P2RX1

P2RX1
Identifiers
Aliases	P2RX1, P2X1, purinergic receptor P2X 1
External IDs	OMIM: 600845; MGI: 1098235; HomoloGene: 1921; GeneCards: P2RX1; OMA:P2RX1 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.2 Start 3,896,592 bp End 3,916,476 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B4|11 45.09 cM Start 72,889,929 bp End 72,906,026 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in popliteal artery tibial arteries saphenous vein body of pancreas monocyte granulocyte blood right coronary artery bone marrow cells left coronary artery Top expressed in detrusor urinae muscle umbilical cord blood tunica media of zone of aorta granulocyte thymus embryo tibiofemoral joint Ileal epithelium perirhinal cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding purinergic nucleotide receptor activity ion channel activity cation channel activity ATP binding extracellularly ATP-gated cation channel activity ATP-gated ion channel activity Cellular component integral component of membrane postsynaptic membrane membrane plasma membrane integral component of nuclear inner membrane integral component of plasma membrane membrane raft neuron projection secretory granule membrane specific granule membrane external side of plasma membrane protein-containing complex glutamatergic synapse integral component of postsynaptic membrane integral component of presynaptic active zone membrane Biological process response to ATP regulation of calcium ion transport synaptic transmission, glutamatergic protein heterooligomerization regulation of smooth muscle contraction vasoconstriction ceramide biosynthetic process serotonin secretion by platelet blood coagulation ion transport response to organic substance cation transmembrane transport platelet activation regulation of blood pressure regulation of vasoconstriction positive regulation of ion transport insemination protein homooligomerization activation of cysteine-type endopeptidase activity involved in apoptotic process regulation of vascular associated smooth muscle contraction neuronal action potential signal transduction apoptotic process purinergic nucleotide receptor signaling pathway neutrophil degranulation excitatory postsynaptic potential regulation of presynaptic cytosolic calcium ion concentration regulation of synaptic vesicle exocytosis cation transport ion transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5023 18436 Ensembl ENSG00000108405 ENSMUSG00000020787 UniProt P51575 P51576 RefSeq (mRNA) NM_002558 NM_008771 RefSeq (protein) NP_002549 NP_032797 Location (UCSC) Chr 17: 3.9 – 3.92 Mb Chr 11: 72.89 – 72.91 Mb PubMed search
Wikidata
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P2X purinoceptor 1, also ATP receptor, is a protein that in humans is encoded by the P2RX1 gene.

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with relatively high calcium permeability. Expressed in smooth muscle and platelets. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle, being responsible, for example, for sympathetic vasoconstriction in small arteries, arterioles and vas deferens. Mouse studies suggest that this receptor is essential for normal male reproductive function. It is possible that the development of selective antagonists for this receptor may provide an effective non-hormonal male contraceptive pill.

See also

• P2X receptor

Further reading

• North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
• Longhurst PA, Schwegel T, Folander K, Swanson R (1996). "The human P2x1 receptor: molecular cloning, tissue distribution, and localization to chromosome 17". Biochim. Biophys. Acta. 1308 (3): 185–8. doi:10.1016/0167-4781(96)00112-1. PMID 8809107.
• Clifford EE, Parker K, Humphreys BD, et al. (1998). "The P2X1 receptor, an adenosine triphosphate-gated cation channel, is expressed in human platelets but not in human blood leukocytes". Blood. 91 (9): 3172–81. doi:10.1182/blood.V91.9.3172. PMID 9558372.
• Sun B, Li J, Okahara K, Kambayashi J (1998). "P2X1 purinoceptor in human platelets. Molecular cloning and functional characterization after heterologous expression". J. Biol. Chem. 273 (19): 11544–7. doi:10.1074/jbc.273.19.11544. PMID 9565569.
• Mulryan K, Gitterman DP, Lewis CJ, et al. (2000). "Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors". Nature. 403 (6765): 86–9. Bibcode:2000Natur.403...86M. doi:10.1038/47495. PMID 10638758. S2CID 4416421.
• Oury C, Toth-Zsamboki E, Van Geet C, et al. (2000). "A natural dominant negative P2X1 receptor due to deletion of a single amino acid residue". J. Biol. Chem. 275 (30): 22611–4. doi:10.1074/jbc.C000305200. PMID 10816552.
• Dhulipala PD, Lianos EA, Kotlikoff MI (2001). "Regulation of human P2X1 promoter activity by beta helix-loop-helix factors in smooth muscle cells". Gene. 269 (1–2): 167–75. doi:10.1016/S0378-1119(01)00442-5. PMID 11376948.
• Ennion SJ, Evans RJ (2002). "Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface". Mol. Pharmacol. 61 (2): 303–11. doi:10.1124/mol.61.2.303. PMID 11809854.
• Vial C, Rolf MG, Mahaut-Smith MP, Evans RJ (2002). "A study of P2X1 receptor function in murine megakaryocytes and human platelets reveals synergy with P2Y receptors". Br. J. Pharmacol. 135 (2): 363–72. doi:10.1038/sj.bjp.0704486. PMC 1573149. PMID 11815371.
• Oury C, Toth-Zsamboki E, Thys C, et al. (2003). "The ATP-gated P2X1 ion channel acts as a positive regulator of platelet responses to collagen". Thromb. Haemost. 86 (5): 1264–71. PMID 11816716.
• Toth-Zsamboki E, Oury C, Watanabe H, et al. (2002). "The intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential for its function". FEBS Lett. 524 (1–3): 15–9. Bibcode:2002FEBSL.524...15T. doi:10.1016/S0014-5793(02)02987-3. PMID 12135734. S2CID 7845543.
• Oury C, Toth-Zsamboki E, Vermylen J, Hoylaerts MF (2002). "P2X(1)-mediated activation of extracellular signal-regulated kinase 2 contributes to platelet secretion and aggregation induced by collagen". Blood. 100 (7): 2499–505. doi:10.1182/blood-2002-03-0812. hdl:2268/23403. PMID 12239162.
• Rolf MG, Mahaut-Smith MP (2003). "Effects of enhanced P2X₁ receptor Ca²⁺ influx on functional responses in human platelets". Thromb. Haemost. 88 (3): 495–502. doi:10.1055/s-0037-1613243. PMID 12353081. S2CID 41234874.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Valdecantos P, Briones R, Moya P, et al. (2003). "Pharmacological identification of P2X1, P2X4 and P2X7 nucleotide receptors in the smooth muscles of human umbilical cord and chorionic blood vessels". Placenta. 24 (1): 17–26. doi:10.1053/plac.2002.0862. PMID 12495655.
• Oury C, Kuijpers MJ, Toth-Zsamboki E, et al. (2003). "Overexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype". Blood. 101 (10): 3969–76. doi:10.1182/blood-2002-10-3215. PMID 12521992.
• Wang L, Andersson M, Karlsson L, et al. (2004). "Increased mitogenic and decreased contractile P2 receptors in smooth muscle cells by shear stress in human vessels with intact endothelium". Arterioscler. Thromb. Vasc. Biol. 23 (8): 1370–6. doi:10.1161/01.ATV.0000080350.37408.5A. PMID 12791671.
• Vial C, Pitt SJ, Roberts J, et al. (2004). "Lack of evidence for functional ADP-activated human P2X1 receptors supports a role for ATP during hemostasis and thrombosis". Blood. 102 (10): 3646–51. doi:10.1182/blood-2003-06-1963. PMID 12907444. S2CID 22284207.

External links

• P2RX1+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.