UniProtKB/Swiss-Prot entry P84122

• FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).
• CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
• SUBCELLULAR LOCATION: Secreted.
• TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
• PTM: 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.
• PTM: N-glycosylated (By similarity).
• MISCELLANEOUS: Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin.
• MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.
• SIMILARITY: Belongs to the peptidase S1 family [view classification].
• SIMILARITY: Contains 1 peptidase S1 domain [view classification].