Renin is a secreted endopeptidase that plays a crucial role in the regulation of blood pressure and salt balance through the cleavage of angiotensinogen, which is the only known physiological substrate of Renin. The 406 aa precursor includes a signal peptide (aa 1 - 23), a propeptide (aa 24 - 66), and a mature chain (aa 67 - 406). The amino acid sequence of human Renin is 100%, 73%, 71% and 67% identical to that of chimpanzee, canine, mouse and rat.
Mouse Renin is a secreted, 42 - 47 kDa glycosylated member of the peptidase A1 family. It is an aspartyl protease that cleaves angiotensinogen to form angiotensin I. In mouse, there are two genes that code for Renin. One is in the submandibular gland and the other is in the kidney. The two mature Renin molecules are 95% amino acid (aa) identical. Renal Renin (Renin-1) is synthesized as a 381 aa proform (aa 22 - 402). In the kidney, prorenin is proteolytically cleaved after Thr71 to generate a mature enzyme. Mouse pro-renin shares 70% and 85% aa sequence identity with human and rat pro-renin, respectively.