagine-linked oligosaccharides of human complement component C3. Biochem. J. 233, 613–616.
6. Hase, S., Kikuchi, N., Ikenaka, T., and Inoue, K. (1985) Structures of sugar chains of the third component of human complement. J. Biochem. 98, 863–874.
|
| Bomi1474
| Zinc finger protein 462
| Bos taurus
| F1MIB3
| https://www.uniprot.org/uniprot/F1MIB3
| Whey, Exosome
| XP_005210549.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005210549.1
| 2501
| 283374
| https://www.uniprot.org/uniprot/F1MIB3.fasta
| ZNF462
| 515561
| https://www.ncbi.nlm.nih.gov/gene/515561
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1475
| SCY1 like pseudokinase 2
| Bos taurus
| A6QLN8
| https://www.uniprot.org/uniprot/A6QLN8
| Whey
| NP_001095999.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001095999.1
| 929
| 103376
| https://www.uniprot.org/uniprot/A6QLN8.fasta
| SCYL2
| 782059
| https://www.ncbi.nlm.nih.gov/gene/782059
| Unreviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi148
| Vitamin D-binding protein
| Bos taurus
| Q3MHN5
| https://www.uniprot.org/uniprot/Q3MHN5
| Whey
| NP_001030457.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001030457.1
| 474
| 53342
| https://www.uniprot.org/uniprot/Q3MHN5.fasta
| GC
| 530076
| https://www.ncbi.nlm.nih.gov/gene/530076
| Reviewed: Experimental evidence at transcript level
| Serum,
| Role in the transport of vitamin D metabolites; maintains total levels of vitamin D and regulates the amounts of free (unbound) vitamin D available for specific tissues and cell types to utilize; binds actin and fatty acids preventing their polymerization; immune functions such as in B-cells, DBP seems to participate
in the linkage of surface immunoglobulins
| Role in the transport of vitamin D metabolites; maintains total levels of vitamin D and regulates the amounts of free (unbound) vitamin D available for specific tissues and cell types to utilize; binds actin and fatty acids preventing their polymerization; immune functions such as in B-cells, DBP seems to participate
in the linkage of surface immunoglobulins
| Colostrum could be a rich source of vitamin D associated with DBP and could play an important role in the intake of vitamin D sterols in the newborn.
| Glycosylated; GC1 forms have glycosylations at positions 418 and 420, whereas GC2 has glycosylation only at 418; trisaccharides as most frequent in GC1 with lesser amounts of disaccharides as found in humans
|
|
|
|
| 1. Ena, J., Pérez, M. D., Aranda, P., Sánchez, L., and Calvo, M. (1992) Presence and changes in the concentration of vitamin D-binding protein throughout early lactation in human and bovine colostrum and milk. J. Nutr. Biochem. 3, 498–502.
2. HIRSCHFELD, J. (1959) Immune-electrophoretic demonstration of qualitative differences in human sera and their relation to the haptoglobins. Acta Pathol. Microbiol. Scand. 47, 160–168.
3. Svasti, J., Kurosky, A., Bennett, A., and Bowman, B. H. (1979) Molecular basis for the three major forms of human serum vitamin D binding protein (group-specific component). Biochemistry 18, 1611–1617.
4. Cooke, N. E. and David, E. V. (1985) Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family. J. Clin. Invest. 76, 2420–2424.
5. Svasti, J. and Bowman, B. H. (1978) Human group-specific component. Changes in electrophoretic mobility resulting from vitamin D binding and from neuraminidase digestion. J. Biol. Chem. 253, 4188–4194.
6. Ravnsborg, T., Olsen, D. T., Thysen, A. H., Christiansen, M., Houen, G., and Højrup, P. (2010) The glycosylation and characterization of the candidate Gc macrophage activating factor. Biochim. Biophys. Acta 1804, 909–917.
7. Mc Leod, J. F., Kowalski, M. A., and Haddad, J. G. (1989) Interactions among serum vitamin D binding protein, monomeric actin, profilin, and profilactin. J. Biol. Chem. 264, 1260–1267.
8. Calvo, M. and Ena, J. M. (1989) Relations between vitamin D and fatty acid binding properties of vitamin D-binding protein. Biochem. Biophys. Res. Commun. 163, 14–17.
|
| Bomi149
| Gelsolin
| Bos taurus
| Q3SX14
| https://www.uniprot.org/uniprot/Q3SX14
| Whey
| NP_001029799.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029799.1
| 731
| 80731
| https://www.uniprot.org/uniprot/Q3SX14.fasta
| GSN
| 535077
| https://www.ncbi.nlm.nih.gov/gene/535077
| Reviewed: Experimental evidence at transcript level
|
| Gelsolin superfamily proteins have roles in a
diversity of cellular processes; regulation
of actin dynamics; antiapoptotic role; inhibit Aß-induced neurotoxicity; increased expression of gelsolin in oxidative stress helps cells to escape death
| Gelsolin superfamily proteins have roles in a
diversity of cellular processes; regulation
of actin dynamics; antiapoptotic role; inhibit Aß-induced neurotoxicity; increased expression of gelsolin in oxidative stress helps cells to escape death
| downregulated in clinical mastitis
|
|
|
|
|
| 1. Chauhan, V., Ji, L., & Chauhan, A. (2008). Anti-amyloidogenic, anti-oxidant and anti-apoptotic role of gelsolin in Alzheimer’s disease. Biogerontology, 9(6), 381–389. https://doi.org/10.1007/s10522-008-9169-z.
2. Kiselar, J. G., Janmey, P. A., Almo, S. C., & Chance, M. R. (2003). Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting. Proceedings of the National Academy of Sciences of the United States of America, 100(7), 3942–3947. https://doi.org/10.1073/pnas.0736004100.
3. Lueck, A., Yin, H. L., Kwiatkowski, D. J., & Allen, P. G. (2000). Calcium regulation of gelsolin and adseverin: a natural test of the helix latch hypothesis. Biochemistry, 39(18), 5274–5279. https://doi.org/10.1021/bi992871v.
|
| Bomi1494
| Dedicator of cytokinesis 5
| Bos taurus
| F1MJ73
| https://www.uniprot.org/uniprot/F1MJ73
| Whey, Exosome
|
|
| 1869
| 215189
| https://www.uniprot.org/uniprot/F1MJ73.fasta
| DOCK5
| 505572
| https://www.ncbi.nlm.nih.gov/gene/505572
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1496
| Unc-80 homolog, NALCN channel complex subunit
| Bos taurus
| F1MJ95
| https://www.uniprot.org/uniprot/F1MJ95
| Whey, Exosome
| NP_001193492.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193492.1
| 3258
| 363665
| https://www.uniprot.org/uniprot/F1MJ95.fasta
| UNC80
| 536610
| https://www.ncbi.nlm.nih.gov/gene/536610
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi15
| Protein S100-A8
| Bos taurus
| P28782
| https://www.uniprot.org/uniprot/P28782
| Whey
| NP_001107197.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001107197.1
| 89
| 10460
| https://www.uniprot.org/uniprot/P28782.fasta
| S100A8
| 616818
| https://www.ncbi.nlm.nih.gov/gene/616818
| Reviewed: Experimental evidence at protein level
| S100A8 and S100A9 are small calcium-binding proteins that are highly expressed in neutrophil and monocyte cytosol, endothelial and epithelial cells; uterus, cervix
| s100 A8 and A9 are found at high levels in the extracellular milieu during inflammatory conditions; Extracellular S100A8, S100A9, and S100A8/A9 mediate regulatory
and biological functions, including antiproliferative, antitumoral,
antimicrobial, and antinociceptive activities and induce neutrophil adhesion to fibrinogen in vitro; vital role in regulating the
interactions between the mammalian foetus and the uterus; important in regulating reproductive functions; showed specific patterns during the different stages
of pregnancy; exert strong proinflammatory
and chemotactic activities by promoting leukocyte
recruitment; In murine macrophages,
S100A8, but not S100A9, is induced by TLR agonists in an interleukin (IL)-10-dependent
manner; some agonists require cAMP and/or PGE2 generation for full expression; In murine keratinocytes, S100A8 is induced
by oxidative stress whereas S100A9 is not, confirming; S100A9 is a p38 MAPK target phosphorylated after phagocyte activation; S100A9 reduces microtubule polymerization and
F-actin cross-linking by the S100A8/S100A9 complex; S100A8 and S100A9 form a heterocomplex. S100A8/S100A9 inhibits casein kinase I and II
suggesting a role in myeloid cell differentiation
| s100 A8 and A9 are found at high levels in the extracellular milieu during inflammatory conditions; Extracellular S100A8, S100A9, and S100A8/A9 mediate regulatory
and biological functions, including antiproliferative, antitumoral,
antimicrobial, and antinociceptive activities and induce neutrophil adhesion to fibrinogen in vitro; vital role in regulating the
interactions between the mammalian foetus and the uterus; important in regulating reproductive functions; showed specific patterns during the different stages
of pregnancy; exert strong proinflammatory
and chemotactic activities by promoting leukocyte
recruitment; In murine macrophages,
S100A8, but not S100A9, is induced by TLR agonists in an interleukin (IL)-10-dependent
manner; some agonists require cAMP and/or PGE2 generation for full expression; In murine keratinocytes, S100A8 is induced
by oxidative stress whereas S100A9 is not, confirming; S100A9 is a p38 MAPK target phosphorylated after phagocyte activation; S100A9 reduces microtubule polymerization and
F-actin cross-linking by the S100A8/S100A9 complex; S100A8 and S100A9 form a heterocomplex. S100A8/S100A9 inhibits casein kinase I and II
suggesting a role in myeloid cell differentiation
| involved in the innate immune defense
against pathogens;
|
|
|
|
| P28783
| 1. Ryckman, C., Vandal, K., Rouleau, P., Talbot, M., & Tessier, P. A. (2003). Proinflammatory activities of S100: proteins S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion. Journal of Immunology (Baltimore, Md. : 1950), 170(6), 3233–3242. https://doi.org/10.4049/jimmunol.170.6.3233.
2. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13.
3. Elgawish, R. A., Ogata, Y., Hidaka, T., Nii, T., Yoshimura, Y., & Isobe, N. (2018). Changes in plasma concentrations of S100A7 and S100A8 in dairy cows during pregnancy. Reproduction in Domestic Animals = Zuchthygiene, 53(4), 1013–1015. https://doi.org/10.1111/rda.13185
|
| Bomi150
| Alpha-fetoprotein
| Bos taurus
| Q3SZ57
| https://www.uniprot.org/uniprot/Q3SZ57
| Whey
| NP_001029434.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029434.1
| 610
| 68588
| https://www.uniprot.org/uniprot/Q3SZ57.fasta
| AFP
| 506011
| https://www.ncbi.nlm.nih.gov/gene/506011
| Reviewed: Experimental evidence at transcript level
| fetal liver, yolk sac of mammals; bovine fetal fluids; ascitic fluid, cerebrospinal fluid (CSF) and bile,
from human fetuses;
| contribute to the efficiency of stimulation
of proliferation in cell culture systems; growth-promoting activity;
| contribute to the efficiency of stimulation
of proliferation in cell culture systems; growth-promoting activity;
| Innate immunity agents in milk
| glycoprotein; bAFP in FBS is approximately
evenly divided between Con A
reactive and non-reactive variants; bAFP in amniotic fluid from an early gestation
animal exhibited 72% reactive and 28%
non-reactive variants
| significant changes in lectin-binding
properties of glycoproteins are associated
with normal and tumor cell growth as well
as fetal development; non-reactive variants of bAFP in FBS
increases in parallel with fetal development;
|
|
|
| 1. Smith, J. A., Francis, T. I., Edington, G. M., & Williams, A. O. (1971). Human alpha fetoprotein in body fluids. British Journal of Cancer, 25(2), 337–342. https://doi.org/10.1038/bjc.1971.43.
2. Janzen, R. G., Mably, E. R., Tamaoki, T., Church, R. B., & Lorscheider, F. L. (1982). Synthesis of alpha-fetoprotein by the pre-implantation and post-implantation bovine embryo. Journal of Reproduction and Fertility, 65(1), 105–110. https://doi.org/10.1530/jrf.0.0650105.
3. He, Y., & Keel, B. A. (1994). Biochemical characterization of bovine alpha-fetoprotein and comparison with human alpha-fetoprotein. Comparative Biochemistry and Physiology. Biochemistry and Molecular Biology, 108(3), 327–336. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7521727.
|
| Bomi1501
| Dynein axonemal heavy chain 9
| Bos taurus
| F1MJJ0
| https://www.uniprot.org/uniprot/F1MJJ0
| Whey, Exosome
|
|
| 4485
| 510010
| https://www.uniprot.org/uniprot/F1MJJ0.fasta
| DNAH9
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1506
| URB2 ribosome biogenesis homolog
| Bos taurus
| F1MJR1
| https://www.uniprot.org/uniprot/F1MJR1
| Whey
|
|
| 1521
| 169560
| https://www.uniprot.org/uniprot/F1MJR1.fasta
| URB2
| 514623
| https://www.ncbi.nlm.nih.gov/gene/514623
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi151
| Syndecan binding protein (Syntenin)
| Bos taurus
| Q3SZA6
| https://www.uniprot.org/uniprot/Q3SZA6
| Whey
| NP_001068951.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068951.1
| 298
| 32389
| https://www.uniprot.org/uniprot/Q3SZA6.fasta
| SDCBP
| 510979
| https://www.ncbi.nlm.nih.gov/gene/510979
| Unreviewed: Experimental evidence at transcript level
|
| might have flexible cell-type-specific roles, forming unique
scaffolds that are dependent on the available intracellular
environment; at least ten putative binding PDZ2 tandem, but neither the isolated domains nor
partners reported for syntenin , including IL-5 receptor α-subunit, neuroglian, pro-TGFα
| might have flexible cell-type-specific roles, forming unique
scaffolds that are dependent on the available intracellular
environment; at least ten putative binding PDZ2 tandem, but neither the isolated domains nor
partners reported for syntenin , including IL-5 receptor α-subunit, neuroglian, pro-TGFα
| IgA-inducing protein in colostrum
|
|
|
|
|
| 1. Kang, B. S., Cooper, D. R., Jelen, F., Devedjiev, Y., Derewenda, U., Dauter, Z., Otlewski, J., and Derewenda, Z. S. (2003) PDZ tandem of human syntenin: crystal structure and functional properties. Structure 11, 459–468.
2. Grootjans, J. J., Zimmermann, P., Reekmans, G., Smets, A., Degeest, G., Dürr, J., and David, G. (1997) Syntenin, a PDZ protein that binds syndecan cytoplasmic domains. Proc. Natl. Acad. Sci. U. S. A. 94, 13683–13688.
3. Koroll, M., Rathjen, F. G., and Volkmer, H. (2001) The Neural Cell Recognition Molecule Neurofascin Interacts with Syntenin-1 but Not with Syntenin-2, Both of Which Reveal Self-associating Activity. J. Biol. Chem. 276, 10646–10654.
|
| Bomi1514
| Dynein axonemal heavy chain 2
| Bos taurus
| F1MK55
| https://www.uniprot.org/uniprot/F1MK55
| Whey, MFGM, Exosome
| NP_001178178.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001178178.1
| 4424
| 508289
| https://www.uniprot.org/uniprot/F1MK55.fasta
| DNAH2
| 789044
| https://www.ncbi.nlm.nih.gov/gene/789044
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1516
| Tumor protein 63 (p63)
| Bos taurus
| F1MKA9
| https://www.uniprot.org/uniprot/F1MKA9
| Whey
| NP_001178266.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001178266.1
| 680
| 76742
| https://www.uniprot.org/uniprot/F1MKA9.fasta
| TP63
| 615335
| https://www.ncbi.nlm.nih.gov/gene/615335
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1518
| TBC1 domain family member 1
| Bos taurus
| O97790
| https://www.uniprot.org/uniprot/O97790
| Whey, MFGM, Exosome
| NP_001159996.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001159996.1
| 1165
| 132097
| https://www.uniprot.org/uniprot/O97790.fasta
| TBC1D1
| 282704
| https://www.ncbi.nlm.nih.gov/gene/282704
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi152
| Alpha-1-acid glycoprotein
| Bos taurus
| Q3SZR3
| https://www.uniprot.org/uniprot/Q3SZR3
| Whey
| NP_001035592.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001035592.1
| 202
| 23182
| https://www.uniprot.org/uniprot/Q3SZR3.fasta
| ORM1
| 497200
| https://www.ncbi.nlm.nih.gov/gene/497200
| Reviewed: Experimental evidence at transcript level
|
| Belongs to the “lipocalins” family,
a group of proteins that are deputed to the
binding and transport of small hydrophobic
molecules; classified as immunocalins, a subfamily of proteins
that may also immunomodulate the inflammatory
reaction; acute Phase Proteins, structurally
un-related group of mainly liverderived
plasma proteins that are associated
with an acute phase reaction
| Belongs to the “lipocalins” family,
a group of proteins that are deputed to the
binding and transport of small hydrophobic
molecules; classified as immunocalins, a subfamily of proteins
that may also immunomodulate the inflammatory
reaction; acute Phase Proteins, structurally
un-related group of mainly liverderived
plasma proteins that are associated
with an acute phase reaction
| A predicted role in milk: an immunomodulatory
molecule; could play
several roles during inflammatory challenges
in the mammary gland; inhibit several
activities of neutrophils that can
cause severe cell and tissue damages in the
mammary gland; in humans, the protein significantly inhibits the proliferation
of peripheral blood T-cells , induces the
expression of several pro- and anti-inflammatory
cytokines by monocytes and
can directly antagonise the capillary leakage
induced by some inflammatory mediators,
such as histamine, platelet activating
factor and bradykinin; physiological amount may be increased
during mastitis
| A glycoprotein; carbohydrate moiety accounting for
26.6% of its molecular weight; presence of sialic acid-containing diantennary
oligosaccharides which is composed
of only N-glycolylneuraminic acid as reported in bovine milk; presence of 2 isoforms in milk, one from mammary galnd and another from somatic cells; isoforms share a
similar content of sialic acid a(2-3)- and a(2-6)-linked to
galactose; somatic cells produce AGP isoforms that are strongly
fucosylated and contain an elevated number of diantennary
glycans; in humans the protein has five N-linked glycans; different degrees of branching; structurally heterogeneous due to the great diversity
of the terminating sugars;
| Reported in bovine: immunomodulatory function of is dependent on both
its fucosylation and its branching degree; hyperfucosylated
AGP from somatic cells is anti-inflammatory, since it can reduce the local
inflammatory reaction by both ameliorating neutrophilsmediated
damage and by reducing the complement activation
|
|
|
| 1. Ceciliani, F., Pocacqua, V., Lecchi, C., Fortin, R., Rebucci, R., Avallone, G., … Sartorelli, P. (2007). Differential expression and secretion of α1-acid glycoprotein in bovine milk. Journal of Dairy Research, 74(03), 374. https://doi.org/10.1017/S0022029907002646.
2. Guha, A., Guha, R., & Gera, S. (2013). Comparison of α1-Antitrypsin, α1-Acid Glycoprotein, Fibrinogen and NOx as Indicator of Subclinical Mastitis in Riverine Buffalo (Bubalus bubalis). Asian-Australasian Journal of Animal Sciences, 26(6), 788–794. https://doi.org/10.5713/ajas.2012.12261.
3. Ceciliani, F., Pocacqua, V., Provasi, E., Comunian, C., Bertolini, A., Bronzo, V., … Sartorelli, P. (2005). Identification of the bovine α 1-acid glycoprotein in colostrum and milk. Veterinary Research, 36(5–6), 735–746. https://doi.org/10.1051/vetres:2005029.
4. Guha, A., Guha, R., & Gera, S. (2013). Comparison of α1-Antitrypsin, α1-Acid Glycoprotein, Fibrinogen and NOx as Indicator of Subclinical Mastitis in Riverine Buffalo (Bubalus bubalis). Asian-Australasian Journal of Animal Sciences, 26(6), 788–794. https://doi.org/10.5713/ajas.2012.12261.
5. Lijima, S., Shiba, K., Kimura, M., Nagai, K., & Iwai, T. (2000). Changes of α1-acid glycoprotein microheterogeneity in acute inflammation stages analyzed by isoelectric focusing using serum obtained postoperatively. Electrophoresis, 21(4), 753–759. https://doi.org/10.1002/(SICI)1522-2683(20000301)21:4<753::AID-ELPS753>3.0.CO;2-Y.
6. Eap, C. B., Cuendet, C., & Baumann, P. (1988). Orosomucoid (alpha-1 acid glycoprotein) phenotyping by use of immobilized pH gradients with 8 M urea and immunoblotting - A new variant encountered in a population study. Human Genetics, 80(2), 183–185. https://doi.org/10.1007/BF00702865.
|
| Bomi1521
| Histidine-rich glycoprotein
| Bos taurus
| F1MKS5
| https://www.uniprot.org/uniprot/F1MKS5
| Whey
|
|
| 536
| 60743
| https://www.uniprot.org/uniprot/F1MKS5.fasta
| HRG
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1528
| Zinc finger FYVE domain-containing protein
| Bos taurus
| F1MKY4
| https://www.uniprot.org/uniprot/F1MKY4
| Whey
|
| https://www.ncbi.nlm.nih.gov/protein/XP_002686450.1
| 1421
| 155929
| https://www.uniprot.org/uniprot/F1MKY4.fasta
| ZFYVE9
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1529
| Pleckstrin homology domain containing A7
| Bos taurus
| F1MKZ7
| https://www.uniprot.org/uniprot/F1MKZ7
| Whey
|
|
| 1203
| 136398
| https://www.uniprot.org/uniprot/F1MKZ7.fasta
| PLEKHA7
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi153
| Serum amyloid P-component
| Bos taurus
| Q3T004
| https://www.uniprot.org/uniprot/Q3T004
| Whey
| NP_001029638.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029638.1
| 224
| 25183
| https://www.uniprot.org/uniprot/Q3T004.fasta
| APCS
| 514488
| https://www.ncbi.nlm.nih.gov/gene/514488
| Reviewed: Experimental evidence at transcript level
| secreted from the liver and macrophages into the circulation
| DNA and chromatin binding protein in plasma; soluble pattern recognition receptor of the innate immune system; function to aid in the
removal of damaged tissue; regulate certain monocyte differentiation states; potentially powerful antifibrotic agent; plays role in coagulation and inflammation
| DNA and chromatin binding protein in plasma; soluble pattern recognition receptor of the innate immune system; function to aid in the
removal of damaged tissue; regulate certain monocyte differentiation states; potentially powerful antifibrotic agent; plays role in coagulation and inflammation
|
| Glycosylated; a single N-linked
biantennary oligosaccharide attached to Asn32
|
|
|
|
| 1. Xi, D., Zhao, J., Guo, K., Hu, L., Chen, H., Fu, W., … Guo, Z. (2018). Serum amyloid P component therapeutically attenuates atherosclerosis in mice via its effects on macrophages. Theranostics, 8(12), 3214–3223. https://doi.org/10.7150/thno.22704.
2. Hohenester, E., Hutchinson, W. L., Pepys, M. B., & Wood, S. P. (1997). Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. Journal of Molecular Biology, 269(4), 570–578. https://doi.org/10.1006/jmbi.1997.1075.
|
| Bomi1531
| Sterol regulatory element binding transcription factor 2
| Bos taurus
| F1ML06
| https://www.uniprot.org/uniprot/F1ML06
| Whey
|
|
| 1140
| 122519
| https://www.uniprot.org/uniprot/F1ML06.fasta
| SREBF2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi154
| Basigin
| Bos taurus
| Q3ZBX0
| https://www.uniprot.org/uniprot/Q3ZBX0
| Whey
| NP_001068839.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068839.1
| 271
| 29773
| https://www.uniprot.org/uniprot/Q3ZBX0.fasta
| BSG
| 508716
| https://www.ncbi.nlm.nih.gov/gene/508716
| Reviewed: Experimental evidence at protein level
|
| belongs to the immunoglobulin
superfamily; members of CD147 family; receptor for cyclophilins,
S100A9 and platelet glycoprotein VI; basigin-
1 serves as the receptor for the rod-derived cone
viability factor; tightly associates with monocarboxylate
transporters and is essential for their cell
surface translocation and activities; associates with other proteins
including GLUT1, CD44 and CD98; has important role in the transport of
nutrients, migration of inflammatory leukocytes and induction
of matrix metalloproteinases; important
in vision, spermatogenesis and other physiological
phenomena and plays significantly in the pathogenesis
of numerous diseases, including cancer; receptor for an invasive protein RH5, which is
present in malaria parasites; in the kidney, BSG serves as a major carrier of a
carbohydrate ligand for E-selectin, which initiates the
first step of neutrophil recruitment; has a glycan moeity that is involved in spermatogenesis; regulates endometrial tissue modelling, maintains the integrity of the uterus in bovines
| belongs to the immunoglobulin
superfamily; members of CD147 family; receptor for cyclophilins,
S100A9 and platelet glycoprotein VI; basigin-
1 serves as the receptor for the rod-derived cone
viability factor; tightly associates with monocarboxylate
transporters and is essential for their cell
surface translocation and activities; associates with other proteins
including GLUT1, CD44 and CD98; has important role in the transport of
nutrients, migration of inflammatory leukocytes and induction
of matrix metalloproteinases; important
in vision, spermatogenesis and other physiological
phenomena and plays significantly in the pathogenesis
of numerous diseases, including cancer; receptor for an invasive protein RH5, which is
present in malaria parasites; in the kidney, BSG serves as a major carrier of a
carbohydrate ligand for E-selectin, which initiates the
first step of neutrophil recruitment; has a glycan moeity that is involved in spermatogenesis; regulates endometrial tissue modelling, maintains the integrity of the uterus in bovines
|
| Members of CD147 family, EMMPRIN, basigin, 5A11/HT7 from different species, tissues or cells appear as diverse glycosylated forms, with large variation in molecular weight. Basigin in human, mouse and chicken has three Asn glycosylation sites to which
high mannose-type and complex-type glycans are
linked; High mannose-type glycans are composed
of mannose and N-acetylglucosamine, while complextype
glycans have outer chains containing sialic acid,
galactose and N-acetylglucosamine. Importantly, poly-
N-acetyllactosamine (a repeating structure of galactose
and N-acetylglucosamine) is present in an outer chain,
the so-called b1,6-branch, of BSG glycans; CD147 exhibited both high-mannose type and bi-antennary complex-type oligosaccharides; presence of β1,6-branched oligosaccharides, the sialyl Lewis X structure, namely, Galβ1, 4Fucα1,3GlcNAc, in N-glycans of CD147 ;
| affecting protein maturation and translocation to the cell membrane, facilitating oligomerization; participate in the interaction with other proteins and exert corresponding biological effects
|
|
|
| 1. Miyauchi, T., Kanekura, T., Yamaoka, A., Ozawa, M., Miyazawa, S., & Muramatsu, T. (1990). Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen. Journal of Biochemistry, 107(2), 316–323. https://doi.org/10.1093/oxfordjournals.jbchem.a123045.
