This gene encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. The precursor protein is cleaved into two chains that form a heterodimer linked by a disulfide bond. This protein is a member of the trypsin family of peptidases. Mutations in this gene cause enterokinase deficiency, a malabsorption disorder characterized by diarrhea and failure to thrive. [provided by RefSeq, Jul 2008],catalytic activity:Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.,disease:Defects in PRSS7 are a cause of enterokinase deficiency [MIM:226200], a life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive.,function:Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.,PTM:The chains are derived from a single precursor that is cleaved by a trypsin-like protease.,similarity:Belongs to the peptidase S1 family.,similarity:Contains 1 MAM domain.,similarity:Contains 1 peptidase S1 domain.,similarity:Contains 1 SEA domain.,similarity:Contains 1 SRCR domain.,similarity:Contains 2 CUB domains.,similarity:Contains 2 LDL-receptor class A domains.,subunit:Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond.,tissue specificity:Intestinal brush border.,
