P2RX5
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
- ↑ 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.
- ↑ 2.0 2.1 "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. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- 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.
- 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.
- 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.
- 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
- P2RX5 protein, human at the US 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.
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