2. Kato, N., Yuzawa, Y., Kosugi, T., Hobo, A., Sato, W., Miwa, Y., … Kadomatsu, K. (2009). The E-selectin ligand basigin/CD147 is responsible for neutrophil recruitment in renal ischemia/reperfusion. Journal of the American Society of Nephrology : JASN, 20(7), 1565–1576. https://doi.org/10.1681/ASN.2008090957.
3. Tang, W., Chang, S. B., & Hemler, M. E. (2004). Links between CD147 function, glycosylation, and caveolin-1. Molecular Biology of the Cell, 15(9), 4043–4050. https://doi.org/10.1091/mbc.E04-05-0402.
4. Huang, W., Luo, W.-J., Zhu, P., Tang, J., Yu, X.-L., Cui, H.-Y., … Chen, Z.-N. (2013). Modulation of CD147-induced matrix metalloproteinase activity: role of CD147 N-glycosylation. The Biochemical Journal, 449(2), 437–448. https://doi.org/10.1042/BJ20120343.
5. Miyauchi, T., Masuzawa, Y., & Muramatsu, T. (1991). The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen. Journal of Biochemistry, 110(5), 770–774. https://doi.org/10.1093/oxfordjournals.jbchem.a123657.
6. Mishra, B., Kizaki, K., Sato, T., Ito, A., & Hashizume, K. (2012). The role of extracellular matrix metalloproteinase inducer (EMMPRIN) in the regulation of bovine endometrial cell functions. Biology of Reproduction, 87(6), 149. https://doi.org/10.1095/biolreprod.112.102152.
|
| Bomi1541
| Ring finger protein 214
| Bos taurus
| F1MLH7
| https://www.uniprot.org/uniprot/F1MLH7
| Whey
|
|
| 704
| 77507
| https://www.uniprot.org/uniprot/F1MLH7.fasta
| RNF214
| 616238
| https://www.ncbi.nlm.nih.gov/gene/616238
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1547
| Myosin VIIB
| Bos taurus
| F1MLR9
| https://www.uniprot.org/uniprot/F1MLR9
| Whey
| XP_010800120.1
| https://www.ncbi.nlm.nih.gov/protein/XP_010800120.1
| 2140
| 244771
| https://www.uniprot.org/uniprot/F1MLR9.fasta
| MYO7B
| 522053
| https://www.ncbi.nlm.nih.gov/gene/522053
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi155
| Zinc-alpha-2-glycoprotein
| Bos taurus
| Q3ZCH5
| https://www.uniprot.org/uniprot/Q3ZCH5
| Whey
| NP_001029503.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029503.1
| 299
| 33852
| https://www.uniprot.org/uniprot/Q3ZCH5.fasta
| AZGP1
| 508800
| https://www.ncbi.nlm.nih.gov/gene/508800
| Reviewed: Experimental evidence at transcript level
| serum, cerebrospinal fluid, urine, saliva,sweat, semen, amniotic fluid
| Stimulate lipolysis; potential biomarker for several carcinomas; has RNAse activity; regulation of melanin production; hinder tumor proliferation; transport of nephritic by-products; has important role in fertilization
| Stimulate lipolysis; potential biomarker for several carcinomas; has RNAse activity; regulation of melanin production; hinder tumor proliferation; transport of nephritic by-products; has important role in fertilization
| Regulates lipid metabolism during lactation
| Glycosylated; typical N-linked biantennary structure,substituted with N-acetylneuraminic acid in a 2,6 linkage and lacks fucose; 4 putative glycosylation sites; Asn 89, 92,106, 239; Asn 89,106, 239 carry glucosamines; Asn 239 is heavilly silalylated on mannose 2,6 arm;
|
|
|
|
| 1. Hirai, K., Hussey, H. J., Barber, M. D., Price, S. A., and Tisdale, M. J. (1998) Biological evaluation of a lipid-mobilizing factor isolated from the urine of cancer patients. Cancer Res. 58, 2359–2365.
2. Bao, Y., Bing, C., Hunter, L., Jenkins, J. R., Wabitsch, M., and Trayhurn, P. (2005) Zinc-α 2 -glycoprotein, a lipid mobilizing factor, is expressed and secreted by human (SGBS) adipocytes. FEBS Lett. 579, 41–47.
3. Frenette, G., Dubé, J. Y., Lazure, C., Paradis, G., Chrétien, M., and Tremblay, R. R. (1987) The major 40-kDa glycoprotein in human prostatic fluid is identical to Zn-alpha 2-glycoprotein. Prostate 11, 257–270.
4. Schwick, H. G. and Haupt, H. (1981) Purified human plasma proteins of unknown function. Jpn. J. Med. Sci. Biol. 34, 299–327.
5. Ohkubo, I., Niwa, M., Takashima, A., Nishikimi, N., Gasa, S., and Sasaki, M. (1990) Human seminal plasma Zn-alpha 2-glycoprotein: its purification and properties as compared with human plasma Zn-alpha 2-glycoprotein. Biochim. Biophys. Acta 1034, 152–156.
6. BURGI, W. and SCHMID, K. (1961) Preparation and properties of Zn-alpha 2-glycoprotein of normal human plasma. J. Biol. Chem. 236, 1066–1074.
7. Bundred, N. J., Miller, W. R., and Walker, R. A. (1987) An immunohistochemical study of the tissue distribution of the breast cyst fluid protein, zinc alpha 2 glycoprotein. Histopathology 11, 603–610.
8. Jain, S., Rajput, A., Kumar, Y., Uppuluri, N., Arvind, A. S., and Tatu, U. (2005) Proteomic analysis of urinary protein markers for accurate prediction of diabetic kidney disorder. J. Assoc. Physicians India 53, 513–520.
9. Ding, M., Umetsu, K., Nakayashiki, N., Choi, W. Y., Jia, J., and Suzuki, T. (1990) Distribution of Human Zn-Alpha-2-Glycoprotein Types in Chinese and Korean Populations. Hum. Hered. 40, 311–312.
10. Freije, J. P., Fueyo, A., Uría, J. A., Velasco, G., Sánchez, L. M., López-Boado, Y. S., and López-Otín, C. (1993) Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes. Genomics 18, 575–587.
11. Ueyama, H., Naitoh, H., and Ohkubo, I. (1994) Structure and expression of rat and mouse mRNAs for Zn-alpha 2-glycoprotein. J. Biochem. 116, 677–681.
12. Fueyo, A., Uría, J. A., Freije, J. M., and López-Otín, C. (1994) Cloning and expression analysis of the cDNA encoding rat Zn-alpha 2-glycoprotein. Gene 145, 245–249.
13. Araki, T., Gejyo, F., Takagaki, K., Haupt, H., Schwick, H. G., Bürgi, W., Marti, T., Schaller, J., Rickli, E., and Brossmer, R. (1988) Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens. Proc. Natl. Acad. Sci. U. S. A. 85, 679–683.
14. Karpenko, V., Kaupová, M., and Kodícek, M. (1997) The conformation and stability of human Zn-alpha 2-glycoprotein in aqueous and methanolic solutions. Biophys. Chem. 69, 209–217.
|
| Bomi1551
| Kinectin 1
| Bos taurus
| F1MLU7
| https://www.uniprot.org/uniprot/F1MLU7
| Whey
|
|
| 1302
| 150587
| https://www.uniprot.org/uniprot/F1MLU7.fasta
| KTN1
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1555
| Ig-like domain-containing protein
| Bos taurus
| F1MLW7
| https://www.uniprot.org/uniprot/F1MLW7
| Whey, MFGM, Exosome
|
|
| 139
| 14635
| https://www.uniprot.org/uniprot/F1MLW7.fasta
|
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi156
| Cathepsin L2
| Bos taurus
| Q5E998
| https://www.uniprot.org/uniprot/Q5E998
| Whey
|
|
| 334
| 37393
| https://www.uniprot.org/uniprot/Q5E998.fasta
| CTSV
|
|
| Reviewed: Experimental evidence at transcript level
| Ubiquitously expressed, highly expressed in osteoclasts;
| e regulation of cell-cycle progression; proteolytic processing of the N-terminus of
the histone H3 tail; cleaves elastin; special role in bone resorption under normal and pathological
conditions
| e regulation of cell-cycle progression; proteolytic processing of the N-terminus of
the histone H3 tail; cleaves elastin; special role in bone resorption under normal and pathological
conditions
|
|
|
|
|
|
| 1. Turk, B., Bieth, J. G., Björk, I., Dolenc, I., Turk, D., Cimerman, N., … Turk, V. (1995). Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins. Biological Chemistry Hoppe-Seyler, 376(4), 225–230. https://doi.org/10.1515/bchm3.1995.376.4.225.
2. Turk, B., Dolenc, I., Turk, V., & Bieth, J. G. (1993). Kinetics of the pH-induced Inactivation of Human Cathepsin L. Biochemistry, 32(1), 375–380. https://doi.org/10.1021/bi00052a046.
3. Hervé-Grépinet, V., Veillard, F., Godat, E., Heuzé-Vourc’h, N., Lecaille, F., & Lalmanach, G. (2008). Extracellular catalase activity protects cysteine cathepsins from inactivation by hydrogen peroxide. FEBS Letters, 582(9), 1307–1312. https://doi.org/10.1016/j.febslet.2008.03.007.
|
| Bomi1563
| Sulfhydryl oxidase
| Bos taurus
| F1MM32
| https://www.uniprot.org/uniprot/F1MM32
| Whey, MFGM, Exosome
|
|
| 608
| 67021
| https://www.uniprot.org/uniprot/F1MM32.fasta
| QSOX1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi157
| Cofilin -1
| Bos taurus
| Q5E9F7
| https://www.uniprot.org/uniprot/Q5E9F7
| Whey
| NP_001015655.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001015655.1
| 166
| 18519
| https://www.uniprot.org/uniprot/Q5E9F7.fasta
| CFL1
| 534553
| https://www.ncbi.nlm.nih.gov/gene/534553
| Reviewed: Experimental evidence at transcript level
|
| Regulates actin cytoskeleton dynamics; Important for normal progress through mitosis and normal cytokinesis; Plays a role in the regulation of cell morphology and cytoskeletal organization; required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation; Required for neural tube morphogenesis and neural crest cell migration
| Regulates actin cytoskeleton dynamics; Important for normal progress through mitosis and normal cytokinesis; Plays a role in the regulation of cell morphology and cytoskeletal organization; required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation; Required for neural tube morphogenesis and neural crest cell migration
| Upregulated in intramammary infection during S. uberis challenge
| Cofilin oxidation leads to formation of intramolecular disulfide bonds and to dephosphorylation at Ser3 ; phosphorylation at Ser3 for role in actin filament dynamics
| cofilin requires dephosphorylation of an N-terminal serine and deprotonation of a C-terminal histidine for increased activity
|
|
|
| 1. Mudaliar, M., Tassi, R., Thomas, F. C., McNeilly, T. N., Weidt, S. K., McLaughlin, M., … Zadoks, R. N. (2016). Mastitomics, the integrated omics of bovine milk in an experimental model of Streptococcus uberis mastitis: 2. Label-free relative quantitative proteomics. Molecular BioSystems, 12(9), 2748–2761. https://doi.org/10.1039/c6mb00290k.
2. Klemke, M., Wabnitz, G. H., Funke, F., Funk, B., Kirchgessner, H., & Samstag, Y. (2008). Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions. Immunity, 29(3), 404–413. https://doi.org/10.1016/j.immuni.2008.06.016.
3. Klamt, F., Zdanov, S., Levine, R. L., Pariser, A., Zhang, Y., Zhang, B., … Shacter, E. (2009). Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nature Cell Biology, 11(10), 1241–1246. https://doi.org/10.1038/ncb1968.
|
| Bomi1573
| Ciliary rootlet coiled-coil, rootletin family member 2
| Bos taurus
| F1MMB4
| https://www.uniprot.org/uniprot/F1MMB4
| Whey, Exosome
|
|
| 1432
| 159610
| https://www.uniprot.org/uniprot/F1MMB4.fasta
| CROCC2
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1575
| X-ray repair cross complementing 6
| Bos taurus
| F1MMD5
| https://www.uniprot.org/uniprot/F1MMD5
| Whey
| NP_001179175.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179175.1
| 612
| 70476
| https://www.uniprot.org/uniprot/F1MMD5.fasta
|
| 510132
| https://www.ncbi.nlm.nih.gov/gene/510132
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi158
| Lysozyme C, milk isozyme
| Bos taurus
| Q6B411
| https://www.uniprot.org/uniprot/Q6B411
| Whey
| NP_001071297.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001071297.1
| 148
| 16783
| https://www.uniprot.org/uniprot/Q6B411.fasta
| LYZ1
| 281287
| https://www.ncbi.nlm.nih.gov/gene/281287
| Reviewed: Experimental evidence at transcript level
| tears, saliva, milk, mucus
| antimicrobial
activity; catalyses the hydrolysis of
glycosidic bonds of mucopolysaccharides in bacterial
cell walls; immune-regulatory activities,
inactivation of certain viruses; antiinflammatory; antitumour
| antimicrobial
activity; catalyses the hydrolysis of
glycosidic bonds of mucopolysaccharides in bacterial
cell walls; immune-regulatory activities,
inactivation of certain viruses; antiinflammatory; antitumour
| role of fighting infections in breastfeeding infants; natural antimicrobial agent;
|
|
|
|
|
| 1. Ozturkoglu-Budak, S. (2018). Effect of different treatments on the stability of lysozyme, lactoferrin and β-lactoglobulin in donkey’s milk. International Journal of Dairy Technology, 71(1), 36–45. https://doi.org/10.1111/1471-0307.12380.
2. Chandan, R. C., Parry, R. M., & Shahani, K. M. (1965). Purification and some properties of bovine milk lysozyme. Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 110(2), 389–398. https://doi.org/10.1016/S0926-6593(65)80046-7.
|
| Bomi1583
| Cilia and flagella associated protein 57
| Bos taurus
| F1MMP2
| https://www.uniprot.org/uniprot/F1MMP2
| Whey, Exosome
|
|
| 1266
| 147180
| https://www.uniprot.org/uniprot/F1MMP2.fasta
| CFAP57
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1585
| Spectrin alpha, erythrocytic 1
| Bos taurus
| F1MMQ8
| https://www.uniprot.org/uniprot/F1MMQ8
| Whey, MFGM, Exosome
| NP_001193517.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193517.1
| 2411
| 280957
| https://www.uniprot.org/uniprot/F1MMQ8.fasta
| SPTA1
| 505122
| https://www.ncbi.nlm.nih.gov/gene/505122
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1589
| Centrosomal protein 112
| Bos taurus
| F1MMT4
| https://www.uniprot.org/uniprot/F1MMT4
| Whey, MFGM
|
|
| 293
| 33571
| https://www.uniprot.org/uniprot/F1MMT4.fasta
| CEP112
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi159
| Alpha-2-macroglobulin
| Bos taurus
| Q7SIH1
| http://www.uniprot.org/uniprot/Q7SIH1
| Whey
| NP_001103265.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001103265.1
| 1510
| 167576
| http://www.uniprot.org/uniprot/Q7SIH1.fasta
| A2M
| 513856
| https://www.ncbi.nlm.nih.gov/gene/513856
| Reviewed: Experimental evidence at protein level
| Serum, plasma, inflammatory synovial fluid, cerebrospinal fluid, saliva, urine
| Protease inhibitory activity; inhibits the excessive protease activity in the human body fluids, plays an important role in regulation of hormones, growth factors and
physiological activity;
| Protease inhibitory activity; inhibits the excessive protease activity in the human body fluids, plays an important role in regulation of hormones, growth factors and
physiological activity;
| Acute phase proteins; levels elevate in mastitic milk; prevents clotting of mastitic milk by inhibiting renin
| Glycosylayted; 4 identical subunits have 8-N glycosylated sites in each subunit as found in humans;
|
| 1ayo
|
|
| 1. Perez, M. D., Sanchez, L., Aranda, P., Sala, F. J., and Calvo, M. (1989) Time-course levels of alpha 2-macroglobulin and albumin in cow colostrum and milk and alpha 2-macroglobulin levels in mastitic cow milk. Ann. Rech. Vet. 20, 251–258.
2. 1. Chuang, W.-H., Liu, P.-C., Hung, C.-Y., and Lee, K.-K. (2014) Purification, characterization and molecular cloning of alpha-2-macroglobulin in cobia, Rachycentron canadum. Fish Shellfish Immunol. 41, 346–355.
3. 1. Paiva, M. M., Soeiro, M. N. C., Barbosa, H. S., Meirelles, M. N. L., Delain, E., and Araújo-Jorge, T. C. (2010) Glycosylation patterns of human alpha2-macroglobulin: Analysis of lectin binding by electron microscopy. Micron 41, 666–673.
4. 1. Buresova, V., Hajdusek, O., Franta, Z., Sojka, D., and Kopacek, P. (2009) IrAM—An α2-macroglobulin from the hard tick Ixodes ricinus: Characterization and function in phagocytosis of a potential pathogen Chryseobacterium indologenes. Dev. Comp. Immunol. 33, 489–498.
5. 1. Sheikh, A. M., Chauhan, V., Tsiouris, J. A., Mehta, P. D., Burguess, K., Fenko, M. D., Spivack, W., Vaughan, M., and Malik, M. (2003) Elevated levels of serum alpha(2) macroglobulin in wild black bears during hibernation. Biochimie 85, 1027–1032.
|
| Bomi1591
| Histone-lysine N-methyltransferase
| Bos taurus
| F1MMY4
| https://www.uniprot.org/uniprot/F1MMY4
| Whey
|
|
| 1365
| 151244
| https://www.uniprot.org/uniprot/F1MMY4.fasta
| NSD2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi16
| Alpha-2-antiplasmin
| Bos taurus
| P28800
| https://www.uniprot.org/uniprot/P28800
| Whey
| NP_777095.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777095.1
| 492
| 54711
| https://www.uniprot.org/uniprot/P28800.fasta
| SERPINF2
| 282522
| https://www.ncbi.nlm.nih.gov/gene/282522
| Reviewed: Experimental evidence at protein level
| synthesized and secreted by the liver, kidney and brain;
| primary inhibitor of fibrinolysis, inhibiting plasmin directly; facilitates tissue repai
| primary inhibitor of fibrinolysis, inhibiting plasmin directly; facilitates tissue repai
| presence in milk control proteolysis
caused by the plasmin system in dairy products
| Human α 2-antiplasmin Glycosylated; 11% to 14% carbohydrate (four
putative N-linked glycosylation sites at asparagine residues 99, 268,
282, and 289) and a sulfated tyrosine residue at position 457; contains 1 disulfide bridge (between the cysteine
residues in positions 43 and 116; 70% of circulating protein is N-terminally cleaved between the proline residue at
position 12 and the asparagine residue at position 13; 30% circulatates with a methionine (Met) residue at the N terminus;
| Posttranslational modifications of the 2
termini of a2AP constitute major regulatory mechanisms for the
inhibitory function of the protein; N-terminal cleavage leads to
increased crosslinking of a2AP to fibrin, and C-terminal cleavage
leads to loss of its plasmin inhibitory capacity
|
| Defeciency increases fibrinolysis; leads to severe bleeding with hemophilialike
bleeding symptoms
|
| 1. Leebeek, F. W., Stibbe, J., Knot, E. A., Kluft, C., Gomes, M. J., & Beudeker, M. (1988). Mild haemostatic problems associated with congenital heterozygous alpha 2-antiplasmin deficiency. Thrombosis and Haemostasis, 59(1), 96–100. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/3363537.
2. Moroi, M., & Aoki, N. (1976). Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. The Journal of Biological Chemistry, 251(19), 5956–5965. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/134998.
3. WIMAN, B., & COLLEN, D. (1977). Purification and Characterization of Human Antiplasmin, the Fast‐Acting Plasmin Inhibitor in Plasma. European Journal of Biochemistry, 78(1), 19–26. https://doi.org/10.1111/j.1432-1033.1977.tb11709.
4. Wiman, B., Lijnen, H. R., & Collen, D. (1979). On the specific interaction between the lysine-binding sites in plasmin and complementary sites in α2-antiplasmin and in fibrinogen. BBA - Protein Structure, 579(1), 142–154. https://doi.org/10.1016/0005-2795(79)90094-1.
5. Lijnen, H. R., Van Hoef, B., & Collen, D. (1981). On the role of the carbohydrate side chains of human plasminogen in its interaction with alpha 2-antiplasmin and fibrin. European Journal of Biochemistry, 120(1), 149–154. https://doi.org/10.1111/j.1432-1033.1981.tb05682.
6. Hortin, G., Fok, K. F., Toren, P. C., & Strauss, A. W. (1987). Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin. The Journal of Biological Chemistry, 262(7), 3082–3085. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/2434496.
7. Lee, K. N., Jackson, K. W., Christiansen, V. J., Chung, K. H., & McKee, P. A. (2004). A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion. Blood, 103(10), 3783–3788. https://doi.org/10.1182/blood-2003-12-4240.
8. Christensen, S., Valnickova, Z., Thogersen, I. B., Olsen, E. H., & Enghild, J. J. (1997). Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties. The Biochemical Journal, 323 ( Pt 3), 847–852. https://doi.org/10.1042/bj3230847.
|
| Bomi160
| Collectin-46
| Bos taurus
| Q8MHZ9
| https://www.uniprot.org/uniprot/Q8MHZ9
| Whey
| NP_001001856.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001001856.1
| 371
| 37445
| https://www.uniprot.org/uniprot/Q8MHZ9.fasta
| CL46
| 415114
| https://www.ncbi.nlm.nih.gov/gene/415114
| Reviewed: Experimental evidence at transcript level
| dominant
place of CL-46 expression is the thymus; also present in liver
and moderate expression was detected in the mammary
gland and in tissues throughout the digestive
system
| involved in the innate immune defense; bind to microbial surface carbohydrates
inducing aggregation and, thereby, impeding infectivity; binds to the
collectin receptor (C1qR) localized on many types of cells identified as a surface variant of calreticulin; show antiviral activities towards influenza A virus and rotaviruses ; displays protective activity against bacterial infections
| involved in the innate immune defense; bind to microbial surface carbohydrates
inducing aggregation and, thereby, impeding infectivity; binds to the
collectin receptor (C1qR) localized on many types of cells identified as a surface variant of calreticulin; show antiviral activities towards influenza A virus and rotaviruses ; displays protective activity against bacterial infections
| provide the first line of
defence against these microbes
| Potential
N-glycosylation site is localized at asparagine 90 in the
collagen-like region
|
|
|
|
| 1. Nissen, A., Andersen, P. H., Bendixen, E., Ingvartsen, K. L., and Røntved, C. M. (2017) Colostrum and milk protein rankings and ratios of importance to neonatal calf health using a proteomics approach. J. Dairy Sci. 100, 2711–2728.
2. Lu, J. (1997) Collectins: Collectors of microorganisms for the innate immune system. BioEssays 19, 509–518.
3. Hansen, S., Holm, D., Moeller, V., Vitved, L., Bendixen, C., Reid, K. B. M., Skjoedt, K., and Holmskov, U. (2002) CL-46, a novel collectin highly expressed in bovine thymus and liver. J. Immunol. 169, 5726–5734.
4. Holmskov, U., Laursen, S. B., Malhotra, R., Wiedemann, H., Timpl, R., Stuart, G. R., Tornøe, I., Madsen, P. S., Reid, K. B., and Jensenius, J. C. (1995) Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Biochem. J. 305 ( Pt 3), 889–896.
5. Lim, B. L., Willis, A. C., Reid, K. B., Lu, J., Laursen, S. B., Jensenius, J. C., and Holmskov, U. (1994) Primary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-D. J. Biol. Chem. 269, 11820–11824.
6. Haurum, J. S., Thiel, S., Haagsman, H. P., Laursen, S. B., Larsen, B., and Jensenius, J. C. (1993) Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: mannan-binding protein and conglutinin. Biochem. J. 293 ( Pt 3), 873–878.
