Primary Information
BoMiProt ID	Bomi16
Protein Name	Alpha-2-antiplasmin
Organism	Bos taurus
Uniprot ID	P28800
Milk Fraction	Whey
Ref Sequence ID	NP_777095.1
Aminoacid Length	492
Molecular Weight	54711
FASTA Sequence	Download
Gene Name	SERPINF2
Gene ID	282522
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Presence in other biological fluids/tissue/cells	synthesized and secreted by the liver, kidney and brain;
Protein Function	primary inhibitor of fibrinolysis, inhibiting plasmin directly; facilitates tissue repair.  The plasma serine protease inhibitor alpha 2-antiplasmin (α2-AP, otherwise known as α2-plasmin inhibitor) is a rapid-acting plasmin inhibitor recently found in human plasma, which seems to have a significant role in the regulation of in vivo fibrinolysis.
Biochemical Properties	a serine protease inhibitor;α 2-antiplasmin is found in either plasminogen-bound or free circulating form; Bovine a2-AP has a molecular mass that is low enough to cross from the blood stream into milk - makes it likable to be the in the plasmin system of milk;
Significance in milk	presence in milk control proteolysis caused by the plasmin system in dairy products
PTMs	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;
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation	>sp|P28800|A2AP_BOVIN Alpha-2-antiplasmin OS=Bos taurus OX=9913 GN=SERPINF2 PE=1 SV=2 MALLWGLLALILSCLSSLCSAQFSPVSTMEPLDLQLMDGQAQQKLPPLSLLKLDNQEPGG QIAPKKAPEDCKLSPTPEQTRRLARAMMTFTTDLFSLVAQSSTRPNLILSPLSVALALSH LALGAQN*127QTLQRLKEVLHADSGPCLPHLLSRLCQDLGPGAFRLAARMYLQKGFPIKEDFL EQSEQLFGAKPMSLTGMKGEDLANINRWVKEATEGKIEDFLSDLPDDTVLLLLNAIHFQG FWRSKFDPN*249LTQRGAFHLDEQFTVPVDMMQALTYPLHWFLLEQPEIQVAHFPFKNN*296MSFV VLMPTRFEWN*310ASQVLAN*317LTWDILHQPSLSERPTKVQLPKLHLKYQLDLVATLSQLGLQEL FQAPDLRGISDERLVVSSVQHQSALELSEAGVQAAAATSTAMSRMSLSSFIVNRPFLFFI LEDSTSLPLFVGSVRNPNPGAQPERKEQQDSPDGKDSFQDHKGLPRGDKPFDPDLKLGPP SEEDYAQPSSPK
Predicted Disorder Regions	40-77,395-397,439-492
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	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
Additional Comments	Defeciency increases fibrinolysis; leads to severe bleeding with hemophilialike bleeding symptoms
Bibliography	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. 9.Mohammed BAB. Alpha 2-antiplasmin deficiency in a Sudanese child: a case report. J Med Case Rep. 2021 May 7;15(1):238. doi: 10.1186/s13256-021-02813-6. PMID: 33957960; PMCID: PMC8103643.