enteropeptidase; enterokinase; serine protease 7; transmembrane protease serine 15 (TMPRSS15, ENTK, PRSS7)
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Function
- responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin & carboxypeptidase A)
- catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, & proelastases
- activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond
- the chains are derived from a single precursor that is cleaved by a trypsin-like protease
- heterodimer of a catalytic (light) chain & a multidomain (heavy) chain linked by a disulfide bond
Structure
- belongs to the peptidase S1 family
- contains 2 CUB domains
- contains 2 LDL-receptor class A domains
- contains 1 MAM domain
- contains 1 peptidase S1 domain
- contains 1 SEA domain
- contains 1 SRCR domain
Compartment
- membrane; single-pass type 2 membrane protein (probable)
Expression
Pathology
- defects in TMPRSS15 are a cause of enterokinase deficiency