enteropeptidase; enterokinase; serine protease 7; transmembrane protease serine 15 (TMPRSS15, ENTK, PRSS7)

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: intestinal brush border Pathology: - defects in TMPRSS15 are a cause of enterokinase deficiency

General

glycoprotein myristoylated protein secreted protein serine protease

Properties

SIZE: entity length = 1019 aa MW = 113 kD COMPARTMENT: cellular membrane MOTIF: glycine residue {G2} transmembrane domain {19-47} SEA domain {52-169} MOTIF: N-glycosylation site {N116} N-glycosylation site {N147} N-glycosylation site {N179} LDL-receptor class A {182-223} MOTIF: cysteine residue {C184} MODIFICATION: cysteine residue {C197} cysteine residue {C191} MODIFICATION: cysteine residue {C210} cysteine residue {C197} MODIFICATION: cysteine residue {C184} cysteine residue {C204} MODIFICATION: cysteine residue {C221} cysteine residue {C210} MODIFICATION: cysteine residue {C191} cysteine residue {C221} MODIFICATION: cysteine residue {C204} CUB domain {225-334} MOTIF: cysteine residue {C225} MODIFICATION: cysteine residue {C253} cysteine residue {C253} MODIFICATION: cysteine residue {C225} N-glycosylation site {N328} N-glycosylation site {N335} MAM domain {342-504} MOTIF: cysteine residue {*1} (2) MODIFICATION: cysteine residue {*2} cysteine residue {*2} (2) MODIFICATION: cysteine residue {*1} N-glycosylation site {N388} N-glycosylation site {N440} N-glycosylation site {N470} N-glycosylation site {N503} CUB domain {524-634} MOTIF: cysteine residue {C524} MODIFICATION: cysteine residue {C552} N-glycosylation site {N534} cysteine residue {C552} MODIFICATION: cysteine residue {C524} N-glycosylation site {N630} LDL-receptor class A {641-679} MOTIF: cysteine residue {C643} MODIFICATION: cysteine residue {C655} cysteine residue {C650} MODIFICATION: cysteine residue {C668} cysteine residue {C655} MODIFICATION: cysteine residue {C643} cysteine residue {C662} MODIFICATION: cysteine residue {C677} cysteine residue {C668} MODIFICATION: cysteine residue {C650} cysteine residue {C677} MODIFICATION: cysteine residue {C662} SRCR {678-771} MOTIF: N-glycosylation site {N682} N-glycosylation site {N706} N-glycosylation site {N725} cysteine residue {C757} MODIFICATION: cysteine residue {C767} cysteine residue {C767} MODIFICATION: cysteine residue {C757} cysteine residue {C772} MODIFICATION: cysteine residue {CINTERCHAIN (BETWEEN HEAVY AND LIGHT CHAINS) (BY SIMILARITY} S1 domain {785-1019} MOTIF: cysteine residue {C810} MODIFICATION: cysteine residue {C826} histidine residue {H825} cysteine residue {C826} MODIFICATION: cysteine residue {C810} N-glycosylation site {N848} aspartate residue {D876} N-glycosylation site {N887} N-glycosylation site {N909} cysteine residue {C910} MODIFICATION: cysteine residue {C977} cysteine residue {C941} MODIFICATION: cysteine residue {C956} N-glycosylation site {N949} cysteine residue {C956} MODIFICATION: cysteine residue {C941} cysteine residue {C967} MODIFICATION: cysteine residue {C995} serine residue {S971} cysteine residue {C977} MODIFICATION: cysteine residue {C910} cysteine residue {C995} MODIFICATION: cysteine residue {C967}

Database Correlations

OMIM correlations MORBIDMAP 606635 UniProt P98073 PFAM correlations Entrez Gene 5651 Kegg hsa:5651 ENZYME 3.4.21.9