P2RX5

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Purinergic receptor P2X, ligand-gated ion channel, 5
Identifiers
Symbols P2RX5; MGC47755; P2X5; P2X5R
External IDs OMIM: 602836 MGI: 2137026 HomoloGene: 1924
Orthologs
Human Mouse
Entrez 5026 94045
Ensembl n/a ENSMUSG00000005950
Refseq NM_002561 (mRNA)
NP_002552 (protein)		 NM_033321 (mRNA)
NP_201578 (protein)
Location n/a Chr 11: 72.98 - 72.99 Mb
Pubmed search [1] [2]

Purinergic receptor P2X, ligand-gated ion channel, 5, also known as P2RX5, is a human gene.[1]

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. Three transcript variants encoding distinct isoforms have been identified for this gene.[1]

Contents

See also

References

  1. ^ a b "Entrez Gene: P2RX5 purinergic receptor P2X, ligand-gated ion channel, 5".

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. PMID 9110174. 
  • Lê KT, Paquet M, Nouel D, et al. (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. PMID 9414125. 
  • 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. PMID 10673275. 
  • 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. PMID 12477932. 
  • 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. 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. PMID 16322791. 
  • 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

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v • d • e
Ion channel, receptor: ligand-gated ion channels
Cys-loop receptors
5-HT3 (A, B, C, D, E)
GABA A (α1, α2, α3, α4, α5, α6, β1, β2, β3, γ1, γ2, γ3, δ, ε, π, θ) • GABA C (ρ1, ρ2, ρ3)
α1 • α2 • α3 • α4 • β
monomers: α1 • α2 • α3 • α4 • α5 • α6 • α7 • α9 • α10 • β1 • β2 • β3 • β4 • δ • ε
pentamers: (α4)2(β2)3 • (α7)5 • (α1)2(β4)3 - Ganglion type • (α1)2β1δε - Muscle type
Ionotropic glutamates
AMPA (1, 2, 3, 4) • Kainate (1, 2, 3, 4, 5)  • NMDA (1, 2A, 2B, 2C, 2D, 3A, 3B, L1A, L1B)
ATP-gated channels

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  • This page was last modified on 10 July 2008, at 04:52.

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