| Modification Notes |
Corin, also designated atrial natriuretic peptide-converting enzyme, localizes to the membrane as a single-pass type II membrane protein. Corin acts as a serine protease that utilizes atrial and brain natriuretic peptides (ANP and BNP) as substrates, which play a role in blood coagulation, platelet activation, fibrinolysis, and thrombosis. The extracellular domain of Corin contains two frizzled-like cysteine-rich domains, eight low density lipoprotein receptor (LDLR) repeats, a macrophage scavenger receptor-like domain, and a trypsin-like protease domain at the C-terminus. The frizzled 1 domain and LDLR repeats 1-4 are responsible for substrate recognition. Corin converts Pro-ANP to ANP by cleaving between arginine 123 and serine 124. Corin is highly expressed in cardiomyocytes, and mice deficient in the Corin protein exhibit hypertension and have cardiac hypertrophy. |