KCNK5
Potassium channel, two pore domain subfamily K, member 5 | |||||||||||||
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Identifiers | |||||||||||||
Symbols | KCNK5 ; K2p5.1; KCNK5b; TASK-2; TASK2 | ||||||||||||
External IDs | OMIM: 603493 MGI: 1336175 HomoloGene: 2773 IUPHAR: 517 GeneCards: KCNK5 Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 8645 | 16529 | |||||||||||
Ensembl | ENSG00000164626 | ENSMUSG00000023243 | |||||||||||
UniProt | O95279 | Q80XE0 | |||||||||||
RefSeq (mRNA) | NM_003740 | NM_021542 | |||||||||||
RefSeq (protein) | NP_003731 | NP_067517 | |||||||||||
Location (UCSC) |
Chr 6: 39.19 – 39.23 Mb |
Chr 14: 20.14 – 20.18 Mb | |||||||||||
PubMed search | |||||||||||||
Potassium channel subfamily K member 5 is a protein that in humans is encoded by the KCNK5 gene.[1][2][3]
This gene encodes K2P5.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. The message for this gene is mainly expressed in the cortical distal tubules and collecting ducts of the kidney. The protein is highly sensitive to external pH and this, in combination with its expression pattern, suggests it may play an important role in renal potassium transport.[3]
See also
References
- ↑ Reyes R, Duprat F, Lesage F, Fink M, Salinas M, Farman N, Lazdunski M (Dec 1998). "Cloning and expression of a novel pH-sensitive two pore domain K+ channel from human kidney". J Biol Chem 273 (47): 30863–9. doi:10.1074/jbc.273.47.30863. PMID 9812978.
- ↑ Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S (Dec 2005). "International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels". Pharmacol Rev 57 (4): 527–40. doi:10.1124/pr.57.4.12. PMID 16382106.
- 1 2 "Entrez Gene: KCNK5 potassium channel, subfamily K, member 5".
Further reading
- Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nat. Rev. Neurosci. 2 (3): 175–84. doi:10.1038/35058574. PMID 11256078.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Gray AT, Zhao BB, Kindler CH, et al. (2000). "Volatile anesthetics activate the human tandem pore domain baseline K+ channel KCNK5". Anesthesiology 92 (6): 1722–30. doi:10.1097/00000542-200006000-00032. PMID 10839924.
- 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.
- Morton MJ, O'Connell AD, Sivaprasadarao A, Hunter M (2003). "Determinants of pH sensing in the two-pore domain K(+) channels TASK-1 and -2". Pflugers Arch. 445 (5): 577–83. doi:10.1007/s00424-002-0901-2. PMID 12634929.
- Niemeyer MI, Cid LP, Valenzuela X, et al. (2004). "Extracellular conserved cysteine forms an intersubunit disulphide bridge in the KCNK5 (TASK-2) K+ channel without having an essential effect upon activity". Mol. Membr. Biol. 20 (2): 185–91. doi:10.1080/0968768031000084181. PMID 12851074.
- 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.
- Rusznák Z, Pocsai K, Kovács I, et al. (2004). "Differential distribution of TASK-1, TASK-2 and TASK-3 immunoreactivities in the rat and human cerebellum". Cell. Mol. Life Sci. 61 (12): 1532–42. doi:10.1007/s00018-004-4082-3. PMID 15197476.
- 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.
External links
- KCNK5 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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