P2RX2

P2RX2
Identifiers
Aliases	P2RX2, DFNA41, P2X2, purinergic receptor P2X 2
External IDs	MGI: 2665170 HomoloGene: 14251 GeneCards: P2RX2
Gene ontology Molecular function • purinergic nucleotide receptor activity • extracellular ATP-gated cation channel activity • ion channel activity • ligand-gated ion channel activity • identical protein binding • ATP binding Cellular component • integral component of membrane • membrane • receptor complex • integral component of nuclear inner membrane • integral component of plasma membrane • intracellular • apical plasma membrane • plasma membrane Biological process • peristalsis • response to ATP • positive regulation of calcium-mediated signaling • response to hypoxia • positive regulation of calcium ion transport into cytosol • urinary bladder smooth muscle contraction • sensory perception of sound • ion transport • response to organic substance • cation transmembrane transport • neuromuscular synaptic transmission • behavioral response to pain • neuromuscular junction development • skeletal muscle fiber development • transport • detection of hypoxic conditions in blood by carotid body chemoreceptor signaling • protein homooligomerization • response to carbohydrate • sensory perception of taste • chemical synaptic transmission • blood coagulation • purinergic nucleotide receptor signaling pathway Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	22953	231602
Ensembl	ENSG00000187848	ENSMUSG00000029503
UniProt	Q9UBL9	Q8K3P1
RefSeq (mRNA)	NM_001282164 NM_001282165 NM_012226 NM_016318 NM_170682 NM_170683 NM_174872 NM_174873	NM_001164833 NM_001164834 NM_153400 NM_001310700 NM_001310701
RefSeq (protein)	NP_001269093.1 NP_001269094.1 NP_036358.2 NP_057402.1 NP_733782.1 NP_733783.1 NP_777361.1 NP_777362.1	NP_001158305.1 NP_001158306.1 NP_001297629.1 NP_001297630.1 NP_700449.2
Location (UCSC)	Chr 12: 132.62 – 132.62 Mb	Chr 5: 110.34 – 110.34 Mb
PubMed search	[1]	[2]
Wikidata

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P2X purinoceptor 2 is a protein that in humans is encoded by the P2RX2 gene.^[3][4][5]

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Six transcript variants encoding six distinct isoforms have been identified for this gene.^[5]

See also

• Purinergic receptor

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Lynch KJ, Touma E, Niforatos W, Kage KL, Burgard EC, van Biesen T, Kowaluk EA, Jarvis MF (Dec 1999). "Molecular and functional characterization of human P2X(2) receptors". Mol Pharmacol. 56 (6): 1171–81. PMID 10570044.
4. Brake AJ, Wagenbach MJ, Julius D (Oct 1994). "New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor". Nature. 371 (6497): 519–23. doi:10.1038/371519a0. PMID 7523952.
5. "Entrez Gene: P2RX2 purinergic receptor P2X, ligand-gated ion channel, 2".

Further reading

• North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
• Barrera NP, Ormond SJ, Henderson RM, et al. (2005). "Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize". J. Biol. Chem. 280 (11): 10759–65. doi:10.1074/jbc.M412265200. PMID 15657042.
• Mason HS, Bourke S, Kemp PJ (2005). "Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species". Mol. Pharmacol. 66 (6): 1525–35. doi:10.1124/mol.104.000851. PMID 15331767.
• Aschrafi A, Sadtler S, Niculescu C, et al. (2004). "Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes". J. Mol. Biol. 342 (1): 333–43. doi:10.1016/j.jmb.2004.06.092. PMID 15313628.
• Boué-Grabot E, Emerit MB, Toulmé E, et al. (2004). "Cross-talk and co-trafficking between rho1/GABA receptors and ATP-gated channels". J. Biol. Chem. 279 (8): 6967–75. doi:10.1074/jbc.M307772200. PMID 14660627.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Järlebark LE, Housley GD, Raybould NP, et al. (2003). "ATP-gated ion channels assembled from P2X2 receptor subunits in the mouse cochlea". NeuroReport. 13 (15): 1979–84. doi:10.1097/00001756-200210280-00030. PMID 12395104.
• Khakh BS, Zhou X, Sydes J, et al. (2000). "State-dependent cross-inhibition between transmitter-gated cation channels". Nature. 406 (6794): 405–10. doi:10.1038/35019066. PMID 10935636.
• Brändle U, Spielmanns P, Osteroth R, et al. (1997). "Desensitization of the P2X(2) receptor controlled by alternative splicing". FEBS Lett. 404 (2–3): 294–8. doi:10.1016/S0014-5793(97)00128-2. PMID 9119082.
• Lewis C, Neidhart S, Holy C, et al. (1995). "Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons". Nature. 377 (6548): 432–5. doi:10.1038/377432a0. PMID 7566120.

External links

• P2RX2 protein, human at the US 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.