P2RX5

Purinergic receptor P2X, ligand-gated ion channel, 5
Identifiers
Symbols	P2RX5; LRH-1; MGC47755; P2X5; P2X5R
External IDs	OMIM: 602836 MGI: 2137026 HomoloGene: 1924 IUPHAR: P2X5 GeneCards: P2RX5 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 Cellular component • integral to plasma membrane • membrane Biological process • transport • cation transport • signal transduction • nervous system development • positive regulation of calcium ion transport into cytosol • purinergic nucleotide receptor signaling pathway • purinergic nucleotide receptor signaling pathway • positive regulation of calcium-mediated signaling Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5026	94045
Ensembl	ENSG00000083454	ENSMUSG00000005950
UniProt	Q93086	Q3UYI1
RefSeq (mRNA)	NM_001204519.1	NM_033321.3
RefSeq (protein)	NP_001191448.1	NP_201578.2
Location (UCSC)	Chr 17: 3.58 – 3.6 Mb	Chr 11: 72.97 – 72.99 Mb
PubMed search	[1]	[2]

P2X purinoceptor 5 is a protein that in humans is encoded by the P2RX5 gene.^[1][2]

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Several characteristic motifs of ATP-gated channels are present in its primary structure, but, unlike other members of the purinoceptors family, this receptor has only a single transmembrane domain. Four transcript variants encoding distinct isoforms have been identified for this gene.^[2]

See also

• P2X receptor

References

1. ^ Le KT, Paquet M, Nouel D, Babinski K, Seguela P (Jan 1998). "Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system". FEBS Lett 418 (1–2): 195–9. doi:10.1016/S0014-5793(97)01380-X. PMID 9414125. 
2. ^ ^{a b} "Entrez Gene: P2RX5 purinergic receptor P2X, ligand-gated ion channel, 5". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5026. 

Further reading

• North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951. 
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146. 
• Touchman JW, Anikster Y, Dietrich NL, et al. (2000). "The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion". Genome Res. 10 (2): 165–73. doi:10.1101/gr.10.2.165. PMC 310836. PMID 10673275. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310836. 
• 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. 
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
• Greig AV, Linge C, Terenghi G, et al. (2003). "Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes". J. Invest. Dermatol. 120 (6): 1007–15. doi:10.1046/j.1523-1747.2003.12261.x. PMID 12787128. 
• Greig AV, Linge C, Healy V, et al. (2003). "Expression of purinergic receptors in non-melanoma skin cancers and their functional roles in A431 cells". J. Invest. Dermatol. 121 (2): 315–27. doi:10.1046/j.1523-1747.2003.12379.x. PMID 12880424. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• de Rijke B, van Horssen-Zoetbrood A, Beekman JM, et al. (2006). "A frameshift polymorphism in P2X5 elicits an allogeneic cytotoxic T lymphocyte response associated with remission of chronic myeloid leukemia". J. Clin. Invest. 115 (12): 3506–16. doi:10.1172/JCI24832. PMC 1297240. PMID 16322791. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1297240. 
• Metcalfe MJ, Baker DM, Burnstock G (2007). "Purinoceptor expression on keratinocytes reflects their function on the epidermis during chronic venous insufficiency". Arch. Dermatol. Res. 298 (6): 301–7. doi:10.1007/s00403-006-0693-x. PMID 16967306. 
• Duckwitz W, Hausmann R, Aschrafi A, Schmalzing G (2007). "P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate". J. Biol. Chem. 281 (51): 39561–72. doi:10.1074/jbc.M606113200. PMID 17001079. 

External links

• MeSH P2RX5+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)