Peptidase S1A, enteropeptidase (IPR011163)

Short name: Pept_S1A_enterop

Overlapping homologous superfamilies


Family relationships


Enteropeptidase (EC: originally called enterokinase, belongs to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A. It is the protease in mammalian intestinal brush border that is responsible for generation of active trypsin from trypsinogen; trypsin, in turn, activates other digestive enzymes. The mature enteropeptidase has heavy and light chains, connected by a disulphide bond and derived from a single precursor molecule. The light chain comprises the carboxyl-terminal domain of the precursor and contains the trypsin domain (IPR001254). Near the amino end of the heavy chain is a region that may be a signal sequence or signal-anchor. The remainder of the heavy chain comprises a series of domains: SEA, which is likely heavily glycosylated; the first of two Low density lipoprotein-receptor class A domains; the first of two CUB domains; MAM; CUB;Low density lipoprotein-receptor class A domains and SRCR.

For additional information please see [PMID: 8052624].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004252 serine-type endopeptidase activity

Cellular Component

GO:0016020 membrane

Contributing signatures

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