P2RX6

Purinergic receptor P2X, ligand-gated ion channel, 6
Identifiers
Symbols	P2RX6; MGC129625; P2RXL1; P2X6; P2XM
External IDs	OMIM: 608077 MGI: 1337113 HomoloGene: 3975 IUPHAR: GeneCards: P2RX6 Gene
Gene Ontology Molecular function • purinergic nucleotide receptor activity • purinergic nucleotide receptor activity • transmembrane receptor activity • extracellular ATP-gated cation channel activity • extracellular ATP-gated cation channel activity • ion channel activity • ATP binding • channel activity • identical protein binding Cellular component • membrane fraction • cytoplasm • integral to plasma membrane • postsynaptic density • membrane • cell junction • neuronal cell body • dendritic spine Biological process • transport • cation transport • muscle contraction • signal transduction • purinergic nucleotide receptor signaling pathway • purinergic nucleotide receptor signaling pathway • protein homooligomerization • protein heterooligomerization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9127	18440
Ensembl	ENSG00000099957	ENSMUSG00000022758
UniProt	O15547	Q3UUD0
RefSeq (mRNA)	NM_001159554.1	NM_011028
RefSeq (protein)	NP_001153026.1	NP_035158
Location (UCSC)	Chr 22: 21.37 – 21.38 Mb	Chr 16: 17.56 – 17.58 Mb
PubMed search	[1]	[2]

P2X purinoceptor 6 is a protein that in humans is encoded by the P2RX6 gene.^[1][2][3][4]

The protein encoded by this gene belongs to the family of P2X receptors, which are ATP-gated ion channels and mediate rapid and selective permeability to cations. This gene is predominantly expressed in skeletal muscle, and regulated by p53. The encoded protein is associated with VE-cadherin at the adherens junctions of human umbilical vein endothelial cells.^[4]

See also

• Purinergic receptor

References

1. ^ Urano T, Nishimori H, Han H, Furuhata T, Kimura Y, Nakamura Y, Tokino T (Sep 1997). "Cloning of P2XM, a novel human P2X receptor gene regulated by p53". Cancer Res 57 (15): 3281–7. PMID 9242461. 
2. ^ Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al. (Dec 1999). "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208. 
3. ^ Collo G, North RA, Kawashima E, Merlo-Pich E, Neidhart S, Surprenant A, Buell G (Sep 1996). "Cloning OF P2X5 and P2X6 receptors and the distribution and properties of an extended family of ATP-gated ion channels". J Neurosci 16 (8): 2495–507. PMID 8786426. 
4. ^ ^{a b} "Entrez Gene: P2RXL1 purinergic receptor P2X-like 1, orphan receptor". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9127. 

Further reading

• Khakh BS, Burnstock G, Kennedy C, et al. (2001). "International union of pharmacology. XXIV. Current status of the nomenclature and properties of P2X receptors and their subunits.". Pharmacol. Rev. 53 (1): 107–18. PMID 11171941. 
• Soto F, Garcia-Guzman M, Karschin C, Stühmer W (1996). "Cloning and tissue distribution of a novel P2X receptor from rat brain.". Biochem. Biophys. Res. Commun. 223 (2): 456–60. doi:10.1006/bbrc.1996.0915. PMID 8670303. 
• Glass R, Loesch A, Bodin P, Burnstock G (2002). "P2X4 and P2X6 receptors associate with VE-cadherin in human endothelial cells.". Cell. Mol. Life Sci. 59 (5): 870–81. doi:10.1007/s00018-002-8474-y. PMID 12088286. 
• Maguire PB, Wynne KJ, Harney DF, et al. (2003). "Identification of the phosphotyrosine proteome from thrombin activated platelets.". Proteomics 2 (6): 642–8. doi:10.1002/1615-9861(200206)2:6<642::AID-PROT642>3.0.CO;2-I. PMID 12112843. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=545604. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 

External links

• MeSH P2RXL1+protein,+human

Ionotropic glutamates

Ligand-gated only	AMPA (1, 2, 3, 4) · Kainate (1, 2, 3, 4, 5)
Voltage- and ligand-gated	NMDA (1, 2A, 2B, 2C, 2D, 3A, 3B, L1A, L1B)
‘Orphan’	GluD (δ1, δ2)

ATP-gated channels

Purinergic receptors

P2X (1, 2, 3, 4, 5, 6, 7)

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)