Thrombin light chain (IPR018992)

Short name: Thrombin_light_chain

Overlapping homologous superfamilies

Domain relationships



Thrombin is a Na+-activated, allosteric serine protease that functions in blood homeostasis, inflammation and wound healing [PMID: 18329094]. Thrombin (or coagulation factor II) is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, and (in complex with thrombomodulin) protein C [PMID: 18282807]. Sodium binding is the major driving force behind the procoagulant, prothrombotic and signaling functions of the enzyme, but is dispensable for cleavage of the anticoagulant protein C [PMID: 15656349]. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.

GO terms

Biological Process

GO:0007596 blood coagulation
GO:0006508 proteolysis

Molecular Function

GO:0004252 serine-type endopeptidase activity

Cellular Component

GO:0005576 extracellular region

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.