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Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction.

We isolated cDNAs encoding a 115 kd human atrial natriuretic peptide (alpha ANP) receptor (ANP‐A receptor) that possesses guanylate cyclase activity, by low‐stringency hybridization with sea urchin Arbacia punctulata membrane guanylate cyclase probes. The human ANP‐A receptor has a 32 residue signal sequence followed by a 441 residue extracellular domain homologous to the 60 kd ANP‐C receptor. A 21 residue transmembrane domain precedes a 568 residue cytoplasmic domain with homology to the protein kinase family and to a subunit of the soluble guanylate cyclase. COS‐7 cells transfected with an ANP‐A receptor expression vector displayed specific [125I]alpha ANP binding, and exhibited alpha ANP stimulated cGMP production. These data demonstrate a new paradigm of cellular signal transduction where extracellular ligand binding allosterically regulates cyclic nucleotide second‐messenger production by a receptor cytoplasmic catalytic domain.