P2RX2

P2RX2
Identifiers
AliasesP2RX2, DFNA41, P2X2, purinergic receptor P2X 2
External IDsMGI: 2665170 HomoloGene: 14251 GeneCards: P2RX2
Gene location (Human)
Chr.Chromosome 12 (human)[1]
Band12q24.33Start132,618,776 bp[1]
End132,622,386 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

22953

231602

Ensembl

ENSG00000187848

ENSMUSG00000029503

UniProt

Q9UBL9

Q8K3P1

RefSeq (mRNA)

NM_001164833
NM_001164834
NM_153400
NM_001310700
NM_001310701

RefSeq (protein)

NP_001158305
NP_001158306
NP_001297629
NP_001297630
NP_700449

Location (UCSC)Chr 12: 132.62 – 132.62 MbChr 5: 110.34 – 110.34 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

P2X purinoceptor 2 is a protein that in humans is encoded by the P2RX2 gene.[5][6][7]

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.[7]

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000187848 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029503 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. ↑ 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.
  7. 1 2 "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.

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


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