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Guanylyl cyclases, catalyzing the production of cGMP from GTP, are classified as soluble and membrane forms. 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 and type B. Also see NPR3, 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 and BNP, respectively).
AI893888; ANPa; ANP-A; ANPRA; ANPR-A; atrial natriuretic peptide A-type receptor; atrial natriuretic peptide receptor 1; atrial natriuretic peptide receptor A; atrial natriuretic peptide receptor type A; atrionatriuretic peptide receptor A; Gca; GC-A; Guanylate cyclase A; guanylyl cyclase-A; GUC2A; GUCY2A; natriuretic peptide A type receptor; natriuretic peptide receptor 1; natriuretic peptide receptor A; natriuretic peptide receptor A/guanylate cyclase A (atrionatriuretic peptide receptor A); Nppa receptor; Npr1; Npra; NPR-A; Pndr; testicular tissue protein Li 20
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