Guanylyl cyclases, catalyzing the production of cGMP from GTP, are classified as soluble and membrane forms (Garbers and Lowe, 1994 [PubMed 7982997]). The membrane guanylyl cyclases, often termed guanylyl cyclases A through F, form a family of cell-surface receptors with a similar topographic structure: an extracellular ligand-binding domain, a single membrane-spanning domain, and an intracellular region that contains a protein kinase-like domain and a cyclase catalytic domain. GC-A and GC-B function as receptors for natriuretic peptides; they are also referred to as atrial natriuretic peptide receptor A (NPR1) and type B (NPR2; MIM 108961). Also see NPR3 (MIM 108962), which encodes a protein with only the ligand-binding transmembrane and 37-amino acid cytoplasmic domains. NPR1 is a membrane-bound guanylate cyclase that serves as the receptor for both atrial and brain natriuretic peptides (A
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Function:
Catalytic activity:GTP = 3',5'-cyclic GMP + diphosphate.,Function:Receptor for atrial natriuretic peptide. Has guanylate cyclase activity on binding of ANF.,miscellaneous:There seem to be at least three natriuretic peptide hormone receptors: two with guanylate cyclase activity (NPR1/ANP-A and NPR2/ANP-B) and one (NPR3/ANP-C) which is probably responsible for the clearance of natriuretic peptides from the circulation without a role in signal transduction.,PTM:Phosphorylation of the protein kinase-like domain is required for full activation by ANP.,similarity:Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.,similarity:Contains 1 guanylate cyclase domain.,similarity:Contains 1 protein kinase domain.,