Natriuretic peptide receptor family
Natriuretic peptide receptors (provisional nomenclature) are a family (ENSFM00250000000198) of homodimeric, catalytic receptors with a single TM domain and guanylyl cyclase (EC 4.6.1.2) activity on the intracellular domain of the protein sequence. Isoforms are activated by the peptide hormones atrial natriuretic peptide (ANP, ENSG00000175206), brain natriuretic peptide (BNP, ENSG00000120937) and C-type natriuretic peptide (CNP, ENSG00000163273). Another family member is GC-C, the receptor for guanylin (ENSG00000113389) and uroguanylin (ENSG00000044012). Family members have conserved ligand-binding, catalytic (guanylyl cyclase) and regulatory domains with the exception of NPR-C which has an extracellular binding domain homologous to that of other NPRs, but with a truncated intracellular domain which appears to couple, via the Gi/o family of G-proteins, to activation of phospholipase C, inwardly-rectifying potassium channels and inhibition of adenylyl cyclase activity [11].
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
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10. Morishita, Y; Sano, T; Ando, K; Saitoh, Y; Kase, H; Yamada, K; Matsuda, Y. (1991) Microbial polysaccharide, HS-142-1, competitively and selectively inhibits ANP binding to its guanylyl cyclase-containing receptor. Biochem. Biophys. Res. Commun., 176 (3): 949-57. [PMID:1674870]
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The polysaccharide obtained from fermentation of Aureobasidium species, HS142-1, acts as an antagonist at both NPR-A and NPR-B receptors [10].
Gucy2D (RetGC1, GC-E, ENSG00000132518) and Gucy2F (RetGC2, GC-F, ENSG00000101890) are predominantly retinal guanylyl cyclase activities, which are inhibited by calcium ions acting through the guanylyl cyclase activating peptides GCAP1 (GUCA1A, ENSG00000048545), GCAP2 (GUCA1B, ENSG00000112599) and GCAP3 (GUCA1C, ENSG00000138472) [6].