7. Holmskov, U., Teisner, B., Willis, A. C., Reid, K. B., and Jensenius, J. C. (1993) Purification and characterization of a bovine serum lectin (CL-43) with structural homology to conglutinin and SP-D and carbohydrate specificity similar to mannan-binding protein. J. Biol. Chem. 268, 10120–10125.
8. Loveless, R. W., Holmskov, U., and Feizi, T. (1995) Collectin-43 is a serum lectin with a distinct pattern of carbohydrate recognition. Immunology 85, 651–659.
|
| Bomi1601
| Centrosomal protein 164
| Bos taurus
| F1MNI1
| https://www.uniprot.org/uniprot/F1MNI1
| Whey, Exosome
|
|
| 1442
| 162153
| https://www.uniprot.org/uniprot/F1MNI1.fasta
| CEP164
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1602
| Zinc finger protein 507
| Bos taurus
| F1MNI3
| https://www.uniprot.org/uniprot/F1MNI3
| Whey
| NP_001193127.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193127.1
| 953
| 105128
| https://www.uniprot.org/uniprot/F1MNI3.fasta
| ZNF507
| 540613
| https://www.ncbi.nlm.nih.gov/gene/540613
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1609
| Ectonucleotide pyrophosphatase/phosphodiesterase 1
| Bos taurus
| F1MNS5
| https://www.uniprot.org/uniprot/F1MNS5
| Whey
| NP_001193141.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193141.1
| 924
| 104388
| https://www.uniprot.org/uniprot/F1MNS5.fasta
| ENPP1
| 615535
| https://www.ncbi.nlm.nih.gov/gene/615535
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi161
| Mucin 15
| Bos taurus
| Q8MI01
| https://www.uniprot.org/uniprot/Q8MI01
| Whey
| NP_788804.1
| https://www.ncbi.nlm.nih.gov/protein/NP_788804.1
| 280
| 30239
| https://www.uniprot.org/uniprot/Q8MI01-2.fasta
| MUC15
| 337919
| https://www.ncbi.nlm.nih.gov/gene/337919
| Reviewed: Experimental evidence at protein level
| mammary gland, lungs, lymph nodes
| protection
of epithelial surfaces, immune responses, adhesion,
inflammation, tumor genesis
| protection
of epithelial surfaces, immune responses, adhesion,
inflammation, tumor genesis
| associated with the milk fat globule
membrane; function as a protective
mucin, perhaps as a coconstituent with gel-forming mucins
in mucus, or it may act at the apical cell surfaces as a ligand
for other cell surface molecules
| Heavily O-glycosylated; glycans are composed
of fucose, galactose, mannose, N-acetylgalactosamine,
N-acetylglycosamine, and sialic acid; hybrid-type N-glycans - sialylated and contain terminal
poly-lactosamine structures; O-linked glycans
were found to constitute some unsubstituted Core-
1 structures and a substantial number of sialylated
Core-1 O-linked glycans; complex
O-glycans contain high amounts N-acetylglucosamine
residues and a small subset of is decorated with lactosamine on their
terminal ends
| dense glycosylation in the mucin
domain may primarily be to change the biophysical
properties of the mucin; mucin glycans provide
protective barriers, provide lubrication because of
their water-binding capacity, and change the overall
structure of the glycosylated region into an extended
conformation
|
|
|
| 1. Pallesen, L. T., Berglund, L., Rasmussen, L. K., Petersen, T. E., & Rasmussen, J. T. (2002). Isolation and characterization of MUC15, a novel cell membrane-associated mucin. European Journal of Biochemistry, 269(11), 2755–2763. https://doi.org/10.1046/j.1432-1033.2002.02949.
2. Pallesen, L. T., Pedersen, L. R. L., Petersen, T. E., & Rasmussen, J. T. (2007). Characterization of carbohydrate structures of bovine MUC15 and distribution of the mucin in bovine milk. Journal of Dairy Science, 90(7), 3143–3152. https://doi.org/10.3168/jds.2007-0082.
|
| Bomi1617
| Phospholipid-transporting ATPase
| Bos taurus
| F1MP29
| https://www.uniprot.org/uniprot/F1MP29
| Whey
|
|
| 1167
| 134098
| https://www.uniprot.org/uniprot/F1MP29.fasta
| LOC516849
| 516849
| https://www.ncbi.nlm.nih.gov/gene/516849
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1618
| Forkhead associated phosphopeptide binding domain 1
| Bos taurus
| F1MP58
| https://www.uniprot.org/uniprot/F1MP58
| Whey, Exosome
|
|
| 1434
| 164824
| https://www.uniprot.org/uniprot/F1MP58.fasta
| FHAD1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1619
| HMG box domain-containing protein
| Bos taurus
| F1MP59
| https://www.uniprot.org/uniprot/F1MP59
| Whey
|
|
| 356
| 41417
| https://www.uniprot.org/uniprot/F1MP59.fasta
|
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi162
| Mucin 1
| Bos taurus
| Q8WML4
| https://www.uniprot.org/uniprot/Q8WML4
| Whey
| NP_776540.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776540.1
| 580
| 58092
| https://www.uniprot.org/uniprot/Q8WML4.fasta
| MUC1
| 281333
| https://www.ncbi.nlm.nih.gov/gene/281333
| Reviewed: Experimental evidence at protein level
| mammary, salivary,
lung, pancreas, kidney and stomach
| integral membrane component; glycosylated molecule of MUCl on the surface of epithelia
presents a physical barrier protecting the cell; anti-invasion characteristics;roles as a growth inhibitor; at
digestion;protecting membrane proteins from protease action;being a large, extended
membrane protein, it may shield other nearby residents.
| integral membrane component; glycosylated molecule of MUCl on the surface of epithelia
presents a physical barrier protecting the cell; anti-invasion characteristics;roles as a growth inhibitor; at
digestion;protecting membrane proteins from protease action;being a large, extended
membrane protein, it may shield other nearby residents.
| MUCl may
be a factor regulating size of MFGs, membrane secretion,
and fat content of milk; sialic acid of mucins on MFGs prevent their clumping and
clogging the ducts through which they must pass
| glycoprotein; 50% carbohydrate, 30% of which was sialic acid; polymorphic and
carbohydrate portion is of variable nature; serine and
threonine hydroxyls provide sites for glycosylation; human milk MUC1 has high galactose,
modest level of sialic acid, and lack of detectable mannose; bovine MUC1 has less
galactose, significant mannose and much higher sialic acid; galactose
and N-acetylglucosamine are the dominant sugars in the
human mucin; O-linked oligosaccharides
are comprised of a core unit attached to MUCl via
N-acetylgalactosamine, a backbone, and a terminal region; The core and backbone may be branched and the ends may
be terminated by sialic acid, galactose, fucose or N-acetylgalactosamine;
Sulfation may also occur at the periphery;
| The oligosaccharides carry
substantial sialic acid at their termini and this accounts for
two putative functions of this mucin, i.e., to keep ducts and
lumens open by creating a strong negative charge on the
surface of epithelial cells which would repel opposite sides
of a vessel, and to bind certain pathogenic microorganisms; sialic acid content in terminal positions on oligosaccharides
of the mucin confers a negative charge to the
extracellular surface,that might prevent wall to
wall adherence in lumens and ducts thus preventing their
closure and preserving the integrity of secretory systems
|
|
|
| 1. Patton, S., Huston, G. E., Jenness, R., & Vaucher, Y. (1989). Differences between individuals in high-molecular weight glycoproteins from mammary epithelia of several species. BBA - Biomembranes, 980(3), 333–338. https://doi.org/10.1016/0005-2736(89)90321-0.
2. Schroten, H., Hanisch, F. G., Plogmann, R., Hacker, J., Uhlenbruck, G., Nobis-Bosch, R., & Wahn, V. (1992). Inhibition of adhesion of S-fimbriated Escherichia coli to buccal epithelial cells by human milk fat globule membrane components: a novel aspect of the protective function of mucins in the nonimmunoglobulin fraction. Infection and Immunity, 60(7), 2893–2899. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1377184.
3. Mather, I. H., & Keenan, T. W. (1975). Studies on the structure of milk fat globule membrane. The Journal of Membrane Biology, 21(1–2), 65–85. https://doi.org/10.1007/bf01941062.
|
| Bomi1620
| Uncharacterized protein (Fragment)
| Bos taurus
| F1MP77
| https://www.uniprot.org/uniprot/F1MP77
| Whey
|
|
| 522
| 60802
| https://www.uniprot.org/uniprot/F1MP77.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1621
| DNA methyltransferase 3 alpha
| Bos taurus
| F1MPD5
| https://www.uniprot.org/uniprot/F1MPD5
| Whey
|
|
| 946
| 106408
| https://www.uniprot.org/uniprot/F1MPD5.fasta
| DNMT3A
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1622
| CD109 molecule
| Bos taurus
| F1MPE1
| https://www.uniprot.org/uniprot/F1MPE1
| Whey, MFGM, Exosome
|
|
| 1441
| 160967
| https://www.uniprot.org/uniprot/F1MPE1.fasta
| CD109
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi163
| Lactadherin
| Bos taurus
| Q95114
| http://www.uniprot.org/uniprot/Q95114
| Whey
| NP_788783.1
| https://www.ncbi.nlm.nih.gov/protein/NP_788783.1
| 427
| 47411
| http://www.uniprot.org/uniprot/Q95114.fasta
| MFGE8
| 281913
| https://www.ncbi.nlm.nih.gov/gene/281913
| Reviewed: Experimental evidence at protein level
| serum, urine, cerebrospinal fluid
| Involved in phagocytosis, angiogenesis, atherosclerosis, tissue remodeling, blood coagulation processes and haemostasis regulation; modulate function as a cell adhesion protein in the
connection of smooth muscles to fibers in arteries; can inhibit enzymes engaged in coagulation processes such
as prothrombinase, factor X, and VIIa; expressed on the acrosomal cap of sperm and helps in fusion with oocyte
| Involved in phagocytosis, angiogenesis, atherosclerosis, tissue remodeling, blood coagulation processes and haemostasis regulation; modulate function as a cell adhesion protein in the
connection of smooth muscles to fibers in arteries; can inhibit enzymes engaged in coagulation processes such
as prothrombinase, factor X, and VIIa; expressed on the acrosomal cap of sperm and helps in fusion with oocyte
| Lines phospholipid bilayer of MFG and stabilises the bilipid structure;
| Glycosylated; contained galactose, N-acetylgalactosamine and fucose, and which was 0-
linked to Ser9 in PAS-6 and to Thr16 in PAS-7 as detected in bovine MFG; N and O-glycosylated depending on different isoforms found in mouse mammary gland
|
| 2pqs, 3bn6
|
|
| 1. Oshima, K., Aoki, N., Negi, M., Kishi, M., Kitajima, K., and Matsuda, T. (1999) Lactation-Dependent Expression of an mRNA Splice Variant with an Exon for a MultiplyO-Glycosylated Domain of Mouse Milk Fat Globule Glycoprotein MFG-E8. Biochem. Biophys. Res. Commun. 254, 522–528.
2. Hvarregaard, J., Andersen, M. H., Berglund, L., Rasmussen, J. T., and Petersen, T. E. (1996) Characterization of glycoprotein PAS-6/7 from membranes of bovine milk fat globules. Eur. J. Biochem. 240, 628–636.
3. Shi, J., Heegaard, C. W., Rasmussen, J. T., and Gilbert, G. E. (2004) Lactadherin binds selectively to membranes containing phosphatidyl-L-serine and increased curvature. Biochim. Biophys. Acta 1667, 82–90.
4. Silvestre, J.-S., Théry, C., Hamard, G., Boddaert, J., Aguilar, B., Delcayre, A., Houbron, C., Tamarat, R., Blanc-Brude, O., Heeneman, S., Clergue, M., Duriez, M., Merval, R., Lévy, B., Tedgui, A., Amigorena, S., and Mallat, Z. (2005) Lactadherin promotes VEGF-dependent neovascularization. Nat. Med. 11, 499–506.
5. Shi, J. and Gilbert, G. E. (2003) Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites. Blood 101, 2628–2636.
6. Gilbert, G. E., Novakovic, V. A., Shi, J., Rasmussen, J., and Pipe, S. W. (2015) Platelet binding sites for factor VIII in relation to fibrin and phosphatidylserine. Blood 126, 1237–1244
|
| Bomi1630
| GRAM domain containing 1B
| Bos taurus
| F1MPQ7
| https://www.uniprot.org/uniprot/F1MPQ7
| Whey
|
|
| 945
| 109101
| https://www.uniprot.org/uniprot/F1MPQ7.fasta
| GRAMD1B
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1631
| Uncharacterized protein (Fragment)
| Bos taurus
| F1MPT5
| https://www.uniprot.org/uniprot/F1MPT5
| Whey, MFGM, Exosome
|
|
| 3697
| 418957
| https://www.uniprot.org/uniprot/F1MPT5.fasta
| DST
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1634
| Transient receptor potential cation channel subfamily M member 1
| Bos taurus
| F1MPU3
| https://www.uniprot.org/uniprot/F1MPU3
| Whey
|
|
| 767
| 89673
| https://www.uniprot.org/uniprot/F1MPU3.fasta
| TRPM1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1635
| Scaffold protein involved in DNA repair
| Bos taurus
| F1MPV0
| https://www.uniprot.org/uniprot/F1MPV0
| Whey
|
|
| 940
| 103198
| https://www.uniprot.org/uniprot/F1MPV0.fasta
| SPIDR
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1636
| 8-oxoguanine DNA glycosylase
| Bos taurus
| F1MPV2
| https://www.uniprot.org/uniprot/F1MPV2
| Whey
| NP_001073754.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001073754.2
| 347
| 38974
| https://www.uniprot.org/uniprot/F1MPV2.fasta
| OGG1
| 520497
| https://www.ncbi.nlm.nih.gov/gene/520497
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi164
| Plasma serine protease inhibitor
| Bos taurus
| Q9N2I2
| https://www.uniprot.org/uniprot/Q9N2I2
| Whey
| NP_788819.1
| https://www.ncbi.nlm.nih.gov/protein/NP_788819.1
| 404
| 45297
| https://www.uniprot.org/uniprot/Q9N2I2.fasta
| SERPINA5
| 338050
| https://www.ncbi.nlm.nih.gov/gene/338050
| Reviewed: Experimental evidence at protein level
|
| Also known as protein C inhicitor; potent inhibitor of blood coagulation and fibrinolysis; inhibits proteases involved in fertilization; regulation of lung remodeling, tissue regeneration, vascular
permeability, proteolysis in the kidney and tumor cell invasion; diverse roles in the thrombosis and hemostasis in
multiple organs and tissues of a variety of species; regulates mammal fertilization; Bovine PCI inhibits bovine
plasmin, but not human plasmin, which cleaves bovine PCI
as well as human PCI at the reactive site
| Also known as protein C inhicitor; potent inhibitor of blood coagulation and fibrinolysis; inhibits proteases involved in fertilization; regulation of lung remodeling, tissue regeneration, vascular
permeability, proteolysis in the kidney and tumor cell invasion; diverse roles in the thrombosis and hemostasis in
multiple organs and tissues of a variety of species; regulates mammal fertilization; Bovine PCI inhibits bovine
plasmin, but not human plasmin, which cleaves bovine PCI
as well as human PCI at the reactive site
| inhibit kallikrein
| single-chain glycoprotein; five putative glycosylation sites: three
Asn-X-Ser/Thr sequences and two Thr/Ser-X-X-Pro.
|
| 3B9F
|
|
| 1. España, F., Berrettini, M., & Griffin, J. H. (1989). Purification and characterization of plasma protein C inhibitor. Thrombosis Research, 55(3), 369–384. https://doi.org/10.1016/0049-3848(89)90069-8.
2. H., Y., H., T., T., H., T., W., H., N., J., N., … Suzuki, K. (2000). Bovine protein c inhibitor has a unique reactive site and can transiently inhibit plasmin. Thrombosis and Haemostasis, 83(2), 262–267. Retrieved from http://ovidsp.ovid.com/ovidweb.cgi?T=JS&PAGE=reference&D=emed7&NEWS=N&AN=30093230.
3. Kuhn, L. A., Griffin, J. H., Fisher, C. L., Greengard, J. S., Bouma, B. N., España, F., & Tainer, J. A. (1990). Elucidating the structural chemistry of glycosaminoglycan recognition by protein C inhibitor. Proceedings of the National Academy of Sciences of the United States of America, 87(21), 8506–8510. https://doi.org/10.1073/pnas.87.21.8506.
|
| Bomi1641
| Lysine demethylase 5A
| Bos taurus
| F1MQ59
| https://www.uniprot.org/uniprot/F1MQ59
| Whey, Exosome
|
|
| 1636
| 186175
| https://www.uniprot.org/uniprot/F1MQ59.fasta
| KDM5A
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1644
| ATRX, chromatin remodeler
| Bos taurus
| F1MQ85
| https://www.uniprot.org/uniprot/F1MQ85
| Whey
|
|
| 2478
| 281459
| https://www.uniprot.org/uniprot/F1MQ85.fasta
| ATRX
| 514473
| https://www.ncbi.nlm.nih.gov/gene/514473
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1649
| Zinc finger DBF-type containing 2
| Bos taurus
| F1MQG4
| https://www.uniprot.org/uniprot/F1MQG4
| Whey, Exosome
|
|
| 2420
| 274065
| https://www.uniprot.org/uniprot/F1MQG4.fasta
| ZDBF2
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi165
| Serpin A3-1
| Bos taurus
| Q9TTE1
| https://www.uniprot.org/uniprot/Q9TTE1
| Whey
| NP_777193.2
| https://www.ncbi.nlm.nih.gov/protein/NP_777193.2
| 411
| 46237
| https://www.uniprot.org/uniprot/Q9TTE1.fasta
| SERPINA3-1
| 286804
| https://www.ncbi.nlm.nih.gov/gene/286804
| Reviewed: Experimental evidence at protein level
| hepatocytes, bronchial epithelial cells
neuronal cells
| bovine plasma trypsin inhibitor; potent serine protease inhibitor with action against trypsin as well as elastase; serpin antiprotease α1-antichymotrypsin ; acute
phase plasma protease inhibitor; regulation
of proteases released by leukocytes during an
inflammatory response; role in blood clotting cascade, apoptosis and
chromatin condensation
| bovine plasma trypsin inhibitor; potent serine protease inhibitor with action against trypsin as well as elastase; serpin antiprotease α1-antichymotrypsin ; acute
phase plasma protease inhibitor; regulation
of proteases released by leukocytes during an
inflammatory response; role in blood clotting cascade, apoptosis and
chromatin condensation
| inhibit chymotrypsin, has a higher specificity for chymotrypsin than α1-antichymotrypsin
|
|
|
|
|
| 1. Hwang, S. R., Steineckert, B., Kohn, A., Palkovits, M., & Hook, V. Y. (1999). Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer’s disease brains. Comparison of act in hippocampus and liver. The Journal of Biological Chemistry, 274(3), 1821–1827. https://doi.org/10.1074/jbc.274.3.1821.
2. Cichy, J., Potempa, J., Chawla, R. K., & Travis, J. (1995). Regulation of alpha 1-antichymotrypsin synthesis in cells of epithelial origin. FEBS Letters, 359(2–3), 262–266. https://doi.org/10.1016/0014-5793(95)00064-g.
3. Chandra, T., Stackhouse, R., Kidd, V. J., Robson, K. J. H., & Woo, S. L. C. (1983). Sequence Homology between Human α1-Antichymotrypsin, α1-Antitrypsin, and Antithrombin III. Biochemistry, 22(22), 5055–5061. https://doi.org/10.1021/bi00291a001.
|
| Bomi1651
| Engulfment and cell motility 1
| Bos taurus
| F1MQH0
| https://www.uniprot.org/uniprot/F1MQH0
| Whey, Exosome
| NP_001106698.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001106698.1
| 727
| 83862
| https://www.uniprot.org/uniprot/F1MQH0.fasta
| ELMO1
| 509821
| https://www.ncbi.nlm.nih.gov/gene/509821
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1655
| Nebulin
| Bos taurus
| F1MQI3
| https://www.uniprot.org/uniprot/F1MQI3
| Whey, MFGM, Exosome
|
|
| 6638
| 769918
| https://www.uniprot.org/uniprot/F1MQI3.fasta
| NEB
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi166
| Ras-related C3 botulinum toxin substrate 2
| Bos taurus
| Q9TU25
| https://www.uniprot.org/uniprot/Q9TU25
| Whey
| NP_786986.1
| https://www.ncbi.nlm.nih.gov/protein/NP_786986.1
| 192
| 21424
| https://www.uniprot.org/uniprot/Q9TU25.fasta
| RAC2
| 327671
| https://www.ncbi.nlm.nih.gov/gene/327671
| Reviewed: Experimental evidence at transcript level
| Rac1 and Rac3 are ubiquitously expressed and therefore
regulate a wide variety of cellular processes, whereas Rac2 is predominantly
expressed in cells of the hematopoietic lineage; Rac1b was
discovered in human tumors;
| act as molecular switches cycling
between an active GTP‐bound and an inactive GDP‐bound form through
nucleotide exchange and hydrolysis; three distinct
mammalian Rac isoforms, Rac1, 2 and 3, share a very high sequence identity; Rac2 is proposed to be responsible for the regulation of the
oxidative burst in hematopoietic cells; serum‐inducible and hyperactive in breast cancer cells;
| act as molecular switches cycling
between an active GTP‐bound and an inactive GDP‐bound form through
nucleotide exchange and hydrolysis; three distinct
mammalian Rac isoforms, Rac1, 2 and 3, share a very high sequence identity; Rac2 is proposed to be responsible for the regulation of the
oxidative burst in hematopoietic cells; serum‐inducible and hyperactive in breast cancer cells;
|
|
|
|
|
|
| 1. Jordan, P., Brazão, R., Boavida, M. G., Gespach, C., & Chastre, E. (1999). Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene, 18(48), 6835–6839. https://doi.org/10.1038/sj.onc.1203233.
2. Haeusler, L. C., Blumenstein, L., Stege, P., Dvorsky, R., & Ahmadian, M. R. (2003). Comparative functional analysis of the Rac GTPases. FEBS Letters, 555(3), 556–560. https://doi.org/10.1016/S0014-5793(03)01351-6.
3. Fiegen, D., Haeusler, L.-C., Blumenstein, L., Herbrand, U., Dvorsky, R., Vetter, I. R., & Ahmadian, M. R. (2004). Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase. The Journal of Biological Chemistry, 279(6), 4743–4749. https://doi.org/10.1074/jbc.M310281200.
4. Haataja, L., Groffen, J., & Heisterkamp, N. (1997). Characterization of RAC3, a novel member of the Rho family. The Journal of Biological Chemistry, 272(33), 20384–20388. https://doi.org/10.1074/jbc.272.33.20384.
|
| Bomi1664
| RRM domain-containing protein
| Bos taurus
| F1MRB9
| https://www.uniprot.org/uniprot/F1MRB9
| Whey, Exosome
|
|
| 1160
| 131065
| https://www.uniprot.org/uniprot/F1MRB9.fasta
| NOL8
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1666
| Pecanex 2
| Bos taurus
| F1MRE3
| https://www.uniprot.org/uniprot/F1MRE3
| Whey
| XP_002698836.1
| https://www.ncbi.nlm.nih.gov/protein/XP_002698836.1
| 2119
| 234964
| https://www.uniprot.org/uniprot/F1MRE3.fasta
| PCNX2
| 528971
| https://www.ncbi.nlm.nih.gov/gene/528971
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1667
| Uncharacterized protein (Fragment)
| Bos taurus
| F1MRG4
| https://www.uniprot.org/uniprot/F1MRG4
| Whey
|
|
| 1274
| 141611
| https://www.uniprot.org/uniprot/F1MRG4.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi167
| Perilipin-2
| Bos taurus
| Q9TUM6
| https://www.uniprot.org/uniprot/Q9TUM6
| Whey
| NP_776405.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776405.1
| 447
| 49102
| https://www.uniprot.org/uniprot/Q9TUM6.fasta
| PLIN2
| 280981
| https://www.ncbi.nlm.nih.gov/gene/280981
| Reviewed: Experimental evidence at transcript level
| adipose and steroidogenic tissue
| Transport proteins involved in lipid synthesis; mediate milk lipid formation and secretion; close correlation between full-length perilipin 2
expression and cytoplasmic lipid droplet accumulation is found
| Transport proteins involved in lipid synthesis; mediate milk lipid formation and secretion; close correlation between full-length perilipin 2
expression and cytoplasmic lipid droplet accumulation is found
| related to milk-component synthesis- can be associated with
the protection of the mammary gland; involved in mik lipid formation
| phosphorylated
| phosphorylation of perilipin is required for the translocation of hormone-sensitive lipase from the cytosol to the lipid droplet surface
|
|
|
| 1. Zhang, L., Boeren, S., Hageman, J. A., van Hooijdonk, T., Vervoort, J., & Hettinga, K. (2015). Perspective on calf and mammary gland development through changes in the bovine milk proteome over a complete lactation. Journal of Dairy Science, 98(8), 5362–5373. https://doi.org/10.3168/jds.2015-9342.
2. Russell, T. D., Palmer, C. A., Orlicky, D. J., Bales, E. S., Chang, B. H.-J., Chan, L., & McManaman, J. L. (2008). Mammary glands of adipophilin-null mice produce an amino-terminally truncated form of adipophilin that mediates milk lipid droplet formation and secretion. Journal of Lipid Research, 49(1), 206–216. https://doi.org/10.1194/jlr.M700396-JLR200.
