Primary Information
BoMiProt ID	Bomi169
Protein Name	Serpin A3-3
Organism	Bos taurus
Uniprot ID	Q3ZEJ6
Milk Fraction	Whey
Ref Sequence ID	NP_001033293.1
Aminoacid Length	411
Molecular Weight	46326
FASTA Sequence	Download
Gene Name	SERPINA3-3
Gene ID	615103
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Presence in other biological fluids/tissue/cells	hepatocytes, intestinal epithelial cells, neutrophils, lung epithelial cells, macrophages, human serum, saliva, tears, milk, semen, urine and bile
Protein Function	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
Biochemical Properties	strong affinity towards neutrophil elastase; irreversible inhibitor for kallikreins 7 and 14; inhibits intra-cellular and cell-surface proteases; inhibits the activity of caspase-3, an intra-cellular cysteine protease which plays an essential role in cell apoptosis;
Significance in milk	inhibits thrombin activity
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Bibliography	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.