NPR1

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).

Full Name

NATRIURETIC PEPTIDE RECEPTOR 1

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.

Biological Process

Blood vessel diameter maintenance1 PublicationNAS:UniProtKB
Body fluid secretionManual Assertion Based On ExperimentTAS:UniProtKB
Cell surface receptor signaling pathway1 PublicationNAS:UniProtKB
cGMP biosynthetic processManual Assertion Based On ExperimentIDA:GO_Central
cGMP-mediated signalingIEA:Ensembl
Dopamine metabolic processIEA:Ensembl
Negative regulation of angiogenesisManual Assertion Based On ExperimentTAS:UniProtKB
Negative regulation of cell growth1 PublicationNAS:UniProtKB
Negative regulation of smooth muscle cell proliferationIEA:Ensembl
Positive regulation of cGMP-mediated signalingIEA:Ensembl
Positive regulation of renal sodium excretionManual Assertion Based On ExperimentTAS:UniProtKB
Positive regulation of urine volumeManual Assertion Based On ExperimentTAS:UniProtKB
Receptor guanylyl cyclase signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of blood pressure1 PublicationNAS:UniProtKB
Regulation of vascular permeabilityManual Assertion Based On ExperimentTAS:UniProtKB
Signal transductionManual Assertion Based On ExperimentIBA:GO_Central

Cellular Location

Membrane

Topology

Extracellular: 33-473
Helical: 474-494
Cytoplasmic: 495-1061

PTM

Phosphorylation of the protein kinase-like domain is required for full activation by ANP.