3. Nielsen, R. L., Andersen, M. H., Mabhout, P., Berglund, L., Petersen, T. E., & Rasmussen, J. T. (1999). Isolation of adipophilin and butyrophilin from bovine milk and characterization of a cDNA encoding adipophilin. Journal of Dairy Science, 82(12), 2543–2549. https://doi.org/10.3168/jds.S0022-0302(99)75508-6.
4. Xu, G., Sztalryd, C., Lu, X., Tansey, J. T., Gan, J., Dorward, H., … Londos, C. (2005). Post-translational regulation of adipose differentiation-related protein by the ubiquitin/proteasome pathway. The Journal of Biological Chemistry, 280(52), 42841–42847. https://doi.org/10.1074/jbc.M506569200.
5. Najt, C. P., Lwande, J. S., McIntosh, A. L., Senthivinayagam, S., Gupta, S., Kuhn, L. A., & Atshaves, B. P. (2014). Structural and functional assessment of perilipin 2 lipid binding domain(s). Biochemistry, 53(45), 7051–7066. https://doi.org/10.1021/bi500918m.
|
| Bomi1672
| Utrophin
| Bos taurus
| F1MRT9
| https://www.uniprot.org/uniprot/F1MRT9
| Whey, MFGM, Exosome
|
|
| 3432
| 394083
| https://www.uniprot.org/uniprot/F1MRT9.fasta
| UTRN
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1674
| Dynein axonemal heavy chain 3
| Bos taurus
| F1MRU4
| https://www.uniprot.org/uniprot/F1MRU4
| Whey, Exosome
|
|
| 3131
| 356446
| https://www.uniprot.org/uniprot/F1MRU4.fasta
| DNAH3
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1679
| Proto-oncogene tyrosine-protein kinase receptor Ret
| Bos taurus
| F1MS00
| https://www.uniprot.org/uniprot/F1MS00
| Whey, MFGM, Exosome
|
|
| 1114
| 123980
| https://www.uniprot.org/uniprot/F1MS00.fasta
| RET
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1680
| PHD finger protein 21A
| Bos taurus
| F1MS13
| https://www.uniprot.org/uniprot/F1MS13
| Whey
|
|
| 682
| 74827
| https://www.uniprot.org/uniprot/F1MS13.fasta
| PHF21A
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1688
| Uncharacterized protein
| Bos taurus
| F1MSA4
| https://www.uniprot.org/uniprot/F1MSA4
| Whey
| NP_001179884.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179884.1
| 909
| 102924
| https://www.uniprot.org/uniprot/F1MSA4.fasta
| RAD54B
| 533414
| https://www.ncbi.nlm.nih.gov/gene/533414
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi169
| Serpin A3-3
| Bos taurus
| Q3ZEJ6
| https://www.uniprot.org/uniprot/Q3ZEJ6
| Whey
| NP_001033293.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001033293.1
| 411
| 46326
| https://www.uniprot.org/uniprot/Q3ZEJ6.fasta
| SERPINA3-3
| 615103
| https://www.ncbi.nlm.nih.gov/gene/615103
| Reviewed: Experimental evidence at protein level
| hepatocytes, intestinal epithelial cells,
neutrophils, lung epithelial cells, macrophages, human serum, saliva, tears, milk, semen, urine
and bile
| antiprotease α1-antitrypsin; acute phase protein; major serine protease inhibitor of human serum; protectsthe fragile connective tissue of the lower
respiratory tract from the uncontrolled proteolysis triggered by
neutrophils during inflammation; has inhibitory properties with immunomodulatory and antiinflammatory
activities against neutrophils, macrophages and
other cell types; modulates
neutrophil chemotaxis in response to soluble immune
complexes by inhibiting ADAM-17 activity
| antiprotease α1-antitrypsin; acute phase protein; major serine protease inhibitor of human serum; protectsthe fragile connective tissue of the lower
respiratory tract from the uncontrolled proteolysis triggered by
neutrophils during inflammation; has inhibitory properties with immunomodulatory and antiinflammatory
activities against neutrophils, macrophages and
other cell types; modulates
neutrophil chemotaxis in response to soluble immune
complexes by inhibiting ADAM-17 activity
| inhibits thrombin activity
|
|
|
|
|
| 1. Chowanadisai, W., & Lönnerdal, B. (2002). Alpha(1)-antitrypsin and antichymotrypsin in human milk: origin, concentrations, and stability. The American Journal of Clinical Nutrition, 76(4), 828–833. https://doi.org/10.1093/ajcn/76.4.828.
2. Huang, C.-M. (2004). Comparative proteomic analysis of human whole saliva. Archives of Oral Biology, 49(12), 951–962. https://doi.org/10.1016/j.archoralbio.2004.06.003.
3. Luo, L.-Y., & Jiang, W. (2006). Inhibition profiles of human tissue kallikreins by serine protease inhibitors. Biological Chemistry, 387(6), 813–816. https://doi.org/10.1515/BC.2006.103.
4. Zhang, B., Lu, Y., Campbell-Thompson, M., Spencer, T., Wasserfall, C., Atkinson, M., & Song, S. (2007). Alpha1-antitrypsin protects beta-cells from apoptosis. Diabetes, 56(5), 1316–1323. https://doi.org/10.2337/db06-1273.
5. Petrache, I., Fijalkowska, I., Medler, T. R., Skirball, J., Cruz, P., Zhen, L., … Tuder, R. M. (2006). alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis. The American Journal of Pathology, 169(4), 1155–1166. https://doi.org/10.2353/ajpath.2006.060058.
6. Bergin, D. A., Reeves, E. P., Meleady, P., Henry, M., McElvaney, O. J., Carroll, T. P., … McElvaney, N. G. (2010). α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8. The Journal of Clinical Investigation, 120(12), 4236–4250. https://doi.org/10.1172/JCI41196.
|
| Bomi1694
| Agrin
| Bos taurus
| F1MSI2
| https://www.uniprot.org/uniprot/F1MSI2
| Whey, MFGM, Exosome
|
|
| 2062
| 218428
| https://www.uniprot.org/uniprot/F1MSI2.fasta
| AGRN
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1698
| UDP-glucose glycoprotein glucosyltransferase 2
| Bos taurus
| F1MSL9
| https://www.uniprot.org/uniprot/F1MSL9
| Whey
|
|
| 1450
| 166848
| https://www.uniprot.org/uniprot/F1MSL9.fasta
| UGGT2
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi17
| Ezrin
| Bos taurus
| P31976
| https://www.uniprot.org/uniprot/P31976
| Whey
| NP_776642.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776642.1
| 581
| 68760
| https://www.uniprot.org/uniprot/P31976.fasta
| EZR
| 281574
| https://www.ncbi.nlm.nih.gov/gene/281574
| Reviewed: Experimental evidence at protein level
| localized at the plasma membrane in actin-rich surface structures such as microvilli, membrane ruffles, and lamellipodia in gut cells, lymphocytes,
hepatocytes, spermatozoids, fibroblasts and in a variety of other cell types
| Member of ERM proteins; morphogenesis, cancer metastasis and
virus infection; establishment of cell polarity, cell
motility and cell signaling; linkers between the plasma membrane and the
cortical actin cytoskeleton; crucial molecule in the dissemination of two
pediatric tumors, rhabdomyosarcoma and osteosarcoma; overexpression increased migration of metastatic melanoma; interaction with podocalyxin increase the invasiveness of cancer cells; involved in the functional localization of PKA; regulates
the structure of the cortical cytoskeleton to control cell surface
topography
| Member of ERM proteins; morphogenesis, cancer metastasis and
virus infection; establishment of cell polarity, cell
motility and cell signaling; linkers between the plasma membrane and the
cortical actin cytoskeleton; crucial molecule in the dissemination of two
pediatric tumors, rhabdomyosarcoma and osteosarcoma; overexpression increased migration of metastatic melanoma; interaction with podocalyxin increase the invasiveness of cancer cells; involved in the functional localization of PKA; regulates
the structure of the cortical cytoskeleton to control cell surface
topography
| maintainence of 3 dimensional structure of matrix which is required in both cell survival and differentiation has been well documented for mammary gland epithelial cells
| Phosphorylated; C-terminal threonine phosphorylation
| Phosphorylation of ezrin is required for both conformational activation and for signaling to downstream events
|
| originally purified from the microfilament bundle of
isolated intestinal microvilli, yet the native protein possessed
no convincing F-actin binding activity
|
| 1. Algrain, M., Turunen, O., Vaheri, A., Louvard, D., & Arpin, M. (1993). Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. The Journal of Cell Biology, 120(1), 129–139. https://doi.org/10.1083/jcb.120.1.129.
2. Dransfield, D. T., Bradford, A. J., Smith, J., Martin, M., Roy, C., Mangeat, P. H., & Goldenring, J. R. (1997). Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. EMBO Journal, 16(1), 35–43. https://doi.org/10.1093/emboj/16.1.35.
3. Bretscher, A. (1983). Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. The Journal of Cell Biology, 97(2), 425–432. https://doi.org/10.1083/jcb.97.2.425.
4. Gautreau, A., Poullet, P., Louvard, D., & Arpin, M. (1999). Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway. Proceedings of the National Academy of Sciences of the United States of America, 96(13), 7300–7305. https://doi.org/10.1073/pnas.96.13.7300.
5. Srivastava, J., Elliott, B. E., Louvard, D., & Arpin, M. (2005). Src-dependent ezrin phosphorylation in adhesion-mediated signaling. Molecular Biology of the Cell, 16(3), 1481–1490. https://doi.org/10.1091/mbc.e04-08-0721
|
| Bomi1702
| Dynein axonemal heavy chain 10
| Bos taurus
| F1MSP8
| https://www.uniprot.org/uniprot/F1MSP8
| Whey, Exosome
|
|
| 4526
| 521159
| https://www.uniprot.org/uniprot/F1MSP8.fasta
| DNAH10
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1714
| Short transient receptor potential channel 5
| Bos taurus
| F1MTE6
| https://www.uniprot.org/uniprot/F1MTE6
| Whey, MFGM
| NP_001160046.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001160046.1
| 974
| 111606
| https://www.uniprot.org/uniprot/F1MTE6.fasta
| TRPC5
| 407103
| https://www.ncbi.nlm.nih.gov/gene/407103
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1715
| Doublecortin domain-containing protein
| Bos taurus
| F1MTI3
| https://www.uniprot.org/uniprot/F1MTI3
| Whey
|
|
| 435
| 49094
| https://www.uniprot.org/uniprot/F1MTI3.fasta
| DCDC1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1718
| Collagen type XXVII alpha 1 chain
| Bos taurus
| F1MTP1
| https://www.uniprot.org/uniprot/F1MTP1
| Whey
|
|
| 1823
| 183619
| https://www.uniprot.org/uniprot/F1MTP1.fasta
| COL27A1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1727
| Aminopeptidase
| Bos taurus
| F1MU34
| https://www.uniprot.org/uniprot/F1MU34
| Whey
| XP_010805927.1
| https://www.ncbi.nlm.nih.gov/protein/XP_010805927.1
| 942
| 107064
| https://www.uniprot.org/uniprot/F1MU34.fasta
| ERAP1
| 514617
| https://www.ncbi.nlm.nih.gov/gene/514617
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1732
| Sperm flagellar 2
| Bos taurus
| F1MUD3
| https://www.uniprot.org/uniprot/F1MUD3
| Whey, MFGM, Exosome
|
|
| 1703
| 195604
| https://www.uniprot.org/uniprot/F1MUD3.fasta
| SPEF2
|
|
| Unreviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1734
| Adenosine deaminase, RNA specific
| Bos taurus
| F1MUM9
| https://www.uniprot.org/uniprot/F1MUM9
| Whey
|
|
| 1149
| 127601
| https://www.uniprot.org/uniprot/F1MUM9.fasta
| ADAR
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1735
| Vesicle amine transport 1
| Bos taurus
| F1MUP9
| https://www.uniprot.org/uniprot/F1MUP9
| Whey, MFGM, Exosome
|
|
| 402
| 42830
| https://www.uniprot.org/uniprot/F1MUP9.fasta
| VAT1
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1737
| RNA helicase aquarius
| Bos taurus
| F1MUW2
| https://www.uniprot.org/uniprot/F1MUW2
| Whey
|
|
| 1472
| 169385
| https://www.uniprot.org/uniprot/F1MUW2.fasta
| AQR
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1750
| Integrin beta
| Bos taurus
| F1MVW3
| https://www.uniprot.org/uniprot/F1MVW3
| Whey
| NP_001179804.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179804.1
| 767
| 85584
| https://www.uniprot.org/uniprot/F1MVW3.fasta
| ITGB8
| 536286
| https://www.ncbi.nlm.nih.gov/gene/536286
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1758
| Cell adhesion molecule L1 like
| Bos taurus
| F1MW33
| https://www.uniprot.org/uniprot/F1MW33
| Whey, MFGM
|
|
| 1225
| 136353
| https://www.uniprot.org/uniprot/F1MW33.fasta
| CHL1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1768
| Mannose receptor C-type 1
| Bos taurus
| F1MWM8
| https://www.uniprot.org/uniprot/F1MWM8
| Whey
|
|
| 1441
| 164397
| https://www.uniprot.org/uniprot/F1MWM8.fasta
| MRC1
| 787578
| https://www.ncbi.nlm.nih.gov/gene/787578
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1770
| Cilia and flagella associated protein 58
| Bos taurus
| F1MWN8
| https://www.uniprot.org/uniprot/F1MWN8
| Whey, Exosome
|
|
| 867
| 103024
| https://www.uniprot.org/uniprot/F1MWN8.fasta
| CFAP58
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1782
| Myosin VC
| Bos taurus
| F1MX93
| https://www.uniprot.org/uniprot/F1MX93
| Whey, MFGM, Exosome
|
|
| 1742
| 203067
| https://www.uniprot.org/uniprot/F1MX93.fasta
| MYO5C
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1787
| A-kinase anchoring protein 9
| Bos taurus
| F1MXF5
| https://www.uniprot.org/uniprot/F1MXF5
| Whey, MFGM, Exosome
|
|
| 3678
| 425891
| https://www.uniprot.org/uniprot/F1MXF5.fasta
| AKAP9
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1789
| Cilia and flagella associated protein 221
| Bos taurus
| F1MXN1
| https://www.uniprot.org/uniprot/F1MXN1
| Whey
|
|
| 257
| 28897
| https://www.uniprot.org/uniprot/F1MXN1.fasta
| CFAP221
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi179
| Fibrinogen alpha
| Bos taurus
| A5PJE3
| https://www.uniprot.org/uniprot/A5PJE3
| Whey, MFGM, Exosome
|
|
| 615
| 66998
| https://www.uniprot.org/uniprot/A5PJE3.fasta
| FGA
|
|
| Unreviewed: Experimental evidence at transcript level
|
| formation of fibrin matrix that enables the movement of fibroblasts and other cells and
stimulates their production during the healing of damaged tissue
| formation of fibrin matrix that enables the movement of fibroblasts and other cells and
stimulates their production during the healing of damaged tissue
| Acute phase proteins; potential marker of mastitis
|
|
|
|
|
| 1. Tabrizi, A. D., Batavani, R. A., Rezaei, S. A., & Ahmadi, M. (2008). Fibrinogen and ceruloplasmin in plasma and milk from dairy cows with subclinical and clinical mastitis. Pakistan Journal of Biological Sciences : PJBS, 11(4), 571–576. https://doi.org/10.3923/pjbs.2008.571.576
|
| Bomi1791
| E3 SUMO-protein ligase RanBP2
| Bos taurus
| F1MXS1
| https://www.uniprot.org/uniprot/F1MXS1
| Whey
| NP_777017.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777017.1
| 3035
| 336781
| https://www.uniprot.org/uniprot/F1MXS1.fasta
| RANBP2
| 785768
| https://www.ncbi.nlm.nih.gov/gene/785768
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1792
| Cortactin binding protein 2
| Bos taurus
| F1MXS6
| https://www.uniprot.org/uniprot/F1MXS6
| Whey, Exosome
|
|
| 1633
| 177466
| https://www.uniprot.org/uniprot/F1MXS6.fasta
| CTTNBP2
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1794
| Signal induced proliferation associated 1 like 1
| Bos taurus
| F1MXV4
| https://www.uniprot.org/uniprot/F1MXV4
| Whey
| XP_005212155.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005212155.1
| 1805
| 199883
| https://www.uniprot.org/uniprot/F1MXV4.fasta
| SIPA1L1
| 787248
| https://www.ncbi.nlm.nih.gov/gene/787248
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi18
| Actin, cytoplasmic 1
| Bos taurus
| P60712
| https://www.uniprot.org/uniprot/P60712
| Whey
| NP_776404.2
| https://www.ncbi.nlm.nih.gov/protein/NP_776404.2
| 375
| 41737
| https://www.uniprot.org/uniprot/P60712.fasta
| ACTB
| 280979
| https://www.ncbi.nlm.nih.gov/gene/280979
| Reviewed: Experimental evidence at protein level
|
| essential in cell division, migration, junction
formation, chromatin remodeling, transcriptional regulation,
vesicle trafficking, and cell shape regulation; Four isoforms, αskeletal-actin,
αcardiac-actin, αsmooth-actin, and ɣ smooth-actin, are expressed
primarily in skeletal, cardiac, and smooth muscle; two isoforms, bcyto-actin and ccyto-actin are ubiquitously
expressed;
| essential in cell division, migration, junction
formation, chromatin remodeling, transcriptional regulation,
vesicle trafficking, and cell shape regulation; Four isoforms, αskeletal-actin,
αcardiac-actin, αsmooth-actin, and ɣ smooth-actin, are expressed
primarily in skeletal, cardiac, and smooth muscle; two isoforms, bcyto-actin and ccyto-actin are ubiquitously
expressed;
| Cytoskeletal proteins; found increased during infection
|
|
| 1HLU, 2BTF, 2OAN, 3U4L, 3UB5
|
| P63258,Q3ZBD2
| 1. Belyantseva, I. A., Perrin, B. J., Sonnemann, K. J., Zhu, M., Stepanyan, R., McGee, J., … Ervasti, J. M. (2009). γ-Actin is required for cytoskeletal maintenance but not development. Proceedings of the National Academy of Sciences of the United States of America, 106(24), 9703–9708. https://doi.org/10.1073/pnas.0900221106.
2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021.
2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021.
3. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13.
|
| Bomi1803
| Complement C5a anaphylatoxin
| Bos taurus
| F1MY85
| https://www.uniprot.org/uniprot/F1MY85
| Whey
| NP_001160088.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001160088.1
| 1677
| 188796
| https://www.uniprot.org/uniprot/F1MY85.fasta
| C5
| 512045
| https://www.ncbi.nlm.nih.gov/gene/512045
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1806
| Spectrin beta chain
| Bos taurus
| F1MYC9
| https://www.uniprot.org/uniprot/F1MYC9
| Whey, Exosome
| NP_001179205.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179205.1
| 2363
| 274391
| https://www.uniprot.org/uniprot/F1MYC9.fasta
| SPTBN1
| 526027
| https://www.ncbi.nlm.nih.gov/gene/526027
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1809
| Zinc finger HIT-type containing 6
| Bos taurus
| F1MYH0
| https://www.uniprot.org/uniprot/F1MYH0
| Whey, Exosome
| XP_002686331.1
| https://www.ncbi.nlm.nih.gov/protein/XP_002686331.1
| 470
| 55045
| https://www.uniprot.org/uniprot/F1MYH0.fasta
| ZNHIT6
| 505578
| https://www.ncbi.nlm.nih.gov/gene/505578
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1813
| Tripartite motif family like 2
| Bos taurus
| F1MYM5
| https://www.uniprot.org/uniprot/F1MYM5
| Whey
|
|
| 426
| 48862
| https://www.uniprot.org/uniprot/F1MYM5.fasta
| TRIML2
|
|
| Unrveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1816
| FRY microtubule binding protein
| Bos taurus
| F1MYQ7
| https://www.uniprot.org/uniprot/F1MYQ7
| Whey
| NP_001192545.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192545.1
| 3013
| 338462
| https://www.uniprot.org/uniprot/F1MYQ7.fasta
| FRY
| 507622
| https://www.ncbi.nlm.nih.gov/gene/507622
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1817
| Nitric oxide synthase
| Bos taurus
| F1MYR5
| https://www.uniprot.org/uniprot/F1MYR5
| Whey
|
|
| 1156
| 131266
| https://www.uniprot.org/uniprot/F1MYR5.fasta
| NOS2
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1825
| Lymphocyte cytosolic protein 1
| Bos taurus
| F1MYX5
| https://www.uniprot.org/uniprot/F1MYX5
| Whey, MFGM, Exosome
|
|
| 631
| 70650
| https://www.uniprot.org/uniprot/F1MYX5.fasta
| LCP1
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1827
| Trichoplein keratin filament binding
| Bos taurus
| F1MYY5
| https://www.uniprot.org/uniprot/F1MYY5
| Whey
| NP_001157498.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001157498.1
| 500
| 61002
| https://www.uniprot.org/uniprot/F1MYY5.fasta
| TCHP
| 522380
| https://www.ncbi.nlm.nih.gov/gene/522380
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1828
| Histone-lysine N-methyltransferase
| Bos taurus
| F1MYZ3
| https://www.uniprot.org/uniprot/F1MYZ3
| Whey, MFGM, Exosome
|
|
| 4903
| 534938
| https://www.uniprot.org/uniprot/F1MYZ3.fasta
| KMT2C
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1830
| Centrosomal protein 162
| Bos taurus
| F1MZ01
| https://www.uniprot.org/uniprot/F1MZ01
| Whey, Exosome
| NP_001193522.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193522.1
| 1402
| 161319
| https://www.uniprot.org/uniprot/F1MZ01.fasta
| CEP162
| 512152
| https://www.ncbi.nlm.nih.gov/gene/512152
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1836
| Leucine rich repeat and coiled-coil centrosomal protein 1
| Bos taurus
| F1MZ78
| https://www.uniprot.org/uniprot/F1MZ78
| Whey, Exosome
| NP_001193720.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193720.1
| 1027
| 118790
| https://www.uniprot.org/uniprot/F1MZ78.fasta
| LRRCC1
| 787651
| https://www.ncbi.nlm.nih.gov/gene/787651
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1848
| La ribonucleoprotein domain family member 1
| Bos taurus
| F1MZU1
| https://www.uniprot.org/uniprot/F1MZU1
| Whey
|
|
| 1097
| 123318
| https://www.uniprot.org/uniprot/F1MZU1.fasta
| LARP1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1854
| Myosin heavy chain 13
| Bos taurus
| F1MZX6
| https://www.uniprot.org/uniprot/F1MZX6
| Whey, MFGM, Exosome
|
|
| 1940
| 223761
| https://www.uniprot.org/uniprot/F1MZX6.fasta
| MYH13
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1860
| RAN binding protein 6
| Bos taurus
| F1N074
| https://www.uniprot.org/uniprot/F1N074
| Whey
| XP_002689654.2
| https://www.ncbi.nlm.nih.gov/protein/XP_002689654.2
| 1105
| 124753
| https://www.uniprot.org/uniprot/F1N074.fasta
| RANBP6
| 526705
| https://www.ncbi.nlm.nih.gov/gene/526705
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1866
| Ubiquitin specific peptidase 34
| Bos taurus
| F1N0A8
| https://www.uniprot.org/uniprot/F1N0A8
| Whey, Exosome
|
|
| 3555
| 405310
| https://www.uniprot.org/uniprot/F1N0A8.fasta
| USP34
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1868
| Tectonin beta-propeller repeat containing 2
| Bos taurus
| F1N0C0
| https://www.uniprot.org/uniprot/F1N0C0
| Whey
|
|
| 1337
| 143793
| https://www.uniprot.org/uniprot/F1N0C0.fasta
| TECPR2
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1869
| Tyrosine-protein kinase
| Bos taurus
| F1N0D6
| https://www.uniprot.org/uniprot/F1N0D6
| Whey, Exosome
| NP_001193463.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193463.1
| 1158
| 133654
| https://www.uniprot.org/uniprot/F1N0D6.fasta
| JAK1
| 537201
| https://www.ncbi.nlm.nih.gov/gene/537201
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi187
| Adenylyl cyclase-associated protein
| Bos taurus
| A6QLB7
| https://www.uniprot.org/uniprot/A6QLB7
| Whey, Exosome
| XP_005204713.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005204713.1
| 471
| 51202
| https://www.uniprot.org/uniprot/A6QLB7.fasta
| CAP1
| 504519
| https://www.ncbi.nlm.nih.gov/gene/504519
| Unreviewed: Experimental evidence at transcript level
| CAP1 is
expressed in virtually all tissues and cells, whereas CAP2
is more specific and occurs mainly in skeletal and cardiac
muscles, brain, and skin
| major function is to remodel the actin cytoskeleton; CAP proteins are involved in many cellular processes, directly or indirectly, through the regulation of actin
dynamics and the cytoskeleton remodeling processes
| major function is to remodel the actin cytoskeleton; CAP proteins are involved in many cellular processes, directly or indirectly, through the regulation of actin
dynamics and the cytoskeleton remodeling processes
| negatively regulate milk synthesis and proliferation of mammary epithelial cells via the PI3K‐mTOR/SREBP‐1c/Cyclin D1 signalling pathway
|
|
|
|
|
| 1. Xie, S., Shen, C., Tan, M., Li, M., Song, X., & Wang, C. (2017). Systematic analysis of gene expression alterations and clinical outcomes of adenylate cyclase-associated protein in cancer. Oncotarget, 8(16), 27216–27239. https://doi.org/10.18632/oncotarget.16111.
