Search by BoMiProt ID - Bomi1


Primary Information

BoMiProt ID Bomi1
Protein Name Inter-alpha-trypsin inhibitor heavy chain H1
Organism Bos taurus
Uniprot IdQ0VCM5
Milk FractionWhey
Ref Sequence Id NP_001068821.1
Amino Acid Lenth 906
Molecular Weight 101237
Fasta Sequence https://www.uniprot.org/uniprot/Q0VCM5.fasta
Gene Name ITIH1
Gene Id 508356
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells IαI family proteins are mainly secreted by the liver and present in the blood;
Protein Function 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
Biochemical Properties The 3 isoforms are all expressed in the liver and coupled with bikunin before they are released into blood circulation - difference being their selective combination with bikunin; The heavy chain(HC)1–3 prepropeptides (∼900 amino acid residues) comprise a signal peptide, a short propeptide, a mature form of HC, and a C-terminal polypeptide; hyaluronan is the most recognized HC interacting molecule; HCs are observed to be covalently linked to hyaluronan via a transesterification reaction, where they are often referred to as SHAP (serum-derived hyaluronanassociated proteins; The effects of SHAPs on hyaluronan include protection against free radicals, enhancement of macromolecular aggregation, and an increase in the binding avidity to other matrix components;
Significance in milk acute phase protein in cattle- was isolated from heifers with experimentally induced 'summer mastitis'
PTMs 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;
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q0VCM5|ITIH1_BOVIN Inter-alpha-trypsin inhibitor heavy chain H1 OS=Bos taurus OX=9913 GN=ITIH1 PE=1 SV=1
MGLRGLLCVCLVSLLALQAVAAQGSPTRNPKGGKKRMAVDAAVDGVVIRSLKVNCKVTSR FAHYIITSQVVNSADTAKEVSFNVEIPKTAFISDFAITADENAFTGDIKDKVTAWKQYRK AAISGENAGLVRASGRTMEQFSIHIIVGPRSKATFRLTYEEVLRRKLMQYDIVIKVKPQQ LVQHFEIDVDIFEPQGIRKLDVEASFLPKELAAQLIKKSFSGKKGHVLFRPTVSQQQTCP TCSTTLLNGDFKVTYDVNRDDACDLLVANNYFAHFFAPQNLKKLNKNVVFVIDISSSMEG QKLKQTKEALHKILGDMRPGDYFDLVLFGSAVQSWKGSLVQASPANLEAARNFVQQFSLA GATNLNGGLLRGIEILNKAQQSLPELSNHASILIMLTDGEPTEGVMDRTQILKNVRDGIK GRFPLYNLGFGHDVDLNFLEVMSLENNGRVQRIYEDHDATQQLQGFYEQVANPLLRDVEL LYPREAVSDLTQHRHKQYYEGSEIMVAGRIADHKLSSFKADVRAHGEGQEFMTTCLVDKE EMKKLLRERGHMLENHVERLWAYLTIQELLAKRMKLEGQEKANVSAKALQMSLAYQFVTP LTSMTVRGMTDQDGLEPIIDKPLDDYLPLEMVGPRKTFMLQAS*643QPAPT*648HSSLDIKKLPDQ VTGVDTDPHFLIHVPQKEDTLCFNINEEPGVVLSLVQDPDTGFSVNGQLIGNEAGSPGKH EGTYFGRLGIANPATDFQLEVTPQNITLNPGSGGPVFSWRDQAFLRQNEVLVTINRKRNL VVSVEDGGTFEVVLHRVWRGSAVRQDFLGFYVLDSHRMSARTHGLLGQFFHPFDYKVSNL HPGSDPTKTDATMVVKNRRLTVTRGLQKDYRKDPRHGAEVTCWFIHNNGDGLIDGIHTDY IVPDIF
Significance of PTMs 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
Linking IDs Bomi2357
Bibliography 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