Search by BoMiProt ID - Bomi165


Primary Information

BoMiProt ID Bomi165
Protein Name Serpin A3-1
Organism Bos taurus
Uniprot IdQ9TTE1
Milk FractionWhey
Ref Sequence Id NP_777193.2
Amino Acid Lenth 411
Molecular Weight 46237
Fasta Sequence https://www.uniprot.org/uniprot/Q9TTE1.fasta
Gene Name SERPINA3-1
Gene Id 286804
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells hepatocytes, bronchial epithelial cells neuronal cells
Protein Function 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
Biochemical Properties inhibits chymotrypsin through direct binding; reactive centre loop (RCL) is partially inserted into the A β-sheet, a structural motif associated with ligand dependent activation in other serpins; RCL is stabilised by salt bridges; efficient inhibitor of human leukocyte elastase and cathepsin G
Significance in milk inhibit chymotrypsin, has a higher specificity for chymotrypsin than α1-antichymotrypsin
Bibliography 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.