Search by BoMiProt ID - Bomi3


Primary Information

BoMiProt ID Bomi3
Protein Name Cystatin-B
Organism Bos taurus
Uniprot IdP25417
Milk FractionMFGM, Exosome
Ref Sequence Id NP_001032538.1
Amino Acid Lenth 98
Molecular Weight 11140
Fasta Sequence https://www.uniprot.org/uniprot/P25417.fasta
Gene Name CSTB
Gene Id 512805
Protein Existence Status Reveiwed:Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells lysosomes of primary myoblasts, primary glial cells, extracelluar fluids and secretory granules of rat endocrine B cells, saliva, urine, serum
Protein Function Stefin family; cystein cathepsin inhibitor; protects neurons against oxidative stress; involved in the defence of tissues against invasion by pathogens; upregulated in septic injury;
Biochemical Properties Monomeric protein with missing intramolecular disulfide bridges or glycosylation; resistant to proteolytic cleavge but the N-terminal is accessible to protease attack; soluble protein; nuclear concentration is higher than cytoplasmic concentration;
Significance in milk Downregulated in mastitis; role in the protection from bacterial infection
Additional Comments Fibrillation is caused by acididc solvants, high temperature, presence of TFE or high ionic strengths
Bibliography 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. Sotiropoulou, G., Anisowicz, A., & Sager, R. (1997). Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. The Journal of Biological Chemistry, 272(2), 903–910. https://doi.org/10.1074/jbc.272.2.903.
3. Ni, J., Abrahamson, M., Zhang, M., Fernandez, M. A., Grubb, A., Su, J., … Gentz, R. (1997). Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins. The Journal of Biological Chemistry, 272(16), 10853–10858. https://doi.org/10.1074/jbc.272.16.10853.
4. 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.
5. Maher, K., Jerič Kokelj, B., Butinar, M., Mikhaylov, G., Manček-Keber, M., Stoka, V., … Kopitar-Jerala, N. (2014). A role for stefin B (cystatin B) in inflammation and endotoxemia. The Journal of Biological Chemistry, 289(46), 31736–31750. https://doi.org/10.1074/jbc.M114.609396