Natriuretic Peptide Receptor A (NPR-A) (A.a. 294-308) (NPR1) Antibody – Rabbit Polyclonal

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 (ANP (MIM 108780) and BNP (MIM 600295), respectively).[supplied by OMIM]

Function: Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand. Ref.10

Catalytic activity: GTP = 3',5'-cyclic GMP + diphosphate.

Subunit structure: Homodimer

Subcellular location: Membrane; Single-pass type I membrane protein.

Post-translational modification: Phosphorylation of the protein kinase-like domain is required for full activation by ANP

Sequence similarities: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.Contains 1 guanylate cyclase domain.Contains 1 protein kinase domain.