CORIN
Corin, also called atrial natriuretic peptide-converting enzyme, is a protein that in humans is encoded by the CORIN gene.
Protein
The CORIN gene encodes a member of the type II transmembrane serine protease class of the trypsin superfamily. Members of this family are composed of multiple structurally distinct domains.
Human corin, a polypeptide of 1042 amino acids, consists of an N-terminal cytoplasmic domain, a transmembrane domain and an extracellular region with two frizzled-like domains, eight LDL receptor-like domains, a scavenger receptor-like domain and a C-terminal trypsin-like serine protease domain. Corin is synthesized as a zymogen that is activated by PCSK6.
Corin exhibits a trypsin-like catalytic activity favoring basic residues at the P1 position.
Human corin contains 19 N-glycosylation sites.N-glycans promote corin expression on the cell surface and protect corin from metalloproteinase-mediated shedding.
Function
Corin converts the atrial natriuretic peptide (ANP) precursor, pro-ANP, to mature ANP, a cardiac hormone that regulates salt-water balance and blood pressure. In mice, corin deficiency prevents pro-ANP processing and causes salt-sensitive hypertension.