NPR1

For another use, see Arabidopsis thaliana.

Natriuretic peptide receptor A/guanylate cyclase A (atrionatriuretic peptide receptor A), also known as NPR1, is an atrial natriuretic peptide receptor. In humans it is encoded by the NPR1 gene.

NPR1
Identifiers
Aliases	NPR1, ANPRA, ANPa, GUC2A, GUCY2A, NPRA, natriuretic peptide receptor 1
External IDs	OMIM: 108960; MGI: 97371; HomoloGene: 37367; GeneCards: NPR1; OMA:NPR1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q21.3 Start 153,678,688 bp End 153,693,992 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 F1|3 39.23 cM Start 90,357,898 bp End 90,373,173 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Descending thoracic aorta ascending aorta right uterine tube gastric mucosa left uterine tube right coronary artery left coronary artery subcutaneous adipose tissue right lung triceps brachii muscle Top expressed in yolk sac spermatocyte muscle of thigh blastocyst morula adrenal gland lip esophagus thyroid gland dentate gyrus of hippocampal formation granule cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein kinase activity nucleotide binding G protein-coupled peptide receptor activity hormone binding guanylate cyclase activity GTP binding lyase activity natriuretic peptide receptor activity phosphorus-oxygen lyase activity ATP binding peptide hormone binding adenylate cyclase activity protein kinase binding peptide receptor activity Cellular component integral component of membrane membrane plasma membrane receptor complex guanylate cyclase complex, soluble intracellular anatomical structure Biological process negative regulation of smooth muscle cell proliferation regulation of cardiac conduction intracellular signal transduction positive regulation of renal sodium excretion positive regulation of urine volume body fluid secretion cyclic nucleotide biosynthetic process receptor guanylyl cyclase signaling pathway regulation of blood pressure cGMP biosynthetic process protein phosphorylation cell surface receptor signaling pathway regulation of vascular permeability dopamine metabolic process negative regulation of cell growth negative regulation of angiogenesis G protein-coupled receptor signaling pathway blood vessel diameter maintenance positive regulation of cGMP-mediated signaling cGMP-mediated signaling signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4881 18160 Ensembl ENSG00000169418 ENSMUSG00000027931 UniProt P16066 P18293 RefSeq (mRNA) NM_000906 NM_008727 RefSeq (protein) NP_000897 NP_032753 Location (UCSC) Chr 1: 153.68 – 153.69 Mb Chr 3: 90.36 – 90.37 Mb PubMed search
Wikidata
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Function

NPR1 is a membrane-bound guanylate cyclase that serves as the receptor for both atrial and brain natriuretic peptides (ANP and BNP, respectively).

It is localized in the kidney where it results in natriuresis upon binding to natriuretic peptides. However, it is found in even greater quantity in the lungs and adipocytes.

See also

• Atrial natriuretic peptide receptor

Further reading

• Pandey KN (2002). "Intracellular trafficking and metabolic turnover of ligand-bound guanylyl cyclase/atrial natriuretic peptide receptor-A into subcellular compartments". Mol. Cell. Biochem. 230 (1–2): 61–72. doi:10.1023/A:1014240006767. PMID 11952097. S2CID 10397726.
• Lucarelli K, Iacoviello M, Dessì-Fulgheri P, et al. (2003). "[Natriuretic peptides and essential arterial hypertension]". Italian Heart Journal Supplement. 3 (11): 1085–91. PMID 12506509.
• Pandey KN (2005). "Internalization and trafficking of guanylyl cyclase/natriuretic peptide receptor-A". Peptides. 26 (6): 985–1000. doi:10.1016/j.peptides.2004.12.020. PMID 15911067. S2CID 34452043.
• Garg R, Pandey KN (2005). "Regulation of guanylyl cyclase/natriuretic peptide receptor-A gene expression". Peptides. 26 (6): 1009–23. doi:10.1016/j.peptides.2004.09.022. PMID 15911069. S2CID 33508201.

External links

• NPR1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.