2. Hubberstey, A., Yu, G., Loewith, R., Lakusta, C., & Young, D. (1996). Mammalian CAP interacts with CAP, CAP2, and actin. Journal of Cellular Biochemistry, 61(3), 459–466. https://doi.org/10.1002/(SICI)1097-4644(19960601)61:3<459::AID-JCB13>3.0.CO;2-E.
3. Zhang, H., Ghai, P., Wu, H., Wang, C., Field, J., & Zhou, G. L. (2013). Mammalian adenylyl cyclase-associated protein 1 (CAP1) regulates cofilin function, the actin cytoskeleton, and cell adhesion. Journal of Biological Chemistry, 288(29), 20966–20977. https://doi.org/10.1074/jbc.M113.484535.
4. Jansen, S., Collins, A., Golden, L., Sokolova, O., & Goode, B. L. (2014). Structure and mechanism of mouse cyclase-associated protein (CAP1) in regulating actin dynamics. Journal of Biological Chemistry, 289(44), 30732–30742. https://doi.org/10.1074/jbc.M114.601765.
5. Yuan, X., Zhen, Z., Zhang, M., Yu, Y., Gao, X., & Ao, J.-X. (2019). Cyclase-associated protein 1 is a key negative regulator of milk synthesis and proliferation of bovine mammary epithelial cells. Cell Biochemistry and Function, 37(3), 185–192. https://doi.org/10.1002/cbf.3387.
|
| Bomi1873
| Beta-1,4-N-acetylgalactosaminyltransferase
| Bos taurus
| F1N0M7
| https://www.uniprot.org/uniprot/F1N0M7
| Whey, Exosome
|
|
| 1003
| 114243
| https://www.uniprot.org/uniprot/F1N0M7.fasta
| B4GALNT3
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi1875
| A-kinase anchoring protein 6
| Bos taurus
| F1N0Q2
| https://www.uniprot.org/uniprot/F1N0Q2
| Whey
| NP_001179852.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179852.1
| 2319
| 256130
| https://www.uniprot.org/uniprot/F1N0Q2.fasta
| AKAP6
| 537810
| https://www.ncbi.nlm.nih.gov/gene/537810
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1878
| L-serine dehydratase/L-threonine deaminase
| Bos taurus
| F1N0R8
| https://www.uniprot.org/uniprot/F1N0R8
| Whey
|
|
| 446
| 47277
| https://www.uniprot.org/uniprot/F1N0R8.fasta
| SDS
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1881
| Adenosine deaminase, RNA specific B1
| Bos taurus
| F1N0T4
| https://www.uniprot.org/uniprot/F1N0T4
| Whey
|
|
| 721
| 78806
| https://www.uniprot.org/uniprot/F1N0T4.fasta
| ADARB1
| 521761
| https://www.ncbi.nlm.nih.gov/gene/521761
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1883
| HMG-box containing 3
| Bos taurus
| F1N0X8
| https://www.uniprot.org/uniprot/F1N0X8
| Whey
|
|
| 1256
| 137187
| https://www.uniprot.org/uniprot/F1N0X8.fasta
| HMGXB3
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1884
| Uridine phosphorylase
| Bos taurus
| F1N0Y0
| https://www.uniprot.org/uniprot/F1N0Y0
| Whey, MFGM
|
|
| 500
| 52584
| https://www.uniprot.org/uniprot/F1N0Y0.fasta
| UPP1
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1886
| Complement C8 beta chain
| Bos taurus
| F1N102
| https://www.uniprot.org/uniprot/F1N102
| Whey
|
|
| 590
| 66686
| https://www.uniprot.org/uniprot/F1N102.fasta
| C8B
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1887
| Serine protease HTRA1
| Bos taurus
| F1N152
| https://www.uniprot.org/uniprot/F1N152
| Whey
| NP_001269011.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001269011.1
| 487
| 51907
| https://www.uniprot.org/uniprot/F1N152.fasta
| HTRA1
|
|
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1888
| Filamin A
| Bos taurus
| F1N169
| https://www.uniprot.org/uniprot/F1N169
| Whey, MFGM, Exosome
| NP_001193443.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193443.1
| 2674
| 280927
| https://www.uniprot.org/uniprot/F1N169.fasta
| FLNA
| 281165
| https://www.ncbi.nlm.nih.gov/gene/281165
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1892
| DExH-box helicase 57
| Bos taurus
| F1N1A2
| https://www.uniprot.org/uniprot/F1N1A2
| Whey
| NP_001192980.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192980.1
| 1383
| 155453
| https://www.uniprot.org/uniprot/F1N1A2.fasta
| DHX57
| 540993
| https://www.ncbi.nlm.nih.gov/gene/540993
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1894
| AE binding protein 1
| Bos taurus
| F1N1C7
| https://www.uniprot.org/uniprot/F1N1C7
| Whey
|
|
| 1170
| 131922
| https://www.uniprot.org/uniprot/F1N1C7.fasta
| AEBP1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1899
| Centromere protein F
| Bos taurus
| F1N1F8
| https://www.uniprot.org/uniprot/F1N1F8
| Whey, MFGM
| XP_005217426.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005217426.1
| 3259
| 374373
| https://www.uniprot.org/uniprot/F1N1F8.fasta
| CENPF
| 533089
| https://www.ncbi.nlm.nih.gov/gene/533089
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi19
| Calmodulin
| Bos taurus
| P62157
| https://www.uniprot.org/uniprot/P62157
| Whey
| NP_001039714.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001039714.1
| 149
| 16838
| https://www.uniprot.org/uniprot/P62157.fasta
| CALM
| 617095
| https://www.ncbi.nlm.nih.gov/gene/617095
| Reviewed: Experimental evidence at protein level
| bovine mammary tissue, CNS, testes,
| Calcium and calmodulin are involved in
regulation of many biochemical processes - muscle contraction, stimulussecretion
coupling, microtubule disassembly,
and several enzymatic activities; helps in large transcellular calcium flux in mammary tissue during lactation; In brain, calmodulin may function to govern
the release of neurotransmitters from vesicular
stores
| Calcium and calmodulin are involved in
regulation of many biochemical processes - muscle contraction, stimulussecretion
coupling, microtubule disassembly,
and several enzymatic activities; helps in large transcellular calcium flux in mammary tissue during lactation; In brain, calmodulin may function to govern
the release of neurotransmitters from vesicular
stores
| CaM appears to
increase prior to onset of lactation; increases in CaM during lactogenesis when
mammary epithelial cells are proliferating; increase
of calmodulin in milk with SCC greater or equal
to 1,000,000
| Trimethyllysine, which is amino acid residue 115 in beef
calmodulin, occurs as the result of posttranslational N-methylation catalyzed
by S-adenosylmethionine:calmodulin (lysine) N-methyltransferase; substrate for protein carboxylmethyltransferase; calmodulin converting
enzyme clips the carboxyl terminal lysine from calmodulin; undergoes acetylation of its N-terminal
amino acid residue (alanine)4
| calmodulin converting
enzyme causes
a change in its electrophoretic mobility
| 1A29, 1AK8, 1CDM, 1CM1, 1CM4, 1CMF, 1CMG, 1DEG, 1FW4, 1LIN, 1PRW, 1QIV, 1QIW, 1XA5, 2CLN, 2F2O, 2F2P, 2FOT, 3IF7, 6O20
| CaM
concentrations double during the G1-S phase
boundary of cell growth in CHO-K1 cell line;
|
| 1. Alston-Mills, B., Barefield, K. L., Corrado, L. J., & Douglass, L. W. (1988). Evidence of calmodulin in bovine milk with high somatic cell counts. Journal of Dairy Science, 71(8), 2246–2249. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/3170865.
2. Riss, T. L., & Baumrucker, C. R. (1982). Calmodulin purification and quantitation from bovine mammary tissue. Journal of Dairy Science, 65(9), 1722–1728. https://doi.org/10.3168/jds.S0022-0302(82)82407-7.
3. Murtaugh, T. J., Rowe, P. M., Vincent, P. L., Wright, L. S., & Siegel, F. L. (1983). Posttranslational modification of calmodulin. Methods in Enzymology, 102, 158–170. https://doi.org/10.1016/s0076-6879(83)02017-0.
4. Murtaugh, T. J., Wright, L. S., & Siegel, F. L. (1986). Posttranslational modification of calmodulin in rat brain and pituitary. Journal of Neurochemistry, 47(1), 164–172. https://doi.org/10.1111/j.1471-4159.1986.tb02845.
|
| Bomi1900
| Heparanase
| Bos taurus
| F1N1G1
| https://www.uniprot.org/uniprot/F1N1G1
| Whey
|
|
| 553
| 61990
| https://www.uniprot.org/uniprot/F1N1G1.fasta
| HPSE
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1902
| Phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1
| Bos taurus
| F1N1Q7
| https://www.uniprot.org/uniprot/F1N1Q7
| Whey
|
|
| 1653
| 185300
| https://www.uniprot.org/uniprot/F1N1Q7.fasta
| PREX1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1908
| Pancreatic adenocarcinoma upregulated factor-like
| Bos taurus
| F1N1Z8
| https://www.uniprot.org/uniprot/F1N1Z8
| Whey, MFGM, Exosome
|
|
| 155
| 16970
| https://www.uniprot.org/uniprot/F1N1Z8.fasta
| LOC104975830
| 104975830
| https://www.ncbi.nlm.nih.gov/gene/104975830
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1926
| Periplakin
| Bos taurus
| F1N2K8
| https://www.uniprot.org/uniprot/F1N2K8
| Whey, MFGM, Exosome
|
|
| 1756
| 202883
| https://www.uniprot.org/uniprot/F1N2K8.fasta
| PPL
| 522886
| https://www.ncbi.nlm.nih.gov/gene/522886
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1927
| ADAM metallopeptidase with thrombospondin type 1 motif 7
| Bos taurus
| F1N2M2
| https://www.uniprot.org/uniprot/F1N2M2
| Whey
|
|
| 1679
| 183080
| https://www.uniprot.org/uniprot/F1N2M2.fasta
| ADAMTS7
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1928
| Plexin A4
| Bos taurus
| F1N2P7
| https://www.uniprot.org/uniprot/F1N2P7
| Whey
|
|
| 1428
| 160600
| https://www.uniprot.org/uniprot/F1N2P7.fasta
| PLXNA4
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1938
| Hyaluronan mediated motility receptor
| Bos taurus
| F1N331
| https://www.uniprot.org/uniprot/F1N331
| Whey, Exosome
|
|
| 664
| 76485
| https://www.uniprot.org/uniprot/F1N331.fasta
| HMMR
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1960
| Echinoderm microtubule associated protein like 6
| Bos taurus
| F1N406
| https://www.uniprot.org/uniprot/F1N406
| Whey
| NP_001179386.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179386.1
| 1958
| 217798
| https://www.uniprot.org/uniprot/F1N406.fasta
| EML6
| 516921
| https://www.ncbi.nlm.nih.gov/gene/516921
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1969
| EMSY, BRCA2 interacting transcriptional repressor
| Bos taurus
| F1N4A6
| https://www.uniprot.org/uniprot/F1N4A6
| Whey
| XP_005216363.1
| https://www.ncbi.nlm.nih.gov/protein/XP_005216363.1
| 1337
| 142870
| https://www.uniprot.org/uniprot/F1N4A6.fasta
| EMSY
| 540919
| https://www.ncbi.nlm.nih.gov/gene/540919
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1972
| Sacsin molecular chaperone
| Bos taurus
| F1N4J2
| https://www.uniprot.org/uniprot/F1N4J2
| Whey, MFGM, Exosome
|
|
| 4.575
| 517643
| https://www.uniprot.org/uniprot/F1N4J2.fasta
| SACS
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1976
| Complement factor I
| Bos taurus
| F1N4M7
| https://www.uniprot.org/uniprot/F1N4M7
| Whey
|
|
| 610
| 68013
| https://www.uniprot.org/uniprot/F1N4M7.fasta
| CFI
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1981
| DNA helicase
| Bos taurus
| F1N506
| https://www.uniprot.org/uniprot/F1N506
| Whey
|
|
| 902
| 101409
| https://www.uniprot.org/uniprot/F1N506.fasta
| MCM2
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1982
| CD5 molecule like
| Bos taurus
| A6QNW7
| https://www.uniprot.org/uniprot/A6QNW7
| Whey, MFGM, Exosome
| NP_001095589.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001095589.1
| 451
| 50212
| https://www.uniprot.org/uniprot/A6QNW7.fasta
| CD5L
| 528593
| https://www.ncbi.nlm.nih.gov/gene/528593
| Unreveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi1987
| DLG associated protein 4
| Bos taurus
| F1N5I2
| https://www.uniprot.org/uniprot/F1N5I2
| Whey
|
|
| 989
| 107411
| https://www.uniprot.org/uniprot/F1N5I2.fasta
| DLGAP4
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi1990
| Dynein axonemal heavy chain 7
| Bos taurus
| F1N5R7
| https://www.uniprot.org/uniprot/F1N5R7
| Whey, MFGM, Exosome
| NP_001137346.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001137346.1
| 4024
| 461307
| https://www.uniprot.org/uniprot/F1N5R7.fasta
| DNAH7
| 517781
| https://www.ncbi.nlm.nih.gov/gene/517781
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2
| Antithrombin-III
| Bos taurus
| F1MSZ6
| https://www.uniprot.org/uniprot/F1MSZ6
| Whey
|
|
| 465
| 52440
| https://www.uniprot.org/uniprot/F1MSZ6.fasta
| SERPINC1
|
|
| Unreviewed: Protein inferred from homology
|
| involved in the coagulation process; inhibits serine proteases of the intrinsic coagulation
pathway such as Factor IXa, Xa and Xla and
thrombin
| involved in the coagulation process; inhibits serine proteases of the intrinsic coagulation
pathway such as Factor IXa, Xa and Xla and
thrombin
|
| Glycosylated: single chain glycoprotein; 4 glycosylation sites in human ATIII. Three
of them, Asn96, 155 and 192, have been identified in
the bovine ATIII sequence.The secreted human ATIII
contains 432 amino acids, 6 of which are cysteines that
form 3 disulfide bridges which are conserved in the
bovine protein: Cys8-Cys128, Cys21-Cys95, Cys247-
Cys430
| Antithrombin
ß, is deprived of its carbohydrate side chain at position
Asn135 and has been shown to display a higher affinity
to heparin; mutation at position 7 from Ile to Asn, which is then subject to
glycosylation, leads to a decreased affinity for heparin
|
| Functional deficiency of antithrombinIII results in a
predisposition towards thrombosis and pulmonary
embolism
|
| 1. Brennan, S. O., George, P. M., & Jordan, R. E. (1987). Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135. FEBS Letters, 219(2), 431–436. https://doi.org/10.1016/0014-5793(87)80266-1.
2. Gray, E., Hogwood, J., & Mulloy, B. (2012). The anticoagulant and antithrombotic mechanisms of heparin. Handbook of Experimental Pharmacology, 207, 43–61. https://doi.org/10.1007/978-3-642-23056-1_3.
3. Lane, D. A., & Caso, R. (1989). Antithrombin: structure, genomic organization, function and inherited deficiency. Bailliere’s Clinical Haematology, 2(4), 961–998. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/2688761.
4. Mourey, L., Samama, J. P., Delarue, M., Choay, J., Lormeau, J. C., Petitou, M., & Moras, D. (1990). Antithrombin III: structural and functional aspects. Biochimie, 72(8), 599–608. https://doi.org/10.1016/0300-9084(90)90123-x.
5. Carrell, R. W., & Owen, M. C. (n.d.). Plakalbumin, alpha 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. Nature, 317(6039), 730–732. https://doi.org/10.1038/317730a0.
|
| Bomi20
| Actin, aortic smooth muscle
| Bos taurus
| P62739
| https://www.uniprot.org/uniprot/P62739
| Whey
| NP_001029674.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029674.1
| 377
| 42009
| https://www.uniprot.org/uniprot/P62739.fasta
| ACTA2
| 515610
| https://www.ncbi.nlm.nih.gov/gene/515610
| Reviewed: Experimental evidence at protein level
|
| essential in cell division, migration, junction
formation, chromatin remodeling, transcriptional regulation,
vesicle trafficking, and cell shape regulation; Four isoforms, αskeletal-actin,
αcardiac-actin, αsmooth-actin, and ɣ smooth-actin, are expressed
primarily in skeletal, cardiac, and smooth muscle; two isoforms, bcyto-actin and ccyto-actin are ubiquitously
expressed; maintenance of the cytoskeleton, cell motility and muscle contraction
| essential in cell division, migration, junction
formation, chromatin remodeling, transcriptional regulation,
vesicle trafficking, and cell shape regulation; Four isoforms, αskeletal-actin,
αcardiac-actin, αsmooth-actin, and ɣ smooth-actin, are expressed
primarily in skeletal, cardiac, and smooth muscle; two isoforms, bcyto-actin and ccyto-actin are ubiquitously
expressed; maintenance of the cytoskeleton, cell motility and muscle contraction
| Cytoskeletal proteins; found increased during infection
|
|
|
|
| Q3ZC07
| 1. Belyantseva, I. A., Perrin, B. J., Sonnemann, K. J., Zhu, M., Stepanyan, R., McGee, J., … Ervasti, J. M. (2009). γ-Actin is required for cytoskeletal maintenance but not development. Proceedings of the National Academy of Sciences of the United States of America, 106(24), 9703–9708. https://doi.org/10.1073/pnas.0900221106.
2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021.
2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021.
3. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13.
|
| Bomi2007
| Leucine rich repeat kinase 1
| Bos taurus
| F1N6C1
| https://www.uniprot.org/uniprot/F1N6C1
| Whey, MFGM, Exosome
| NP_001192703.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192703.1
| 2015
| 224766
| https://www.uniprot.org/uniprot/F1N6C1.fasta
| LRRK1
| 513994
| https://www.ncbi.nlm.nih.gov/gene/513994
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2010
| LDL receptor related protein 2
| Bos taurus
| F1N6H1
| https://www.uniprot.org/uniprot/F1N6H1
| Whey, Exosome
|
|
| 4622
| 517231
| https://www.uniprot.org/uniprot/F1N6H1.fasta
| LRP2
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2011
| Microtubule-actin crosslinking factor 1
| Bos taurus
| F1N6H4
| https://www.uniprot.org/uniprot/F1N6H4
| Whey, MFGM, Exosome
|
|
| 7311
| 827928
| https://www.uniprot.org/uniprot/F1N6H4.fasta
| MACF1
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2014
| ANK_REP_REGION domain-containing protein
| Bos taurus
| F1N6K9
| https://www.uniprot.org/uniprot/F1N6K9
| Whey
|
|
| 314
| 34374
| https://www.uniprot.org/uniprot/F1N6K9.fasta
|
|
|
| Unreveied:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2020
| Collagen type XVIII alpha 1 chain
| Bos taurus
| F1N6W9
| https://www.uniprot.org/uniprot/F1N6W9
| Whey
|
|
| 1514
| 153952
| https://www.uniprot.org/uniprot/F1N6W9.fasta
| COL18A1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2021
| Glucosidase II alpha subunit
| Bos taurus
| F1N6Y1
| https://www.uniprot.org/uniprot/F1N6Y1
| Whey, Exosome
| NP_001192706.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192706.1
| 966
| 109472
| https://www.uniprot.org/uniprot/F1N6Y1.fasta
| GANAB
| 540155
| https://www.ncbi.nlm.nih.gov/gene/540155
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2024
| Family with sequence similarity 83 member C
| Bos taurus
| F1N708
| https://www.uniprot.org/uniprot/F1N708
| Whey
|
|
| 733
| 79816
| https://www.uniprot.org/uniprot/F1N708.fasta
| FAM83C
| 101903690
| https://www.ncbi.nlm.nih.gov/gene/101903690
| Unreveiwed:
|
|
|
|
|
|
|
|
|
|
|
| Bomi2025
| Uncharacterized protein
| Bos taurus
| F1N724
| https://www.uniprot.org/uniprot/F1N724
| Whey, MFGM, Exosome
|
|
| 4501
| 518335
| https://www.uniprot.org/uniprot/F1N724.fasta
| DNAH11
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2027
| Chromodomain helicase DNA binding protein 6
| Bos taurus
| F1N734
| https://www.uniprot.org/uniprot/F1N734
| Whey
| NP_001230229.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001230229.1
| 2721
| 304952
| https://www.uniprot.org/uniprot/F1N734.fasta
| CHD6
| 524776
| https://www.ncbi.nlm.nih.gov/gene/524776
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2028
| Lysine demethylase 2A
| Bos taurus
| F1N735
| https://www.uniprot.org/uniprot/F1N735
| Whey, MFGM
|
|
| 1185
| 135263
| https://www.uniprot.org/uniprot/F1N735.fasta
| KDM2A
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2029
| Uncharacterized protein (Fragment)
| Bos taurus
| F1N740
| https://www.uniprot.org/uniprot/F1N740
| Whey
|
|
| 3979
| 439367
| https://www.uniprot.org/uniprot/F1N740.fasta
| FRAS1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2031
| Citron rho-interacting serine/threonine kinase
| Bos taurus
| F1N747
| https://www.uniprot.org/uniprot/F1N747
| Whey, Exosome
|
|
| 2018
| 230889
| https://www.uniprot.org/uniprot/F1N747.fasta
| CIT
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi2044
| SLX4 structure-specific endonuclease subunit
| Bos taurus
| F1N7Q0
| https://www.uniprot.org/uniprot/F1N7Q0
| Whey, Exosome
|
|
| 1754
| 189476
| https://www.uniprot.org/uniprot/F1N7Q0.fasta
| SLX4
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2050
| Ras-related protein Rab-11A
| Bos taurus
| F2Z4D5
| https://www.uniprot.org/uniprot/F2Z4D5
| Whey, MFGM, Exosome
|
|
| 216
| 24394
| https://www.uniprot.org/uniprot/F2Z4D5.fasta
| RAB11A
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2051
| ARP1 actin related protein 1 homolog A
| Bos taurus
| F2Z4F0
| https://www.uniprot.org/uniprot/F2Z4F0
| Whey, Exosome
| NP_001180177.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001180177.1
| 376
| 42614
| https://www.uniprot.org/uniprot/F2Z4F0.fasta
| ACTR1A
| 514371
| https://www.ncbi.nlm.nih.gov/gene/514371
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2054
| Polymeric immunoglobulin receptor
| Bos taurus
| F1MR22
| https://www.uniprot.org/uniprot/F1MR22
| Whey, MFGM, Exosome
|
|
| 757
| 82622
| https://www.uniprot.org/uniprot/F1MR22.fasta
| PIGR
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2068
| Neuron derived neurotrophic factor
| Bos taurus
| F6QPI1
| https://www.uniprot.org/uniprot/F6QPI1
| Whey
| NP_001192787.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001192787.1
| 568
| 64430
| https://www.uniprot.org/uniprot/F6QPI1.fasta
| NDNF
| 519500
| https://www.ncbi.nlm.nih.gov/gene/519500
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2074
| Cysteine-rich secretory protein 2
| Bos taurus
| Q3ZCL0
| https://www.uniprot.org/uniprot/Q3ZCL0
| Whey, Exosome
| NP_001073103.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001073103.1
| 244
| 27453
| https://www.uniprot.org/uniprot/Q3ZCL0.fasta
| CRISP3
| 618612
| https://www.ncbi.nlm.nih.gov/gene/618612
| Unreveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2088
| Protein FAM81B
| Bos taurus
| Q0II90
| https://www.uniprot.org/uniprot/Q0II90
| Whey
| NP_001069156.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001069156.1
| 414
| 47762
| https://www.uniprot.org/uniprot/Q0II90.fasta
| FAM81B
| 514910
| https://www.ncbi.nlm.nih.gov/gene/514910
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2090
| Fatty acid-binding protein, heart
| Bos taurus
| P10790
| https://www.uniprot.org/uniprot/P10790
| Whey, MFGM, Exosome
| NP_776738.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776738.1
| 133
| 14779
| https://www.uniprot.org/uniprot/P10790.fasta
| FABP3
| 281758
| https://www.ncbi.nlm.nih.gov/gene/281758
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2098
| Fibroblast growth factor-binding protein 1
| Bos taurus
| Q9MZ06
| https://www.uniprot.org/uniprot/Q9MZ06
| Whey, Exosome
| NP_776762.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776762.1
| 234
| 26188
| https://www.uniprot.org/uniprot/Q9MZ06.fasta
| FGFBP1
| 281812
| https://www.ncbi.nlm.nih.gov/gene/281812
| Reviewed: Experimental evidence at protein level
| Detected in the digestive system, thymus, skin, hair, follicles, dental germ, respiratory tract, various glandular tissues, kidney and liver
| Secreted chaperones known to bind and mobilize paracrine FGFs from their heparan sulfate (HS) storage in the extracellular matrix; modulate FGF functions during development, tumorigenesis, tissue homeostasis and tissue repair;
| Secreted chaperones known to bind and mobilize paracrine FGFs from their heparan sulfate (HS) storage in the extracellular matrix; modulate FGF functions during development, tumorigenesis, tissue homeostasis and tissue repair;
| All cysteine residues of bovine FGF-BP are involved in disulfide bonds, suggesting that the maintenance of tertiary structure of FGF-BP in bovine prepartum mammary gland secretion
| glycosylation sites revealed the presence of glycans on Asn155 and Ser172
|
|
|
|
| 1. Lametsch R, Rasmussen JT, Johnsen LB, Purup S, Sejrsen K, Petersen TE, et al. Structural characterization of the fibroblast growth factor-binding protein purified from bovine prepartum mammary gland secretion. J Biol Chem. 2000 Jun 30;275(26):19469–74.
