Search by BoMiProt ID - Bomi16

Primary Information

BoMiProt ID Bomi16
Protein Name Alpha-2-antiplasmin
Organism Bos taurus
Uniprot IdP28800
Milk FractionWhey
Ref Sequence Id NP_777095.1
Amino Acid Lenth 492
Molecular Weight 54711
Fasta Sequence
Gene Name SERPINF2
Gene Id 282522
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry 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 repai
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,
>sp|P28800|A2AP_BOVIN Alpha-2-antiplasmin OS=Bos taurus OX=9913 GN=SERPINF2 PE=1 SV=2
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
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
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.
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.
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.
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
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.
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.