Renin-like domain (IPR034135)

Short name: Renin-like_dom

Overlapping homologous superfamilies

Domain relationships


This entry represents a domain found in renin, a member of the aspartic peptidase A1 family [PMID: 7674916]. Aspartyl proteases (APs), also known as acid proteases, (EC:3.4.23.-) are a widely distributed family of proteolytic enzymes [PMID: 6795036, PMID: 2194475, PMID: 1851433, PMID: 15771507, PMID: 24869856, PMID: 1455179] known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses. APs use an Asp dyad to hydrolyze peptide bonds [PMID: 7608971].

Renin, also known as angiotensinogenase (MEROPS identifier A01.007), is a circulating enzyme that participates in the renin-angiotensin system that mediates extracellular volume, arterial vasoconstriction, and consequently mean arterial blood pressure. The enzyme is secreted by the kidneys from specialized juxtaglomerular cells in response to decreases in glomerular filtration rate (a consequence of low blood volume), diminished filtered sodium chloride and sympathetic nervous system innervation. The enzyme circulates in the blood stream and hydrolyzes angiotensinogen secreted from the liver into the peptide angiotensin I [PMID: 21755055]. Angiotensin I is further cleaved in the lungs by endothelial bound angiotensin converting enzyme (ACE) into angiotensin II, the final active peptide. The enzyme is a member of peptidase family A1 [PMID: 20393195].

Mice have an additional renin secreted by the submandibular salivary gland and known as renin-2 (MEROPS identifier A01.008) [PMID: 1608447].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.