2. Kawakami A, Hirayama K, Kawakami F, Kawakami H, Fujihara M, Ohtsuki K. Purification and biochemical characterization of a fibroblast growth factor-binding protein (FGF-BP) from the lactoferrin fraction of bovine milk. Biochim Biophys Acta - Gen Subj. 2006 Mar;1760(3):421–31.
|
| Bomi21
| Actin, alpha skeletal muscle
| Bos taurus
| P68138
| https://www.uniprot.org/uniprot/P68138
| Whey
| NP_776650.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776650.1
| 377
| 42051
| https://www.uniprot.org/uniprot/P68138.fasta
| ACTA1
| 281592
| https://www.ncbi.nlm.nih.gov/gene/281592
| Reviewed: Experimental evidence at protein level
|
| maintenance of the cytoskeleton, cell motility and muscle contraction
| maintenance of the cytoskeleton, cell motility and muscle contraction
| Cytoskeletal proteins; found increased during infection
|
|
|
|
| Q5E9B5
| 1. Belyantseva, I. A., Perrin, B. J., Sonnemann, K. J., Zhu, M., Stepanyan, R., McGee, J., … Ervasti, J. M. (2009). γ-Actin is required for cytoskeletal maintenance but not development. Proceedings of the National Academy of Sciences of the United States of America, 106(24), 9703–9708. https://doi.org/10.1073/pnas.0900221106.
2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021.
2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021.
3. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13.
|
| Bomi210
| Disintegrin and metalloproteinase domain-containing protein 10
| Bos taurus
| Q10741
| https://www.uniprot.org/uniprot/Q10741
| Whey, Exosome
| NP_776921.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776921.1
| 748
| 84188
| https://www.uniprot.org/uniprot/Q10741.fasta
| ADAM10
| 282132
| https://www.ncbi.nlm.nih.gov/gene/282132
| Reviewed: Experimental evidence at protein level
| detected in secreted vesicles
identified as exosomes;
| metalloproteinases; regulate the bioavailability of adhesion
molecules and ligands to various cellularsignaling
receptors; functions include:
(i) collagen processing as procollagen N-proteinase; (ii) cleavage
of the matrix proteoglycans aggrecan, versican and brevican;
(iii) inhibition of angiogenesis; and (iv) blood coagulation homoeostasis
as the von Willebrand factor cleaving protease; involved in the intramembrane
proteolysis process, whereby it mediates ectodomain shedding of
various membrane-bound receptors, adhesion molecules, growth
factors, and cytokines; involved in the
regulation of the shedding of Notch, HER-2, CD44, IL-6 receptor,
amyloid precursor protein, and cadherins; modulates the activation status of various cellularsignaling
pathways that have an impact on cellular responses such
as proliferation and migration;
| metalloproteinases; regulate the bioavailability of adhesion
molecules and ligands to various cellularsignaling
receptors; functions include:
(i) collagen processing as procollagen N-proteinase; (ii) cleavage
of the matrix proteoglycans aggrecan, versican and brevican;
(iii) inhibition of angiogenesis; and (iv) blood coagulation homoeostasis
as the von Willebrand factor cleaving protease; involved in the intramembrane
proteolysis process, whereby it mediates ectodomain shedding of
various membrane-bound receptors, adhesion molecules, growth
factors, and cytokines; involved in the
regulation of the shedding of Notch, HER-2, CD44, IL-6 receptor,
amyloid precursor protein, and cadherins; modulates the activation status of various cellularsignaling
pathways that have an impact on cellular responses such
as proliferation and migration;
|
| As found in bovine ADAM 10, four potential N-glycosylation sites (N267, N278, N439 and N551); contain high-mannose and complex-type glycans; three located in the metalloprotease
domain (N267, N278 and N439) and one in the disintegrin
domain (N551)
| role in processing, stability, activity and intracellular localization of ADAM 10; N278 are important for the folding of the protein
probably mediating the interaction with calnexin; N439 glycosylation site resulted in increased
susceptibility of bADAM10 to proteases
| 5L0Q
|
|
| 1. Armanious, H., Gelebart, P., Anand, M., Belch, A., & Lai, R. (2011). Constitutive activation of metalloproteinase ADAM10 in mantle cell lymphoma promotes cell growth and activates the TNFα/NFκB pathway. Blood, 117(23), 6237–6246. https://doi.org/10.1182/blood-2010-10-313940.
2. Kuno, K., Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., & Matsushima, K. (1997). Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. The Journal of Biological Chemistry, 272(1), 556–562. https://doi.org/10.1074/jbc.272.1.556.
3. Escrevente, C., Morais, V. A., Keller, S., Soares, C. M., Altevogt, P., & Costa, J. (2008). Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme. Biochimica et Biophysica Acta, 1780(6), 905–913. https://doi.org/10.1016/j.bbagen.2008.03.004.
|
| Bomi2105
| Folate receptor alpha
| Bos taurus
| P02702
| https://www.uniprot.org/uniprot/P02702
| Whey
| NP_001193456.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193456.1
| 241
| 27922
| https://www.uniprot.org/uniprot/P02702.fasta
| FOLR1
| 516067
| https://www.ncbi.nlm.nih.gov/gene/516067
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2118
| Adhesion molecule with Ig like domain 3
| Bos taurus
| G3MX42
| https://www.uniprot.org/uniprot/G3MX42
| Whey
|
|
| 519
| 56766
| https://www.uniprot.org/uniprot/G3MX42.fasta
| AMIGO3
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2124
| Ig-like domain-containing protein
| Bos taurus
| G3MXG6
| https://www.uniprot.org/uniprot/G3MXG6
| Whey, MFGM
|
|
| 140
| 14697
| https://www.uniprot.org/uniprot/G3MXG6.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2126
| Proteinase 3
| Bos taurus
| G3MXK8
| https://www.uniprot.org/uniprot/G3MXK8
| Whey
|
|
| 256
| 27438
| https://www.uniprot.org/uniprot/G3MXK8.fasta
| PRTN3
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2127
| alpha-1,2-Mannosidase
| Bos taurus
| G3MXQ8
| https://www.uniprot.org/uniprot/G3MXQ8
| Whey
|
|
| 655
| 74109
| https://www.uniprot.org/uniprot/G3MXQ8.fasta
| MAN1B1
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi2129
| Androglobin
| Bos taurus
| G3MXR8
| https://www.uniprot.org/uniprot/G3MXR8
| Whey, Exosome
|
|
| 1631
| 186162
| https://www.uniprot.org/uniprot/G3MXR8.fasta
| ADGB
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi2140
| Zinc finger protein 292
| Bos taurus
| G3MYM4
| https://www.uniprot.org/uniprot/G3MYM4
| Whey, MFGM, Exosome
| NP_001179779.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179779.1
| 2719
| 303708
| https://www.uniprot.org/uniprot/G3MYM4.fasta
| ZNF292
| 541264
| https://www.ncbi.nlm.nih.gov/gene/541264
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2144
| Tyrosine-protein kinase receptor
| Bos taurus
| G3MYX8
| https://www.uniprot.org/uniprot/G3MYX8
| Whey
|
|
| 2123
| 237928
| https://www.uniprot.org/uniprot/G3MYX8.fasta
| ROS1
|
|
| Unreveiwed:Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi2145
| Jacalin-type lectin domain-containing protein
| Bos taurus
| G3MZ19
| https://www.uniprot.org/uniprot/G3MZ19
| Whey
|
|
| 157
| 17591
| https://www.uniprot.org/uniprot/G3MZ19.fasta
| ZG16B
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2147
| J domain-containing protein
| Bos taurus
| G3MZ88
| https://www.uniprot.org/uniprot/G3MZ88
| Whey, MFGM
| NP_001179968.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179968.1
| 223
| 25715
| https://www.uniprot.org/uniprot/G3MZ88.fasta
| DNAJB9
| 614588
| https://www.ncbi.nlm.nih.gov/gene/614588
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2148
| BCLAF1 and THRAP3 family member 3
| Bos taurus
| G3MZA4
| https://www.uniprot.org/uniprot/G3MZA4
| Whey, MFGM, Exosome
|
|
| 704
| 83234
| https://www.uniprot.org/uniprot/G3MZA4.fasta
| BCLAF3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2152
| Uncharacterized protein
| Bos taurus
| G3MZE3
| https://www.uniprot.org/uniprot/G3MZE3
| Whey, Exosome
|
|
| 2264
| 256168
| https://www.uniprot.org/uniprot/G3MZE3.fasta
|
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2153
| Uncharacterized protein
| Bos taurus
| G3MZE5
| https://www.uniprot.org/uniprot/G3MZE5
| Whey
|
|
| 1584
| 180891
| https://www.uniprot.org/uniprot/G3MZE5.fasta
|
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2166
| Matrix metallopeptidase 8
| Bos taurus
| G3N0J0
| https://www.uniprot.org/uniprot/G3N0J0
| Whey
|
|
| 470
| 53988
| https://www.uniprot.org/uniprot/G3N0J0.fasta
| MMP8
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi2168
| Discoidin, CUB and LCCL domain containing 1
| Bos taurus
| G3N0M7
| https://www.uniprot.org/uniprot/G3N0M7
| Whey
|
|
| 710
| 77797
| https://www.uniprot.org/uniprot/G3N0M7.fasta
| DCBLD1
| 100298760
| https://www.ncbi.nlm.nih.gov/gene/100298760
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2169
| Uncharacterized protein
| Bos taurus
| G3N0S9
| https://www.uniprot.org/uniprot/G3N0S9
| Whey, MFGM
|
|
| 192
| 21488
| https://www.uniprot.org/uniprot/G3N0S9.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2170
| Cyclin B3
| Bos taurus
| G3N0U2
| https://www.uniprot.org/uniprot/G3N0U2
| Whey
|
|
| 1208
| 137338
| https://www.uniprot.org/uniprot/G3N0U2.fasta
| CCNB3
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi2172
| Uncharacterized protein (Fragment)
| Bos taurus
| G3N0V0
| https://www.uniprot.org/uniprot/G3N0V0
| Whey, MFGM, Exosome
|
|
| 326
| 35952
| https://www.uniprot.org/uniprot/G3N0V0.fasta
|
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2186
| Uncharacterized protein
| Bos taurus
| G3N2H7
| https://www.uniprot.org/uniprot/G3N2H7
| Whey
|
|
| 1578
| 179833
| https://www.uniprot.org/uniprot/G3N2H7.fasta
| LOC786628
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2192
| Pleckstrin homology like domain family B member 1
| Bos taurus
| G3N336
| https://www.uniprot.org/uniprot/G3N336
| Whey, Exosome
|
|
| 1432
| 156086
| https://www.uniprot.org/uniprot/G3N336.fasta
| PHLDB1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2195
| Uncharacterized protein (Fragment)
| Bos taurus
| G3N3C5
| https://www.uniprot.org/uniprot/G3N3C5
| Whey
|
|
| 796
| 85115
| https://www.uniprot.org/uniprot/G3N3C5.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2197
| Zinc finger protein 804B
| Bos taurus
| G3N3V6
| https://www.uniprot.org/uniprot/G3N3V6
| Whey
|
|
| 1.312
| 147904
| https://www.uniprot.org/uniprot/G3N3V6.fasta
| ZNF804B
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi22
| Cathepsin D
| Bos taurus
| P80209
| https://www.uniprot.org/uniprot/P80209
| Whey
|
|
| 390
| 42491
| https://www.uniprot.org/uniprot/P80209.fasta
| CTSD
|
|
| Reviewed: Experimental evidence at protein level
| Serum, ecrine sweat, urine, major secretions of numerous types of cancer cells, ECM and synovial fluid of cartilage during pathological conditions, macrophage-rich regions of atherosclerotic lesions, human keratinocytes
| soluble lysosomal aspartic endopeptidases; role in cancer development; independent tumor marker; regulation of blood vessel formation;
| soluble lysosomal aspartic endopeptidases; role in cancer development; independent tumor marker; regulation of blood vessel formation;
| aspartic proteinase; activate neutrophils and lymphocytes as reported in human milk; regulation of surface receptirs; activation of immune systems in breast-fed infants; degardes αs1, ß- and κ-casein;
| glycoprotein with two N-linked oligosaccharides
modified with mannose 6-phosphate residues at asparagine residues 70 and 199
| Lysosomal targeting
|
| Failure of protein degradation resulted in acumulation of
lipofuscin in variety of cell types, neurodegeneration, developmental regression and
visual loss
|
| 1. Hasilik, A., & Neufeldg, E. F. (1984). Biosynthesis of Lysosomal Enzymes in Fibroblasts. The Journal of Biological Chemistry, 25(10), 4937–4945.
2. Larsen, L. B., Benfeldt, C., Rasmussen, L. K., & Petersen, T. E. (1996). Bovine milk procathepsin D and cathepsin D: coagulation and milk protein degradation. The Journal of Dairy Research, 63(1), 119–130. https://doi.org/10.1017/s0022029900031599.
3. Zühlsdorf, M., Imort, M., Hasilik, A., & von Figura, K. (1983). Molecular forms of beta-hexosaminidase and cathepsin D in serum and urine of healthy subjects and patients with elevated activity of lysosomal enzymes. The Biochemical Journal, 213(3), 733–740. https://doi.org/10.1042/bj2130733.
4. Fortenberry, S. C., Schorey, J. S., & Chirgwin, J. M. (1995). Role of glycosylation in the expression of human procathepsin D. Journal of Cell Science, 108 ( Pt 5), 2001–2006. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7657720.
5. Hasilik, A., & Neufeld, E. F. (1980). Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues. The Journal of Biological Chemistry, 255(10), 4946–4950. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/6989822.
6. Baechle, D., Flad, T., Cansier, A., Steffen, H., Schittek, B., Tolson, J., … Kalbacher, H. (2006). Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. The Journal of Biological Chemistry, 281(9), 5406–5415. https://doi.org/10.1074/jbc.M504670200.
7. Leto, G., Tumminello, F. M., Crescimanno, M., Flandina, C., & Gebbia, N. (2004). Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications. Clinical & Experimental Metastasis, 21(2), 91–106. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/15168727.
8. Hakala, J. K., Oksjoki, R., Laine, P., Du, H., Grabowski, G. A., Kovanen, P. T., & Pentikäinen, M. O. (2003). Lysosomal enzymes are released from cultured human macrophages, hydrolyze LDL in vitro, and are present extracellularly in human atherosclerotic lesions. Arteriosclerosis, Thrombosis, and Vascular Biology, 23(8), 1430–1436. https://doi.org/10.1161/01.ATV.0000077207.49221.06.
9. Vashishta, A., Saraswat Ohri, S., Vetvickova, J., Fusek, M., Ulrichova, J., & Vetvicka, V. (2007). Procathepsin D secreted by HaCaT keratinocyte cells - A novel regulator of keratinocyte growth. European Journal of Cell Biology, 86(6), 303–313. https://doi.org/10.1016/j.ejcb.2007.03.008.
|
| Bomi220
| Apolipoprotein A-IV
| Bos taurus
| Q32PJ2
| https://www.uniprot.org/uniprot/Q32PJ2
| Whey, MFGM
| NP_001032557.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001032557.1
| 380
| 43018
| https://www.uniprot.org/uniprot/Q32PJ2.fasta
| APOA4
| 537301
| https://www.ncbi.nlm.nih.gov/gene/537301
| Reviewed: Experimental evidence at transcript level
| major protein
component of chylomicrons in postprandial lymph and
plasma of both humans and rats; apoA-IV is also
found in bile and cerebrospinal fl uid
| ApoA-IV is primarily
synthesized by the small intestine, attached to chylomicrons
by enterocytes, and secreted into intestinal lymph during fat
absorption; anti-oxidative and anti-infl ammatory
properties, and because it can mediate reverse-cholesterol
transport; The presence of apoA-IV in the
blood is uniquely linked to the absorption and secretion
of dietary lipid; very important
in the integrated control of food intake, metabolism,
and glucose homeostasis
| ApoA-IV is primarily
synthesized by the small intestine, attached to chylomicrons
by enterocytes, and secreted into intestinal lymph during fat
absorption; anti-oxidative and anti-infl ammatory
properties, and because it can mediate reverse-cholesterol
transport; The presence of apoA-IV in the
blood is uniquely linked to the absorption and secretion
of dietary lipid; very important
in the integrated control of food intake, metabolism,
and glucose homeostasis
|
|
|
|
|
|
| 1. Utermann, G., & Beisiegel, U. (1979). Apolipoprotein A-IV: a protein occurring in human mesenteric lymph chylomicrons and free in plasma. Isolation and quantification. European Journal of Biochemistry, 99(2), 333–343. https://doi.org/10.1111/j.1432-1033.1979.tb13261.x.
2. Green, P. H., Glickman, R. M., Riley, J. W., & Quinet, E. (1980). Human apolipoprotein A-IV. Intestinal origin and distribution in plasma. The Journal of Clinical Investigation, 65(4), 911–919. https://doi.org/10.1172/JCI109745.
3. Borghini, I., Barja, F., Pometta, D., & James, R. W. (1995). Characterization of subpopulations of lipoprotein particles isolated from human cerebrospinal fluid. Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, 1255(2), 192–200. https://doi.org/10.1016/0005-2760(94)00232-N.
4. Karathanasis, S. K. (1985). Apolipoprotein multigene family: tandem organization of human apolipoprotein AI, CIII, and AIV genes. Proceedings of the National Academy of Sciences of the United States of America, 82(19), 6374–6378. https://doi.org/10.1073/pnas.82.19.6374.
5. Kalogeris, T. J., Fukagawa, K., & Tso, P. (1994). Synthesis and lymphatic transport of intestinal apolipoprotein A-IV in response to graded doses of triglyceride. Journal of Lipid Research, 35(7), 1141–1151. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7964177.
|
| Bomi2200
| Glyceraldehyde-3-phosphate dehydrogenase
| Bos taurus
| P10096
| https://www.uniprot.org/uniprot/P10096
| Whey, MFGM, Exosome
| NP_001029206.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029206.1
| 333
| 35868
| https://www.uniprot.org/uniprot/P10096.fasta
| GAPDH
| 281181
| https://www.ncbi.nlm.nih.gov/gene/281181
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2202
| STE20 like kinase
| Bos taurus
| G3X696
| https://www.uniprot.org/uniprot/G3X696
| Whey, Exosome
| NP_001193006.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193006.1
| 1240
| 142982
| https://www.uniprot.org/uniprot/G3X696.fasta
| SLK
| 535342
| https://www.ncbi.nlm.nih.gov/gene/535342
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2204
| FERM and PDZ domain containing 3
| Bos taurus
| G3X6D0
| https://www.uniprot.org/uniprot/G3X6D0
| Whey, Exosome
|
|
| 1738
| 190901
| https://www.uniprot.org/uniprot/G3X6D0.fasta
| FRMPD3
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2206
| Rho GTPase activating protein 42
| Bos taurus
| G3X6F7
| https://www.uniprot.org/uniprot/G3X6F7
| Whey, MFGM
|
|
| 795
| 89474
| https://www.uniprot.org/uniprot/G3X6F7.fasta
| ARHGAP42
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2208
| Uncharacterized protein (Fragment)
| Bos taurus
| G3X6I0
| https://www.uniprot.org/uniprot/G3X6I0
| Whey, MFGM
|
|
| 3001
| 318988
| https://www.uniprot.org/uniprot/G3X6I0.fasta
| FCGBP
|
|
| Unreviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2216
| Calcineurin binding protein 1
| Bos taurus
| G3X746
| https://www.uniprot.org/uniprot/G3X746
| Whey
|
|
| 2165
| 238666
| https://www.uniprot.org/uniprot/G3X746.fasta
| CABIN1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2218
| Uncharacterized protein (Fragment)
| Bos taurus
| G3X771
| https://www.uniprot.org/uniprot/G3X771
| Whey
|
|
| 1241
| 136872
| https://www.uniprot.org/uniprot/G3X771.fasta
| ABCB1
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2219
| Phosphorylase b kinase regulatory subunit
| Bos taurus
| G3X778
| https://www.uniprot.org/uniprot/G3X778
| Whey
|
|
| 1007
| 112715
| https://www.uniprot.org/uniprot/G3X778.fasta
| PHKA1
|
|
| Unreviewed: Protein inferred from homology
|
|
|
|
|
|
|
|
|
|
|
| Bomi223
| Apolipoprotein E
| Bos taurus
| Q03247
| https://www.uniprot.org/uniprot/Q03247
| Whey, MFGM, Exosome
| NP_776416.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776416.1
| 316
| 35980
| https://www.uniprot.org/uniprot/Q03247.fasta
| APOE
| 281004
| https://www.ncbi.nlm.nih.gov/gene/281004
| Reviewed: Experimental evidence at protein level
| the liver, brain, spleen,
lungs, adrenal gland, ovaries, kidneys, and muscles as found in humans
| Component of plasma lipoproteins in the transport of lipids among cells of
different organs and within specific tissues; Mediate the
binding of lipoproteins or lipid complexes in the plasma or interstitial fluids to specific cell-surface
receptors; participates in
the distribution/redistribution of lipids among various tissues and cells of the body; plays a key role in regulating the clearance of these lipoproteins from the plasma
| Component of plasma lipoproteins in the transport of lipids among cells of
different organs and within specific tissues; Mediate the
binding of lipoproteins or lipid complexes in the plasma or interstitial fluids to specific cell-surface
receptors; participates in
the distribution/redistribution of lipids among various tissues and cells of the body; plays a key role in regulating the clearance of these lipoproteins from the plasma
| Related to lipid transport; expression decreases over lactation period
| Glycosylated: human mature apolipoprotein E (ApoE) is a 299-amino acid glycoprotein
(34–37 kDa); various other PTMs include methylation, Dihydroxylation, dimethylation; four glycosylation sites (T194, T289, S290, and S296 residues) on
secreted and cellular human ApoE
| serves as a ligand for the low-density lipoprotein
(LDL) receptor (LDLR), that is involved in lipid metabolism; alter the
domain interactions, functions, binding affinities, hydrophobicity, and
structural stability of ApoE; glycation at the K75 position may impair lipoprotein-cell interactions
through heparan sulfate proteoglycans, andmay lead to enhancement
of lipid abnormalities in diabetic patients
|
|
|
| 1. Chartier-Hariln, M.-C. et al. (1994) ‘Apolipoprotein E, ɛ4 allele as a major risk factor for sporadic early and late-onset forms of Alzheimer’s disease: analysis of the 19q13.2 chromosomal region’, Human Molecular Genetics, 3(4), pp. 569–574. doi: 10.1093/hmg/3.4.569.
2. Uen, Y.-H. et al. (2015) ‘Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer’, Journal of Proteomics, 126, pp. 252–262. doi: 10.1016/j.jprot.2015.05.038.
