Prolylcarboxypeptidase (PRCP)

PCP; HUMPCP; Lysosomal Pro-X Carboxypeptidase; Angiotensinase C; Lysosomal carboxypeptidase C; Proline carboxypeptidase

SPN	V574
HGNC	9344
MGI	1919711
PubMed	23744584
RGD	1307842
UniProt	P42785
Wiki	PRCP

Lysosomal Pro-X carboxypeptidase is a lysosomal prolylcarboxypeptidase, which 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. This enzyme 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. Alternatively spliced transcript variants encoding distinct isoforms have been observed.

Reference

"Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families."
J. Biol. Chem. 268:16631-16638(1993) [PubMed] [Europe PMC] [Abstract]

Erratum
J. Biol. Chem. 268:26032-26032(1993)

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Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

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Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney."
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"Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase."
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