Enteropeptidase (TMPRSS15) Antibody – Mouse Monoclonal

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]

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.

Catalytic activity: Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.

Subunit structure: Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond.

Subcellular location: Membrane; Single-pass type II membrane protein

Probable.

Tissue specificity: Intestinal brush border.

Post-translational modification: The chains are derived from a single precursor that is cleaved by a trypsin-like protease.

Involvement in disease: Enterokinase deficiency (ENTKD) [MIM:226200]: Life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Sequence similarities: 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.

Sequence caution: The sequence CAB90389.1 differs from that shown. Reason: Erroneous gene model prediction.