PRCP

PRCP is a member of the peptidase S28 family of serine exopeptidases. The encoded preproprotein is proteolytically processed to generate the mature lysosomal prolylcarboxypeptidase. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotension II, III and des-Arg9-bradykinin. The cleavage occurs at acidic pH, but the enzyme activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein. The importance of angiotension II, one of the substrates of this enzyme, in regulating blood pressure and electrolyte balance suggests that this gene may be related to essential hypertension. A pseudogene of this gene has been identified on chromosome 2. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.

Full Name

prolylcarboxypeptidase (angiotensinase C)

Function

Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

Biological Process

Angiogenesis involved in wound healingManual Assertion Based On ExperimentIBA:GO_Central
Energy homeostasisIEA:Ensembl
Glucose homeostasisIEA:Ensembl
Negative regulation of systemic arterial blood pressureManual Assertion Based On ExperimentIBA:GO_Central
Plasma kallikrein-kinin cascadeIEA:Ensembl
ProteolysisIEA:UniProtKB-KW
Regulation of blood vessel endothelial cell migrationManual Assertion Based On ExperimentIBA:GO_Central
Regulation of reactive oxygen species metabolic processIEA:Ensembl
Regulation of thyroid hormone mediated signaling pathwayIEA:Ensembl

Cellular Location

Lysosome