3. Mahley, R. W. (2016) ‘Apolipoprotein E: from cardiovascular disease to neurodegenerative disorders’, Journal of Molecular Medicine, 94(7), pp. 739–746. doi: 10.1007/s00109-016-1427-y.
|
| Bomi2230
| Uncharacterized protein (Fragment)
| Bos taurus
| G5E513
| https://www.uniprot.org/uniprot/G5E513
| Whey, MFGM, Exosome
|
|
| 439
| 48107
| https://www.uniprot.org/uniprot/G5E513.fasta
|
|
|
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2233
| Protein tyrosine phosphatase, non-receptor type 7
| Bos taurus
| G5E541
| https://www.uniprot.org/uniprot/G5E541
| Whey
|
|
| 339
| 38293
| https://www.uniprot.org/uniprot/G5E541.fasta
|
|
|
| Unreviewed: Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2238
| Transaldolase
| Bos taurus
| G5E5C8
| https://www.uniprot.org/uniprot/G5E5C8
| Whey, Exosome
| NP_001030360.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001030360.2
| 337
| 37681
| https://www.uniprot.org/uniprot/G5E5C8.fasta
| TALDO1
| 513453
| https://www.ncbi.nlm.nih.gov/gene/513453
| Unreveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2242
| SET binding factor 1
| Bos taurus
| G5E5Q8
| https://www.uniprot.org/uniprot/G5E5Q8
| Whey, Exosome
|
|
| 1863
| 207810
| https://www.uniprot.org/uniprot/G5E5Q8.fasta
| SBF1
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2251
| MRG domain-containing protein
| Bos taurus
| G5E5V9
| https://www.uniprot.org/uniprot/G5E5V9
| Whey
|
|
| 231
| 26762
| https://www.uniprot.org/uniprot/G5E5V9.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2253
| Ig-like domain-containing protein
| Bos taurus
| G5E604
| https://www.uniprot.org/uniprot/G5E604
| Whey, MFGM, Exosome
|
|
| 123
| 12941
| https://www.uniprot.org/uniprot/G5E604.fasta
|
|
|
| Unreveiwed:Protein predicted
|
|
|
|
|
|
|
|
|
|
|
| Bomi2265
| Glucose-6-phosphate isomerase
| Bos taurus
| Q3ZBD7
| https://www.uniprot.org/uniprot/Q3ZBD7
| Whey, MFGM, Exosome
| NP_001035561.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001035561.1
| 557
| 62855
| https://www.uniprot.org/uniprot/Q3ZBD7.fasta
| GPI
| 280808
| https://www.ncbi.nlm.nih.gov/gene/280808
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2275
| Rab GDP dissociation inhibitor alpha
| Bos taurus
| P21856
| https://www.uniprot.org/uniprot/P21856
| Whey, Exosome
| NP_776489.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776489.1
| 447
| 50566
| https://www.uniprot.org/uniprot/P21856.fasta
| GDI1
| 281188
| https://www.ncbi.nlm.nih.gov/gene/281188
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2276
| Rab GDP dissociation inhibitor beta
| Bos taurus
| P50397
| https://www.uniprot.org/uniprot/P50397
| Whey, MFGM, Exosome
| NP_001028934.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001028934.1
| 445
| 50488
| https://www.uniprot.org/uniprot/P50397.fasta
| GDI2
| 509832
| https://www.ncbi.nlm.nih.gov/gene/509832
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2277
| Rho GDP-dissociation inhibitor 1
| Bos taurus
| P19803
| https://www.uniprot.org/uniprot/P19803
| Whey, MFGM, Exosome
| NP_788823.1
| https://www.ncbi.nlm.nih.gov/protein/NP_788823.1
| 204
| 23421
| https://www.uniprot.org/uniprot/P19803.fasta
| ARHGDIA
| 338054
| https://www.ncbi.nlm.nih.gov/gene/338054
| Reveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2278
| Rho GDP-dissociation inhibitor 2
| Bos taurus
| Q9TU03
| https://www.uniprot.org/uniprot/Q9TU03
| Whey
| NP_786991.1
| https://www.ncbi.nlm.nih.gov/protein/NP_786991.1
| 200
| 22794
| https://www.uniprot.org/uniprot/Q9TU03.fasta
| ARHGDIB
| 327676
| https://www.ncbi.nlm.nih.gov/gene/327676
| Reveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi228
| Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
| Bos taurus
| O97902
| https://www.uniprot.org/uniprot/O97902
| Whey, Exosome
| NP_787015.1
| https://www.ncbi.nlm.nih.gov/protein/NP_787015.1
| 1129
| 125382
| https://www.uniprot.org/uniprot/O97902.fasta
| ASAP1
| 327705
| https://www.ncbi.nlm.nih.gov/gene/327705
| Reviewed: Experimental evidence at protein level
| Arf GAP1, Arf GAP2 and Arf GAP3 are
found in the Golgi apparatus; GAP1 and AGAP2 are associated with endosomes
| nonredundant regulators of
specialized membrane surfaces implicated in cell migration; regulate membrane structures
that mediate cell adhesion and movement; involved in both actin and membrane remodeling; regulate membrane traffic and the actin cytoskeleton; catalyze the
hydrolysis of GTP bound to Arf proteins,
thereby converting Arf•GTP to Arf•GDP; function as an
Arf effector to regulate podosomes and invadopodia
| nonredundant regulators of
specialized membrane surfaces implicated in cell migration; regulate membrane structures
that mediate cell adhesion and movement; involved in both actin and membrane remodeling; regulate membrane traffic and the actin cytoskeleton; catalyze the
hydrolysis of GTP bound to Arf proteins,
thereby converting Arf•GTP to Arf•GDP; function as an
Arf effector to regulate podosomes and invadopodia
|
| Phosphorylated: Phosphorylation by Proline-rich tyrosine kinase 2
at tyrosine 308 and 782
| affects the phosphoinositide
binding profile of ASAP1
|
|
|
| 1. Brown, M. T. et al. (1998) ‘ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src.’, Molecular and cellular biology, 18(12), pp. 7038–51. doi: 10.1128/mcb.18.12.7038.
2. Kruljac-Letunic, A. et al. (2003) ‘The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1.’, The Journal of biological chemistry, 278(32), pp. 29560–70. doi: 10.1074/jbc.M302278200.
3. Cukierman, E. et al. (1995) ‘The ARF1 GTPase-Activating Protein: Zinc Finger Motif and Golgi Complex Localization’, Science, 270(5244), pp. 1999–2002. doi: 10.1126/science.270.5244.1999.
4. Bharti, S. et al. (2007) ‘Src-dependent phosphorylation of ASAP1 regulates podosomes.’, Molecular and cellular biology, 27(23), pp. 8271–83. doi: 10.1128/MCB.01781-06.
|
| Bomi2282
| Glycosylation-dependent cell adhesion molecule 1
| Bos taurus
| P80195
| https://www.uniprot.org/uniprot/P80195
| Whey, MFGM, Exosome
| NP_777253.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777253.1
| 153
| 17152
| https://www.uniprot.org/uniprot/P80195.fasta
| GLYCAM1
| 282430
| https://www.ncbi.nlm.nih.gov/gene/282430
| Reviewed: Experimental evidence at protein level
| Expressed specifically by the endothelial cells of peripheral and mesenteric lymph nodes; expressed during lactation by mammary epithelial cells
| Mucin-like endothelial glycoprotein that acts as an adhesive ligand for L selectin by presenting one or more O-linked carbohydrates to the lectin domain of this leukocyte cell surface selectin;
| Mucin-like endothelial glycoprotein that acts as an adhesive ligand for L selectin by presenting one or more O-linked carbohydrates to the lectin domain of this leukocyte cell surface selectin;
|
|
|
|
|
|
| 1. Dowbenko D, Kikuta A, Fennie C, Gillett N, Lasky LA. Glycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) mucin is expressed by lactating mammary gland epithelial cells and is present in milk. J Clin Invest. 1993;92(2):952–60.
|
| Bomi2289
| Glucosidase 2 subunit beta
| Bos taurus
| Q28034
| https://www.uniprot.org/uniprot/Q28034
| Whey
| NP_788835.1
| https://www.ncbi.nlm.nih.gov/protein/NP_788835.1
| 533
| 60151
| https://www.uniprot.org/uniprot/Q28034.fasta
| PRKCSH
| 338067
| https://www.ncbi.nlm.nih.gov/gene/338067
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi23
| Xanthine dehydrogenase/oxidase
| Bos taurus
| P80457
| http://www.uniprot.org/uniprot/P80457
| Whey
| NP_776397.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776397.1
| 1332
| 146790
| http://www.uniprot.org/uniprot/P80457.fasta
| XDH
| 280960
| https://www.ncbi.nlm.nih.gov/gene/280960
| Reviewed: Experimental evidence at protein level
| Blood, heart, liver, intestine, endothelial cells and at
the luminal surface of rat liver sinusoidal endothelial
cells,
| catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid; source of superoxide ion, hydrogen peroxide, and nitric oxide, which can function as second messengers in the activation of various pathways; may induce mutagenesis, cell proliferation, and tumor progression, but they are also associated with apoptosis and cell differentiation; XOR activity generates free radicals and other oxidant reactive species resulting in either harmful or beneficial outcomes; modulate endothelial function and arteriolar tone; may be cytotoxic
| catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid; source of superoxide ion, hydrogen peroxide, and nitric oxide, which can function as second messengers in the activation of various pathways; may induce mutagenesis, cell proliferation, and tumor progression, but they are also associated with apoptosis and cell differentiation; XOR activity generates free radicals and other oxidant reactive species resulting in either harmful or beneficial outcomes; modulate endothelial function and arteriolar tone; may be cytotoxic
| Antimicrobial activity; natural antibiotic; encourages breas-feeding in infants; generates hydrogen peroxide
| Bovine XOR is not glycosylated; human XO is N-glycosylated; goat MFGM XO contains sialic acids in O-linked glycosylation
|
| 1fiq, 1fo4, 1n5x, 1v97, 1vdv, 3am9, 3amz, 3ax7, 3ax9, 3b9j, 3bdj, 3etr, 3eub, 3nrz, 3ns1, 3nvv, 3nvw, 3nvy, 3nvz, 3sr6, 3una, 3unc, 3uni
| XOR activity is upreglated in ischaemia that increases ROS; XOR production increases in brain meningitis;
|
| 1. Hancock, J. T., Salisbury, V., Ovejero-Boglione, M. C., Cherry, R., Hoare, C., Eisenthal, R., and Harrison, R. (2002) Antimicrobial properties of milk: dependence on presence of xanthine oxidase and nitrite. Antimicrob. Agents Chemother. 46, 3308–3310.
2. Wang, C.-H., Zhao, T.-X., Li, M., Zhang, C., and Xing, X.-H. (2016) Characterization of a novel Acinetobacter baumannii xanthine dehydrogenase expressed in Escherichia coli. Biotechnol. Lett. 38, 337–344.
3. Parks, D. A. and Granger, D. N. (1986) Xanthine oxidase: biochemistry, distribution and physiology. Acta Physiol. Scand. Suppl. 548, 87–99.
4. de Jong, J. W., van der Meer, P., Nieukoop, A. S., Huizer, T., Stroeve, R. J., and Bos, E. (1990) Xanthine oxidoreductase activity in perfused hearts of various species, including humans. Circ. Res. 67, 770–773.
5. Corte, E. D. and Stirpe, F. (1972) The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem. J. 126, 739–745.
6. Bray, R. C. (1975) 6 Molybdenum Iron-Sulfur Flauin Hydroxylases and Related Enzymes. Enzym. 12, 299–419.
7. Gutteridge, S., Tanner, S. J., and Bray, R. C. (1978) Comparison of the molybdenum centres of native and desulpho xanthine oxidase. The nature of the cyanide-labile sulphur atom and the nature of the proton-accepting group. Biochem. J. 175, 887–897.
8. Wahl, R. C. and Rajagopalan, K. V. (1982) Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases. J. Biol. Chem. 257, 1354–1359.
9.Massey, V., Schopfer, L. M., Nishino, T., and Nishino, T. (1989) Differences in protein structure of xanthine dehydrogenase and xanthine oxidase revealed by reconstitution with flavin active site probes. J. Biol. Chem. 264, 10567–10573.
10. Miyamoto, Y., Akaike, T., Yoshida, M., Goto, S., Horie, H., and Maeda, H. (1996) Potentiation of nitric oxide-mediated vasorelaxation by xanthine oxidase inhibitors. Proc. Soc. Exp. Biol. Med. 211, 366–373.
11. Miyamoto, Y., Akaike, T., Yoshida, M., Goto, S., Horie, H., and Maeda, H. (1996) Potentiation of nitric oxide-mediated vasorelaxation by xanthine oxidase inhibitors. Proc. Soc. Exp. Biol. Med. 211, 366–373
|
| Bomi2307
| Histone H3.3
| Bos taurus
| Q5E9F8
| https://www.uniprot.org/uniprot/Q5E9F8
| Whey, MFGM, Exosome
| NP_001014411.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001014411.1
| 136
| 15328
| https://www.uniprot.org/uniprot/Q5E9F8.fasta
| H3F3A
| 326601
| https://www.ncbi.nlm.nih.gov/gene/326601
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2317
| High mobility group protein B2
| Bos taurus
| P40673
| https://www.uniprot.org/uniprot/P40673
| Whey
| NP_001032705.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001032705.1
| 209
| 24034
| https://www.uniprot.org/uniprot/P40673.fasta
| HMGB2
| 540444
| https://www.ncbi.nlm.nih.gov/gene/540444
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi232
| Beta-1,4-galactosyltransferase 1
| Bos taurus
| P08037
| https://www.uniprot.org/uniprot/P08037
| Whey, MFGM, Exosome
| NP_803478.1
| https://www.ncbi.nlm.nih.gov/protein/NP_803478.1
| 402
| 44843
| https://www.uniprot.org/uniprot/P08037.fasta
| B4GALT1
| 281781
| https://www.ncbi.nlm.nih.gov/gene/281781
| Reviewed: Experimental evidence at protein level
|
| synthesizes a disaccharide unit,
Galβ1-4GlcNAc (N-acetyllactosamine), present in many biologically active carbohydrate
determinants, mediating several biological events, making it a key enzyme in glycobiology; participates in the synthesis of Galβ1-4-GlcNacdisaccharide
unit of glycoconjugates;
| synthesizes a disaccharide unit,
Galβ1-4GlcNAc (N-acetyllactosamine), present in many biologically active carbohydrate
determinants, mediating several biological events, making it a key enzyme in glycobiology; participates in the synthesis of Galβ1-4-GlcNacdisaccharide
unit of glycoconjugates;
| interacts with α-lactalbumin to form the lactose synthase (LS) complex
that transfers galactose from UDP-α-D-Gal to glucose, producing the lactose secreted in milk
|
|
| 1FGX, 1FR8, 1NF5, 1NHE, 1NKH, 1NMM, 1NQI, 1NWG, 1O0R, 1O23, 1OQM, 1PZT, 1PZY, 1TVY, 1TW1, 1TW5, 1YRO, 2FYC, 2FYD, 4KRV
|
|
| 1. Qasba, P. K., Ramakrishnan, B. and Boeggeman, E. (2005) ‘Substrate-induced conformational changes in glycosyltransferases’, Trends in Biochemical Sciences, 30(1), pp. 53–62. doi: 10.1016/j.tibs.2004.11.005.
2. Qasba, P., Ramakrishnan, B. and Boeggeman, E. (2008) ‘Structure and Function of β -1,4-Galactosyltransferase’, Current Drug Targets, 9(4), pp. 292–309. doi: 10.2174/138945008783954943.
3. Harrus, D. et al. (2018) ‘The dimeric structure of wild-type human glycosyltransferase B4GalT1.’, PloS one. Edited by I. André, 13(10), p. e0205571. doi: 10.1371/journal.pone.0205571.
|
| Bomi2321
| Protein HP-20 homolog
| Bos taurus
| Q2KIT0
| https://www.uniprot.org/uniprot/Q2KIT0
| Whey
| NP_001040049.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001040049.1
| 191
| 20646
| https://www.uniprot.org/uniprot/Q2KIT0.fasta
|
| 616715
| https://www.ncbi.nlm.nih.gov/gene/616715
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2325
| Heat shock protein HSP 90-beta
| Bos taurus
| Q76LV1
| https://www.uniprot.org/uniprot/Q76LV1
| Whey, MFGM, Exosome
| NP_001073105.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001073105.1
| 724
| 83253
| https://www.uniprot.org/uniprot/Q76LV1.fasta
| HSP90AB1
| 767874
| https://www.ncbi.nlm.nih.gov/gene/767874
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2332
| Isocitrate dehydrogenase [NADP] cytoplasmic
| Bos taurus
| Q9XSG3
| https://www.uniprot.org/uniprot/Q9XSG3
| Whey, MFGM, Exosome
| NP_851355.2
| https://www.ncbi.nlm.nih.gov/protein/NP_851355.2
| 414
| 46785
| https://www.uniprot.org/uniprot/Q9XSG3.fasta
| IDH1
| 281235
| https://www.ncbi.nlm.nih.gov/gene/281235
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2342
| Inhibitor of nuclear factor kappa-B kinase-interacting protein
| Bos taurus
| A2VE53
| https://www.uniprot.org/uniprot/A2VE53
| Whey
| NP_001075205.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001075205.1
| 349
| 39216
| https://www.uniprot.org/uniprot/A2VE53.fasta
| IKBIP
| 540640
| https://www.ncbi.nlm.nih.gov/gene/540640
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2343
| Leukocyte elastase inhibitor
| Bos taurus
| Q1JPB0
| https://www.uniprot.org/uniprot/Q1JPB0
| Whey, MFGM, Exosome
| NP_001193539.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001193539.1
| 377
| 42236
| https://www.uniprot.org/uniprot/Q1JPB0.fasta
| SERPINB1
| 507264
| https://www.ncbi.nlm.nih.gov/gene/507264
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2348
| Importin-13
| Bos taurus
| A7YWD2
| https://www.uniprot.org/uniprot/A7YWD2
| Whey
| NP_001098860.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001098860.1
| 963
| 108139
| https://www.uniprot.org/uniprot/A7YWD2.fasta
| IPO13
| 523399
| https://www.ncbi.nlm.nih.gov/gene/523399
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2357
| Inter-alpha-trypsin inhibitor heavy chain H4
| Bos taurus
| Q3T052
| https://www.uniprot.org/uniprot/Q3T052
| Whey
| NP_001015590.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001015590.2
| 916
| 101513
| https://www.uniprot.org/uniprot/Q3T052.fasta
| ITIH4
| 513700
| https://www.ncbi.nlm.nih.gov/gene/513700
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2358
| Inositol 1,4,5-trisphosphate receptor type 1
| Bos taurus
| Q9TU34
| https://www.uniprot.org/uniprot/Q9TU34
| Whey, Exosome
| NP_777266.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777266.1
| 2709
| 308318
| https://www.uniprot.org/uniprot/Q9TU34.fasta
| ITPR1
| 317697
| https://www.ncbi.nlm.nih.gov/gene/317697
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2369
| Kininogen-2
| Bos taurus
| P01045
| https://www.uniprot.org/uniprot/P01045
| Whey, Exosome
| NP_001106748.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001106748.1
| 619
| 68710
| https://www.uniprot.org/uniprot/P01045.fasta
| KNG2
| 280833
| https://www.ncbi.nlm.nih.gov/gene/280833
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2371
| Protein KRI1 homolog
| Bos taurus
| Q0V8M0
| https://www.uniprot.org/uniprot/Q0V8M0
| Whey
| NP_001103542.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001103542.1
| 705
| 82540
| https://www.uniprot.org/uniprot/Q0V8M0.fasta
| KRI1
| 511427
| https://www.ncbi.nlm.nih.gov/gene/511427
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2375
| Lipopolysaccharide-binding protein
| Bos taurus
| Q2TBI0
| https://www.uniprot.org/uniprot/Q2TBI0
| Whey, MFGM, Exosome
| NP_001033763.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001033763.1
| 481
| 53698
| https://www.uniprot.org/uniprot/Q2TBI0.fasta
| LBP
| 512242
| https://www.ncbi.nlm.nih.gov/gene/512242
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2376
| L-lactate dehydrogenase A chain
| Bos taurus
| P19858
| https://www.uniprot.org/uniprot/P19858
| Whey, MFGM
| NP_776524.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776524.1
| 332
| 36598
| https://www.uniprot.org/uniprot/P19858.fasta
| LDHA
| 281274
| https://www.ncbi.nlm.nih.gov/gene/281274
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2377
| L-lactate dehydrogenase B chain
| Bos taurus
| Q5E9B1
| https://www.uniprot.org/uniprot/Q5E9B1
| Whey, MFGM, Exosome
| NP_001303267.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001303267.1
| 334
| 36724
| https://www.uniprot.org/uniprot/Q5E9B1.fasta
| LDHB
| 281275
| https://www.ncbi.nlm.nih.gov/gene/281275
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2378
| Legumain
| Bos taurus
| Q95M12
| https://www.uniprot.org/uniprot/Q95M12
| Whey
| NP_776526.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776526.1
| 433
| 49284
| https://www.uniprot.org/uniprot/Q95M12.fasta
| LGMN
| 281281
| https://www.ncbi.nlm.nih.gov/gene/281281
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi238
| Bone morphogenetic protein 3
| Bos taurus
| P22444
| https://www.uniprot.org/uniprot/P22444
| Whey
| NP_001179197.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001179197.1
| 475
| 53501
| https://www.uniprot.org/uniprot/P22444.fasta
| BMP3
| 539527
| https://www.ncbi.nlm.nih.gov/gene/539527
| Reviewed: Experimental evidence at protein level
|
| multifunctional cytokines that elicit pleiotropic effects on biological
processes such as cell proliferation, cell differentiation and tissue morphogenesis; can exert either mitogenic or anti-mitogenic activities; recognized roles in bone formation during
mammalian development
| multifunctional cytokines that elicit pleiotropic effects on biological
processes such as cell proliferation, cell differentiation and tissue morphogenesis; can exert either mitogenic or anti-mitogenic activities; recognized roles in bone formation during
mammalian development
| BMP 4 potentiates growth factor-induced
proliferation of mammary epithelial cells
| As found in human kidney, BMP 2 Glycosylated: high-mannose and complex N-linked oligosaccharides; contains five Glycosylated: potential N-linked glycosylation
sites (Asn-Xaa-Ser/Thr) at the N135, N163, N164, N200 and
N338 positions, four in the prosegment domain and one in the
mature region
| essential for protein and induces osteoblast differentiation
|
|
|
| 1. Liao, W. X. et al. (2003) ‘Effect of intracellular interactions on the processing and secretion of bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9. Implication of the aberrant ovarian phenotype of BMP-15 mutant sheep.’, The Journal of biological chemistry, 278(6), pp. 3713–9. doi: 10.1074/jbc.M210598200.
2. Hang, Q. et al. (2014) ‘Asparagine-linked glycosylation of bone morphogenetic protein-2 is required for secretion and osteoblast differentiation’, Glycobiology, 24(3), pp. 292–304. doi: 10.1093/glycob/cwt110.
3. Heinecke, K. et al. (2009) ‘Receptor oligomerization and beyond: a case study in bone morphogenetic proteins’, BMC Biology, 7(1), p. 59. doi: 10.1186/1741-7007-7-59.
4. Montesano, R., Sarközi, R. and Schramek, H. (2008) ‘Bone morphogenetic protein-4 strongly potentiates growth factor-induced proliferation of mammary epithelial cells’, Biochemical and Biophysical Research Communications, 374(1), pp. 164–168. doi: 10.1016/j.bbrc.2008.07.007.
|
| Bomi2381
| Lon protease homolog, mitochondrial
| Bos taurus
| Q59HJ6
| https://www.uniprot.org/uniprot/Q59HJ6
| Whey
| NP_001015569.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001015569.2
| 961
| 106670
| https://www.uniprot.org/uniprot/Q59HJ6.fasta
| LONP1
| 510796
| https://www.ncbi.nlm.nih.gov/gene/510796
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2382
| Lon protease homolog 2, peroxisomal
| Bos taurus
| Q3SX23
| https://www.uniprot.org/uniprot/Q3SX23
| Whey
| NP_001029895.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029895.1
| 852
| 94310
| https://www.uniprot.org/uniprot/Q3SX23.fasta
| LONP2
| 541085
| https://www.ncbi.nlm.nih.gov/gene/541085
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2386
| Protein LTV1 homolog
| Bos taurus
| Q0VC06
| https://www.uniprot.org/uniprot/Q0VC06
| Whey, Exosome
| NP_001068794.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068794.1
| 475
| 54788
| https://www.uniprot.org/uniprot/Q0VC06.fasta
| LTV1
| 507702
| https://www.ncbi.nlm.nih.gov/gene/507702
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2389
| Leucine zipper putative tumor suppressor 2
| Bos taurus
| A5PKL7
| https://www.uniprot.org/uniprot/A5PKL7
| Whey, Exosome
| NP_001092332.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001092332.1
| 667
| 72466
| https://www.uniprot.org/uniprot/A5PKL7.fasta
| LZTS2
| 504411
| https://www.ncbi.nlm.nih.gov/gene/504411
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2391
| Lysosomal alpha-mannosidase
| Bos taurus
| Q29451
| https://www.uniprot.org/uniprot/Q29451
| Whey
| NP_776986.2
| https://www.ncbi.nlm.nih.gov/protein/NP_776986.2
| 999
| 112919
| https://www.uniprot.org/uniprot/Q29451.fasta
| MAN2B1
| 282272
| https://www.ncbi.nlm.nih.gov/gene/282272
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2396
| Mannose-binding protein C
| Bos taurus
| O02659
| https://www.uniprot.org/uniprot/O02659
| Whey
| NP_776532.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776532.1
| 249
| 26471
| https://www.uniprot.org/uniprot/O02659.fasta
| MBL
| 281297
| https://www.ncbi.nlm.nih.gov/gene/281297
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi24
| Cofilin -2
| Bos taurus
| Q148F1
| https://www.uniprot.org/uniprot/Q148F1
| Whey
| NP_001069622.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001069622.1
| 166
| 18737
| https://www.uniprot.org/uniprot/Q148F1.fasta
| CFL2
| 539332
| https://www.ncbi.nlm.nih.gov/gene/539332
| Reviewed: Experimental evidence at transcript level
| skeletal and cardiac myoblasts
| Regulates actin by enhancing the turnover of actin filaments ;controls the length of actin filaments in sarcomeres
| Regulates actin by enhancing the turnover of actin filaments ;controls the length of actin filaments in sarcomeres
|
| Reversible phosphorylation on ser3
| Cofilin activity is regulated by reversible phosphorylation on ser3. Phosphorylation inactivates and dephosphorylation activates cofilin, regulating its ability to bind G- or F-actin
|
| Mutations in the cofilin-2 gene lead to myopathies in humans; cofilin-2 deficient mice show progressive disruption of the sarcomeric architecture and
abnormal accumulation of F-actin in skeletal muscles
|
| 1. Zhu, H., Yang, H., Zhao, S., Zhang, J., Liu, D., Tian, Y., … Su, Y. (2018). Role of the cofilin 2 gene in regulating the myosin heavy chain genes in mouse myoblast C2C12 cells. International Journal of Molecular Medicine, 41(2), 1096–1102. https://doi.org/10.3892/ijmm.2017.3272.
2. Kremneva, E., Makkonen, M. H., Skwarek-Maruszewska, A., Gateva, G., Michelot, A., Dominguez, R., & Lappalainen, P. (2014). Cofilin-2 controls actin filament length in muscle sarcomeres. Developmental Cell, 31(2), 215–226. https://doi.org/10.1016/j.devcel.2014.09.002.
