Peptidase S1A, plasmin (IPR023317)

Short name: Pept_S1A_plasmin

Overlapping homologous superfamilies

Family relationships


Plasmin is a serine peptidase belonging to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A. Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes, including embryonic development, tissue remodeling, tumor invasion, and inflammation; in ovulation it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its specificity is similar to trypsin but it is less efficient and, thus, cleaves only after certain Lys and Arg residues. Following the signal sequence, plasmin contains one PAN (formerly apple) domain, five kringle domains, and a trypsin domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004252 serine-type endopeptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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