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Wikipedia

P2RX2

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

P2RX2
Identifiers
AliasesP2RX2, DFNA41, P2X2, purinergic receptor P2X 2
External IDsOMIM: 600844 MGI: 2665170 HomoloGene: 14251 GeneCards: P2RX2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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: 110.49 – 110.49 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a cation conducting 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]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000187848 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029503 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. doi:10.1124/mol.56.6.1171. 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. Bibcode:1994Natur.371..519B. doi:10.1038/371519a0. PMID 7523952. S2CID 4371044.
  7. ^ a b "Entrez Gene: P2RX2 purinergic receptor P2X, ligand-gated ion channel, 2".

Further reading edit

  • 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. S2CID 24536809.
  • 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. Bibcode:2002PNAS...9916899M. 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. S2CID 10991307.
  • Khakh BS, Zhou X, Sydes J, et al. (2000). "State-dependent cross-inhibition between transmitter-gated cation channels" (PDF). Nature. 406 (6794): 405–10. Bibcode:2000Natur.406..405K. doi:10.1038/35019066. PMID 10935636. S2CID 4500837.
  • 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. S2CID 39951168.
  • 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. Bibcode:1995Natur.377..432L. doi:10.1038/377432a0. PMID 7566120. S2CID 4361850.

External links edit

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


p2rx2, purinoceptor, protein, that, humans, encoded, gene, identifiersaliases, dfna41, p2x2, purinergic, receptor, 2external, idsomim, 600844, 2665170, homologene, 14251, genecards, gene, location, human, chromosome, human, band12q24, 33start132, end132, gene,. P2X purinoceptor 2 is a protein that in humans is encoded by the P2RX2 gene 5 6 7 P2RX2IdentifiersAliasesP2RX2 DFNA41 P2X2 purinergic receptor P2X 2External IDsOMIM 600844 MGI 2665170 HomoloGene 14251 GeneCards P2RX2Gene location Human Chr Chromosome 12 human 1 Band12q24 33Start132 618 776 bp 1 End132 622 388 bp 1 Gene location Mouse Chr Chromosome 5 mouse 2 Band5 5 FStart110 487 678 bp 2 End110 491 078 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed ingastric mucosaright lungright uterine tubeprostatecaput epididymiscorpus epididymishippocampus properspleenupper lobe of left lungamygdalaTop expressed inotolith organutricleseminiferous tubulespermatocytespermatidcochleastria vascularisprostateGreater petrosal nerveneural tubeMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionpurinergic nucleotide receptor activity extracellularly ATP gated cation channel activity ion channel activity ligand gated ion channel activity identical protein binding ATP binding ATP gated ion channel activityCellular componentintegral component of membrane membrane receptor complex integral component of nuclear inner membrane integral component of plasma membrane intracellular anatomical structure apical plasma membrane plasma membrane postsynapse neuronal cell bodyBiological processperistalsis 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 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 excitatory postsynaptic potential response to ischemia cation transport ion transmembrane transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez22953231602EnsemblENSG00000187848ENSMUSG00000029503UniProtQ9UBL9Q8K3P1RefSeq mRNA NM 001282164NM 001282165NM 012226NM 016318NM 170682NM 170683NM 174872NM 174873NM 001164833NM 001164834NM 153400NM 001310700NM 001310701RefSeq protein NP 001269093NP 001269094NP 036358NP 057402NP 733782NP 733783NP 777361NP 777362NP 001158305NP 001158306NP 001297629NP 001297630NP 700449Location UCSC Chr 12 132 62 132 62 MbChr 5 110 49 110 49 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThe product of this gene belongs to the family of purinoceptors for ATP This receptor functions as a cation conducting 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 References edit a b c GRCh38 Ensembl release 89 ENSG00000187848 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000029503 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 doi 10 1124 mol 56 6 1171 PMID 10570044 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 Bibcode 1994Natur 371 519B doi 10 1038 371519a0 PMID 7523952 S2CID 4371044 a b Entrez Gene P2RX2 purinergic receptor P2X ligand gated ion channel 2 Further reading editNorth 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 S2CID 24536809 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 Boue Grabot E Emerit MB Toulme 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 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Jarlebark 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 S2CID 10991307 Khakh BS Zhou X Sydes J et al 2000 State dependent cross inhibition between transmitter gated cation channels PDF Nature 406 6794 405 10 Bibcode 2000Natur 406 405K doi 10 1038 35019066 PMID 10935636 S2CID 4500837 Brandle 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 S2CID 39951168 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 Bibcode 1995Natur 377 432L doi 10 1038 377432a0 PMID 7566120 S2CID 4361850 External links editP2RX2 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 nbsp This membrane protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title P2RX2 amp oldid 1167340722, wikipedia, wiki, book, books, library,

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