NPR1

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, May 2009]

Description

Natriuretic peptide receptor 1

Tissue specificity

Tissue enhanced (adipose tissue)

Subcell location

Nucleoplasm, Nucleoli, Plasma membrane

Predicted location

Membrane

Protein family

Enzymes
FDA approved drug targets
Mapped to neXtProt
Mapped to UniProt SWISS-PROT
Metabolic proteins
Predicted membrane proteins
Protein evidence (Ezkurdia et al 2014)
Protein evidence (Kim et al 2014)
Transporters

Chromosome

1 (153678688 - 153693992)

Ensembl ID

ENSG00000169418  (ver. 103.38)

Orthologs

Mouse Npr1: ENSMUSG00000027931

UniProt

P16066

neXtProt

NX_P16066

Human splice variants
Mouse splice variants

Protein structure