3. Subramanian, K., Gianni, D., Balla, C., Assenza, G. E., Joshi, M., Semigran, M. J., … Del Monte, F. (2015). Cofilin-2 phosphorylation and sequestration in myocardial aggregates: novel pathogenetic mechanisms for idiopathic dilated cardiomyopathy. Journal of the American College of Cardiology, 65(12), 1199–1214. https://doi.org/10.1016/j.jacc.2015.01.031.
4. Yu, B.-B., Lin, G.-X., Li, L., Qu, S., Liang, Z.-G., Chen, K.-H., … Zhu, X.-D. (2018). Cofilin-2 Acts as a Marker for Predicting Radiotherapy Response and Is a Potential Therapeutic Target in Nasopharyngeal Carcinoma. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 24, 2317–2329. https://doi.org/10.12659/msm.909832.
|
| Bomi2403
| Methyltransferase-like protein 2
| Bos taurus
| Q0P5B2
| https://www.uniprot.org/uniprot/Q0P5B2
| Whey
| NP_001068714.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068714.1
| 378
| 43485
| https://www.uniprot.org/uniprot/Q0P5B2.fasta
| METTL2
| 506221
| https://www.ncbi.nlm.nih.gov/gene/506221
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2405
| Melanoma inhibitory activity protein 3
| Bos taurus
| Q0VC16
| https://www.uniprot.org/uniprot/Q0VC16
| Whey
| NP_001160043.2
| https://www.ncbi.nlm.nih.gov/protein/NP_001160043
| 1905
| 211668
| https://www.uniprot.org/uniprot/Q0VC16.fasta
| MIA3
| 509133
| https://www.ncbi.nlm.nih.gov/gene/509133
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2407
| Mitogen-activated protein kinase 7
| Bos taurus
| A5PKJ4
| https://www.uniprot.org/uniprot/A5PKJ4
| Whey
| NP_001092550.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001092550.1
| 781
| 84832
| https://www.uniprot.org/uniprot/A5PKJ4.fasta
| MAPK7
| 537703
| https://www.ncbi.nlm.nih.gov/gene/537703
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi241
| Dipeptidyl peptidase 1
| Bos taurus
| Q3ZCJ8
| https://www.uniprot.org/uniprot/Q3ZCJ8
| Whey
| NP_001028789.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001028789.1
| 463
| 51949
| https://www.uniprot.org/uniprot/Q3ZCJ8.fasta
| CTSC
| 352958
| https://www.ncbi.nlm.nih.gov/gene/352958
| Reviewed: Experimental evidence at transcript level
|
| cystein cathepsin; involved in a normal cellular
protein degradation and turnover; aminodipeptidase
| cystein cathepsin; involved in a normal cellular
protein degradation and turnover; aminodipeptidase
| DPP4 is a key enzyme in intermediary metabolism by regulating important glycemic pathways; expression of DPP4 decreases with the onset of lactation
| Glycosylated: four glycans
|
|
|
|
| 1. Schulz, K. et al. (2015) ‘Effects of Inhibiting Dipeptidyl Peptidase-4 (DPP4) in Cows with Subclinical Ketosis.’, PloS one. Edited by M. Bader, 10(8), p. e0136078. doi: 10.1371/journal.pone.0136078.
2. Turk, B., Turk, D. and Turk, V. (2000) ‘Lysosomal cysteine proteases: more than scavengers.’, Biochimica et biophysica acta, 1477(1–2), pp. 98–111. doi: 10.1016/s0167-4838(99)00263-0.
3. Turk, D. et al. (2001) ‘Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases’, The EMBO Journal, 20(23), pp. 6570–6582. doi: 10.1093/emboj/20.23.6570.
|
| Bomi2410
| Matrix metalloproteinase-9
| Bos taurus
| P52176
| https://www.uniprot.org/uniprot/P52176
| Whey
| NP_777169.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777169.1
| 712
| 79088
| https://www.uniprot.org/uniprot/P52176.fasta
| MMP9
| 282871
| https://www.ncbi.nlm.nih.gov/gene/282871
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2412
| Molybdenum cofactor biosynthesis protein 1
| Bos taurus
| Q1JQD7
| https://www.uniprot.org/uniprot/Q1JQD7
| Whey
| NP_001013615.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001013615.1
| 633
| 69659
| https://www.uniprot.org/uniprot/Q1JQD7.fasta
| MOCS1
| 281917
| https://www.ncbi.nlm.nih.gov/gene/281917
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2416
| Cation-independent mannose-6-phosphate receptor
| Bos taurus
| P08169
| https://www.uniprot.org/uniprot/P08169
| Whey, MFGM, Exosome
| NP_776777.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776777.1
| 2499
| 274529
| https://www.uniprot.org/uniprot/P08169.fasta
| IGF2R
| 281849
| https://www.ncbi.nlm.nih.gov/gene/281849
| Reveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi242
| Cytosolic carboxypeptidase 3
| Bos taurus
| E1B9D8
| https://www.uniprot.org/uniprot/E1B9D8
| Whey
|
|
| 1003
| 116561
| https://www.uniprot.org/uniprot/E1B9D8.fasta
| AGBL3
|
|
| Reviewed: Protein inferred from homology
|
| Some carboxyl peptidase (CPs) function in the degradation of proteins in the
digestive tract while other enzymes play biosynthetic roles in the formation of neuropeptides and
peptide hormones; CPs modify tubulin by removing amino acids from the Cterminus
and from polyglutamyl side chains, thereby altering the properties of microtubules;
| Some carboxyl peptidase (CPs) function in the degradation of proteins in the
digestive tract while other enzymes play biosynthetic roles in the formation of neuropeptides and
peptide hormones; CPs modify tubulin by removing amino acids from the Cterminus
and from polyglutamyl side chains, thereby altering the properties of microtubules;
| active in human milk throughout lactation; digests milk within mammary gland
|
|
|
|
|
| 1. Wu, H.-Y. et al. (2015) ‘Comparison of the enzymatic and functional properties of three cytosolic carboxypeptidase family members.’, The Journal of biological chemistry, 290(2), pp. 1222–32. doi: 10.1074/jbc.M114.604850.
2. Dallas, D. C. et al. (2013) ‘Extensive in vivo Human Milk Peptidomics Reveals Specific Proteolysis Yielding Protective Antimicrobial Peptides’, Journal of Proteome Research, 12(5), pp. 2295–2304. doi: 10.1021/pr400212z.
3. Khaldi, N. et al. (2014) ‘Predicting the Important Enzymes in Human Breast Milk Digestion’, Journal of Agricultural and Food Chemistry, 62(29), pp. 7225–7232. doi: 10.1021/jf405601e.
|
| Bomi2430
| Nucleoside diphosphate kinase B
| Bos taurus
| Q3T0Q4
| https://www.uniprot.org/uniprot/Q3T0Q4
| Whey, MFGM, Exosome
| NP_001069844.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001069844.1
| 152
| 17316
| https://www.uniprot.org/uniprot/Q3T0Q4.fasta
| NME2
| 615447
| https://www.ncbi.nlm.nih.gov/gene/615447
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2434
| Protein kinase C-binding protein NELL2
| Bos taurus
| A6QR11
| https://www.uniprot.org/uniprot/A6QR11
| Whey
| NP_001095554.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001095554.1
| 816
| 91270
| https://www.uniprot.org/uniprot/A6QR11.fasta
| NELL2
| 524622
| https://www.ncbi.nlm.nih.gov/gene/524622
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2439
| NmrA-like family domain-containing protein 1
| Bos taurus
| Q0VCN1
| https://www.uniprot.org/uniprot/Q0VCN1
| Whey, Exosome
| NP_001069500.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001069500.1
| 299
| 33154
| https://www.uniprot.org/uniprot/Q0VCN1.fasta
| NMRAL1
| 534628
| https://www.ncbi.nlm.nih.gov/gene/534628
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2440
| Epididymal secretory protein E1
| Bos taurus
| P79345
| https://www.uniprot.org/uniprot/P79345
| Whey
| NP_776343.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776343.1
| 149
| 16640
| https://www.uniprot.org/uniprot/P79345.fasta
| NPC2
| 280815
| https://www.ncbi.nlm.nih.gov/gene/280815
| Reviewed: Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2446
| Nucleobindin-1
| Bos taurus
| Q0P569
| https://www.uniprot.org/uniprot/Q0P569
| Whey, Exosome
| NP_001068667.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068667.1
| 474
| 54982
| https://www.uniprot.org/uniprot/Q0P569.fasta
| NUCB1
| 505351
| https://www.ncbi.nlm.nih.gov/gene/505351
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2451
| Outer dense fiber protein 2
| Bos taurus
| Q2T9U2
| https://www.uniprot.org/uniprot/Q2T9U2
| Whey, MFGM
| NP_001033269.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001033269.1
| 657
| 75498
| https://www.uniprot.org/uniprot/Q2T9U2.fasta
| ODF2
| 539043
| https://www.ncbi.nlm.nih.gov/gene/539043
| Reveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2453
| Protein OS-9
| Bos taurus
| Q3MHX6
| https://www.uniprot.org/uniprot/Q3MHX6
| Whey, MFGM, Exosome
| NP_001029397.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029397.1
| 667
| 75779
| https://www.uniprot.org/uniprot/Q3MHX6.fasta
| OS9
| 504832
| https://www.ncbi.nlm.nih.gov/gene/504832
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2469
| Protein disulfide-isomerase A4
| Bos taurus
| Q29RV1
| https://www.uniprot.org/uniprot/Q29RV1
| Whey
| NP_001039344.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001039344.1
| 643
| 72526
| https://www.uniprot.org/uniprot/Q29RV1.fasta
| PDIA4
| 415110
| https://www.ncbi.nlm.nih.gov/gene/415110
| Reveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi247
| Cystic fibrosis transmembrane conductance regulator
| Bos taurus
| P35071
| https://www.uniprot.org/uniprot/P35071
| Whey
| NP_776443.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776443.1
| 1481
| 167758
| https://www.uniprot.org/uniprot/P35071.fasta
| CFTR
| 281067
| https://www.ncbi.nlm.nih.gov/gene/281067
| Reviewed: Experimental evidence at transcript level
|
| ATPaseyABC-transporter that functions
as a chloride channel; functions as a
regulator of other ion channels and of intracellular membrane transport processes; inhibits the amiloride sensitive epithelial
sodium channel, volume-regulated anion channels and endogenous calcium-activated chloride
currents; activates the outwardly rectifying chloride
channel; sensitizes potassium channels to sulfonylurea
compounds; alters the ion composition of intracellular
compartments; regulates intracellular vesicle transport
| ATPaseyABC-transporter that functions
as a chloride channel; functions as a
regulator of other ion channels and of intracellular membrane transport processes; inhibits the amiloride sensitive epithelial
sodium channel, volume-regulated anion channels and endogenous calcium-activated chloride
currents; activates the outwardly rectifying chloride
channel; sensitizes potassium channels to sulfonylurea
compounds; alters the ion composition of intracellular
compartments; regulates intracellular vesicle transport
|
| N-glycosylated through addition of two high mannose groups on its fourth extracellular loop
|
|
|
|
| 1. Mansoura, M. K. et al. (1998) ‘Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Anion Binding as a Probe of the Pore’, Biophysical Journal, 74(3), pp. 1320–1332. doi: 10.1016/S0006-3495(98)77845-2.
2. Stutts, M. J., Rossier, B. C. and Boucher, R. C. (1997) ‘Cystic Fibrosis Transmembrane Conductance Regulator Inverts Protein Kinase A-mediated Regulation of Epithelial Sodium Channel Single Channel Kinetics’, Journal of Biological Chemistry, 272(22), pp. 14037–14040. doi: 10.1074/jbc.272.22.14037.
3. Schwiebert, E. M. et al. (1995) ‘CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP.’, Cell, 81(7), pp. 1063–73. doi: 10.1016/s0092-8674(05)80011-x.
4. McNicholas, C. M. et al. (1997) ‘A functional CFTR-NBF1 is required for ROMK2-CFTR interaction’, American Journal of Physiology-Renal Physiology, 273(5), pp. F843–F848. doi: 10.1152/ajprenal.1997.273.5.F843.
5. Barasch, J. et al. (1991) ‘Defective acidification of intracellular organelles in cystic fibrosis’, Nature, 352(6330), pp. 70–73. doi: 10.1038/352070a0.
6. Vennekens, R. et al. (1999) ‘Inhibition of volume-regulated anion channels by expression of the cystic fibrosis transmembrane conductance regulator.’, The Journal of physiology, 515 ( Pt 1)(1), pp. 75–85. doi: 10.1111/j.1469-7793.1999.075ad.x.
|
| Bomi2471
| Phosphatidylethanolamine-binding protein 1
| Bos taurus
| P13696
| https://www.uniprot.org/uniprot/P13696
| Whey, Exosome
| NP_001028795.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001028795.1
| 187
| 20986
| https://www.uniprot.org/uniprot/P13696.fasta
| PEBP1
| 431786
| https://www.ncbi.nlm.nih.gov/gene/431786
| Reveiwed;Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2479
| Phosphoglucomutase-1
| Bos taurus
| Q08DP0
| https://www.uniprot.org/uniprot/Q08DP0
| Whey, Exosome
| NP_001070371.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001070371.1
| 562
| 61589
| https://www.uniprot.org/uniprot/Q08DP0.fasta
| PGM1
| 534402
| https://www.ncbi.nlm.nih.gov/gene/534402
| Reveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi248
| Cholinesterase
| Bos taurus
| P32749
| https://www.uniprot.org/uniprot/P32749
| Whey
| NP_001070374.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001070374.1
| 602
| 68867
| https://www.uniprot.org/uniprot/P32749.fasta
| BCHE
| 534616
| https://www.ncbi.nlm.nih.gov/gene/534616
| Reviewed: Experimental evidence at transcript level
| expressed in
cholinergic neurons
| termination of impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine; serine hydrolases; key
role in ending cholinergic neurotransmission
| termination of impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine; serine hydrolases; key
role in ending cholinergic neurotransmission
| proinflammatory factors in milk
| three potential N-glycosylation sites Asn-265, Asn-350 and Asn-464
| Asn-464 has the most pronounced effect on thermostability
|
|
|
| 1. Dvir, H. et al. (2010) ‘Acetylcholinesterase: From 3D structure to function’, Chemico-Biological Interactions, 187(1–3), pp. 10–22. doi: 10.1016/j.cbi.2010.01.042.
2. Velan, B. et al. (1993) ‘N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis’, Biochemical Journal, 296(3), pp. 649–656. doi: 10.1042/bj2960649.
3. Ollis, D. L. et al. (1992) ‘The alpha/beta hydrolase fold.’, Protein engineering, 5(3), pp. 197–211. doi: 10.1093/protein/5.3.197.
|
| Bomi2487
| Phosphatidylinositol transfer protein beta isoform
| Bos taurus
| Q9TR36
| https://www.uniprot.org/uniprot/Q9TR36
| Whey
| NP_001071508.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001071508.1
| 271
| 31539
| https://www.uniprot.org/uniprot/Q9TR36.fasta
| PITPNB
| 613773
| https://www.ncbi.nlm.nih.gov/gene/613773
| Reveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2495
| Placental prolactin-related protein 3
| Bos taurus
| P12402
| https://www.uniprot.org/uniprot/P12402
| Whey
| NP_776585.1
| https://www.ncbi.nlm.nih.gov/protein/NP_776585.1
| 213
| 25016
| https://www.ncbi.nlm.nih.gov/protein/NP_776585.1
| PRP3
| 281430
| https://www.ncbi.nlm.nih.gov/gene/281430
| Reveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi25
| Complement factor H
| Bos taurus
| Q28085
| https://www.uniprot.org/uniprot/Q28085
| Whey
| NP_001029108.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001029108.1
| 1236
| 140374
| https://www.uniprot.org/uniprot/Q28085.fasta
| CFH
| 280816
| https://www.ncbi.nlm.nih.gov/gene/280816
| Reviewed: Experimental evidence at protein level
| retinal pigment epithelial cells,endothelial cells, epithelial cells, platelets, mesenchymal stem cells, liver
| Serum glycoprotein; accelerates the decay of the alternative pathway C3 convertase; cofactor for factor I-mediated cleavage and inactivation of C3b; recognize
specific markers on host cells and control complement on self surfaces; detects and binds to initial C3b deposits in combination with specific
markers on host cells;
| Serum glycoprotein; accelerates the decay of the alternative pathway C3 convertase; cofactor for factor I-mediated cleavage and inactivation of C3b; recognize
specific markers on host cells and control complement on self surfaces; detects and binds to initial C3b deposits in combination with specific
markers on host cells;
| immune protection
against environmental pathogens
| Glycosylation; as found in humans, eight N-glycans; forty disulfide bonds; absence of hybrid and oligomannose structures; presence of complex, diantennary disialylated, non-fucosylated glycans; Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified; Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative; absence of
hybrid and oligomannose structures
|
|
| In the absence of factor H, spontaneous activation of the alternative pathway of complement occurs in plasma, which leads to consumption of
complement components C3 and factor B
|
| 1. Fenaille, F., Le Mignon, M., Groseil, C., Ramon, C., Riandé, S., Siret, L., & Bihoreau, N. (2007). Site-specific N-glycan characterization of human complement factor H. Glycobiology, 17(9), 932–944. https://doi.org/10.1093/glycob/cwm060.
2. Okemefuna, A. I., Li, K., Nan, R., Ormsby, R. J., Sadlon, T., Gordon, D. L., & Perkins, S. J. (2009). Multimeric Interactions between Complement Factor H and Its C3d Ligand Provide New Insight on Complement Regulation. Journal of Molecular Biology, 391(1), 119–135. https://doi.org/10.1016/j.jmb.2009.06.013.
3. Harrison, R. A., & Lachmann, P. J. (1980). The physiological breakdown of the third component of human complement. Molecular Immunology, 17(1), 9–20. https://doi.org/10.1016/0161-5890(80)90119-4.
4. Licht, C., Pluthero, F. G., Li, L., Christensen, H., Habbig, S., Hoppe, B., … Kahr, W. H. A. (2009). Platelet-associated complement factor H in healthy persons and patients with atypical HUS. Blood, 114(20), 4538–4545. https://doi.org/10.1182/blood-2009-03-205096.
5. Chen, M., Forrester, J. V, & Xu, H. (2007). Synthesis of complement factor H by retinal pigment epithelial cells is down-regulated by oxidized photoreceptor outer segments. Experimental Eye Research, 84(4), 635–645. https://doi.org/10.1016/j.exer.2006.11.015.
6. Brooimans, R. A., van der Ark, A. A., Buurman, W. A., van Es, L. A., & Daha, M. R. (1990). Differential regulation of complement factor H and C3 production in human umbilical vein endothelial cells by IFN-gamma and IL-1. Journal of Immunology (Baltimore, Md. : 1950), 144(10), 3835–3840. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/2139673.
7. Adinolfi, M., Dobson, N. C., & Bradwell, A. R. (1981). Synthesis of two components of human complement, beta 1H and C3bINA, during fetal life. Acta Paediatrica Scandinavica, 70(5), 705–710. https://doi.org/10.1111/j.1651-2227.1981.tb05772.
|
| Bomi2502
| Lysosomal protective protein
| Bos taurus
| Q3MI05
| https://www.uniprot.org/uniprot/Q3MI05
| Whey
| NP_001030403.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001030403.1
| 479
| 53980
| https://www.uniprot.org/uniprot/Q3MI05.fasta
| CTSA
| 518169
| https://www.ncbi.nlm.nih.gov/gene/518169
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2507
| Peroxiredoxin-6
| Bos taurus
| O77834
| https://www.uniprot.org/uniprot/O77834
| Whey, MFGM, Exosome
| NP_777068.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777068.1
| 224
| 25067
| https://www.uniprot.org/uniprot/O77834.fasta
| PRDX6
| 282438
| https://www.ncbi.nlm.nih.gov/gene/282438
| Reveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2509
| Profilin-1
| Bos taurus
| P02584
| https://www.uniprot.org/uniprot/P02584
| Whey, MFGM, Exosome
| NP_001015592.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001015592.1
| 140
| 15057
| https://www.uniprot.org/uniprot/P02584.fasta
| PFN1
| 513895
| https://www.ncbi.nlm.nih.gov/gene/513895
| Reveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi252
| 2',3'-cyclic-nucleotide 3'-phosphodiesterase
| Bos taurus
| P06623
| https://www.uniprot.org/uniprot/P06623
| Whey, MFGM
| NP_851336.1
| https://www.ncbi.nlm.nih.gov/protein/NP_851336.1
| 400
| 44875
| https://www.uniprot.org/uniprot/P06623.fasta
| CNP
| 280752
| https://www.ncbi.nlm.nih.gov/gene/280752
| Reviewed:Experimental evidence at transcript level
| most abundantly
in myelin of oligodendrocytes in the CNS and to a lesser extent
Schwann cells of the PNS
| hydrolyse 2', 3'-cyclic nucleotides (but not 3',5'-
cyclic nucleotides) in vitro resulting in the production of 2'-
derivatives; enzymic activity associated with mitochondrial
membranes isolated from liver; can interact with the actin-based cytoskeleton; regarded as a specific marker of oligodendrocytes
and Schwann cells and it is clear that the majority
of CNP protein in the developing and adult brain is present in
myelin
| hydrolyse 2', 3'-cyclic nucleotides (but not 3',5'-
cyclic nucleotides) in vitro resulting in the production of 2'-
derivatives; enzymic activity associated with mitochondrial
membranes isolated from liver; can interact with the actin-based cytoskeleton; regarded as a specific marker of oligodendrocytes
and Schwann cells and it is clear that the majority
of CNP protein in the developing and adult brain is present in
myelin
| important functional enzyme of the
bovine mammary gland; implicated in
milk fat production; lactation is improved by modulating
the cyclic nucleotide intracellular second messengers which are hydrolyzed into their
inactive form by the phosphodiesterase
| isoprenoid derived from meva-
Ionic acid; only the smaller of the two
CNP isoforms (CNP1) is isoprenylated; C-terminal Cys-Thr-
Ile-Ile (conserved in rat, mouse, bovine, and human CNP)
| isoprenylation and carboxyl methylation of the cys might account for this property
of CNP; isoprenylation is
permissive for the well-known avid association of
CNP with membrane - Inhibition
of isoprenoid synthesis by Lovastatin blocks the binding
of newly synthesized CNP to cell membranes
|
|
|
| 1. Dostaler-Touchette, V. et al. (2009) ‘Cyclic adenosine monophosphate (cAMP)-specific phosphodiesterase is functional in bovine mammary gland.’, Journal of dairy science, 92(8), pp. 3757–65. doi: 10.3168/jds.2009-2065.
2. McFerran, B. and Burgoyne, R. (1997) ‘2’,3’-Cyclic nucleotide 3’-phosphodiesterase is associated with mitochondria in diverse adrenal cell types.’, Journal of cell science, 110 ( Pt 23), pp. 2979–85. Available at: http://www.ncbi.nlm.nih.gov/pubmed/9359886 (Accessed: 5 October 2019).
|
| Bomi2530
| Prostaglandin-H2 D-isomerase
| Bos taurus
| O02853
| https://www.uniprot.org/uniprot/O02853
| Whey
| NP_777216.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777216.1
| 191
| 21229
| https://www.uniprot.org/uniprot/O02853.fasta
| PTGDS
| 286858
| https://www.ncbi.nlm.nih.gov/gene/286858
| Reveiwed:Experimental evidence at protein level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2532
| Parathyroid hormone-related protein
| Bos taurus
| P58073
| https://www.uniprot.org/uniprot/P58073
| Whey
| NP_777178.1
| https://www.ncbi.nlm.nih.gov/protein/NP_777178.1
| 177
| 20408
| https://www.uniprot.org/uniprot/P58073.fasta
| PTHLH
| 286767
| https://www.ncbi.nlm.nih.gov/gene/286767
| Reveiwed:Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi2539
| Glycogen phosphorylase, liver form
| Bos taurus
| Q0VCM4
| https://www.uniprot.org/uniprot/Q0VCM4
| Whey, MFGM, Exosome
| NP_001068671.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001068671.1
| 851
| 97456
| https://www.uniprot.org/uniprot/Q0VCM4.fasta
| PYGL
| 505472
| https://www.ncbi.nlm.nih.gov/gene/505472
| Reviewed: Experimental evidence at transcript level
|
|
|
|
|
|
|
|
|
|
|
| Bomi254
| Coactosin-like protein
| Bos taurus
| Q2HJ57
| https://www.uniprot.org/uniprot/Q2HJ57
| Whey, Exosome
| NP_001040058.1
| https://www.ncbi.nlm.nih.gov/protein/NP_001040058.1
| 142
| 16010
| https://www.uniprot.org/uniprot/Q2HJ57.fasta
| COTL1
| 617165
| https://www.ncbi.nlm.nih.gov/gene/617165
| Reviewed: Experimental evidence at transcript level
| wide tissue distribution and is predominantly expressed
in placenta, lung, kidney and peripheral-blood leucocytes
| filamentous actin (F-actin)-binding protein in humans;
| filamentous actin (F-actin)-binding protein in humans;
|
|
|
|
|
|
| 1. Provost, P. et al. (2001) ‘Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75.’, The Biochemical journal, 359(Pt 2), pp. 255–63. doi: 10.1042/0264-6021:3590255.
|
| Bomi2548
| Tumor necrosis factor receptor superfamily, member 21
| Bos taurus
| Q08DN1
| https://www.uniprot.org/uniprot/Q08DN1
| Whey
| NP_001070379.1
| https://www. |
