Search by BoMiProt ID - Bomi2791

Primary Information

BoMiProt ID Bomi2791
Protein Name Prothrombin
Organism Bos taurus
Uniprot IDP00735
Milk FractionWhey, Exosome
Ref Sequence ID NP_776302.1
Aminoacid Length 625
Molecular Weight 70506
FASTA Sequence Download
Gene Name F2
Gene ID 280685
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Protein Function Prothrombin plays a key role in hemostasis also suggests that it may be important for mouse development.
Biochemical Properties In general, a high degree of homology in the primary structure of prothrombin and intermediates was observed between the human and bovine system. The NH2-terminal sequences of human intermediate 2' and alpha-thrombin A chain are identical. However, human intermediate 2' isolated in a manner identical with that used for the isolation of bovine intermediate 2 is homologous with bovine intermediate 2, beginning with residue 14.
PTMs Cleavage on pair of basic residues, Disulfide bond formation, N-Linked Glycosylation at Asn, Zymogen formation,Attachment of Gamma-carboxyglutamic acid
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.
Additional Comments Prothrombin deficiency in mice results in partial embryonic lethality.
Bibliography 1.Degen SJ, Sun WY. The biology of prothrombin. Crit Rev Eukaryot Gene Expr. 1998;8(2):203-24. doi: 10.1615/critreveukargeneexpr.v8.i2.60. PMID: 9714898. 2.Magnusson S., Sottrup-Jensen L., Petersen T.E., Claeys H.(In) Hemker H.C., Veltkamp J.J. (eds.); Boerhaave symposium on prothrombin and related coagulation factors, pp.25-46, Leiden University Press, Leiden (1975)