KCNK3
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.{{cite journal |vauthors=Duprat F, Lesage F, Fink M, Reyes R, Heurteaux C, Lazdunski M | title = TASK, a human background K+ channel to sense external pH variations near physiological pH | journal = EMBO J | volume = 16 | issue = 17 | pages = 5464–71 |date=Dec 1997 | pmid = 9312005 | pmc = 1170177 | doi = 10.1093/emboj/16.17.5464 }}{{cite journal |vauthors=Lesage F, Lazdunski M | title = Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK (KCNK3) to chromosomes 1q41 and 2p23 | journal = Genomics | volume = 51 | issue = 3 | pages = 478–9 |date=Oct 1998 | pmid = 9721223 | doi = 10.1006/geno.1998.5397 }}{{cite journal |vauthors=Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S | title = International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels | journal = Pharmacol Rev | volume = 57 | issue = 4 | pages = 527–40 |date=Dec 2005 | pmid = 16382106 | doi = 10.1124/pr.57.4.12 | s2cid = 7356601 | url = https://escholarship.org/uc/item/3k15p5vt }}{{cite web | title = Entrez Gene: KCNK3 potassium channel, subfamily K, member 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3777}}
This gene encodes K2P3.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P3.1 is an outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane. Although three transcripts are detected in northern blots, there is currently no sequence available to confirm transcript variants for this gene.
Interactive pathway map
{{NicotineDopaminergicActivity_WP1602|highlight=KCNK3}}
Interactions
KCNK3 has been shown to interact with YWHAB{{cite journal |doi=10.1016/S0092-8674(02)01040-1 |last=O'Kelly |first=Ita |author2=Butler Margaret H |author3=Zilberberg Noam |author4=Goldstein Steve A N |date=Nov 2002 |title=Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals |journal=Cell |volume=111 |issue=4 |pages=577–88 |location = United States| issn = 0092-8674| pmid = 12437930 |s2cid=15898814 |doi-access=free }} and S100A10.{{cite journal |doi=10.1093/emboj/cdf469 |last=Girard |first=Christophe |author2=Tinel Norbert |author3=Terrenoire Cécile |author4=Romey Georges |author5=Lazdunski Michel |author6=Borsotto Marc |date=Sep 2002 |title=p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1 |journal=EMBO J. |volume=21 |issue=17 |pages=4439–48 |location = England| issn = 0261-4189| pmid = 12198146 |pmc=125412 }}
See also
References
{{reflist}}
Further reading
{{refbegin | 2}}
- {{cite journal |vauthors=Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N |title=Potassium leak channels and the KCNK family of two-P-domain subunits. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 175–84 |year= 2001 |pmid= 11256078 |doi=10.1038/35058574 |s2cid=9682396 |url=https://escholarship.org/uc/item/9z7112ns }}
- {{cite journal |vauthors=Patel AJ, Honoré E, Lesage F, etal |title=Inhalational anesthetics activate two-pore-domain background K+ channels. |journal=Nat. Neurosci. |volume=2 |issue= 5 |pages= 422–6 |year= 1999 |pmid= 10321245 |doi= 10.1038/8084 |s2cid=23092576 }}
- {{cite journal |vauthors=Manjunath NA, Bray-Ward P, Goldstein SA, Gallagher PG |title=Assignment of the 2P domain, acid-sensitive potassium channel OAT1 gene KCNK3 to human chromosome bands 2p24.1→p23.3 and murine 5B by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=86 |issue= 3–4 |pages= 242–3 |year= 2000 |pmid= 10575216 |doi=10.1159/000015349 |s2cid=9629583 }}
- {{cite journal |vauthors=Lopes CM, Gallagher PG, Buck ME, etal |title=Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16969–78 |year= 2000 |pmid= 10748056 |doi= 10.1074/jbc.M001948200 |doi-access= free }}
- {{cite journal |vauthors=Ashmole I, Goodwin PA, Stanfield PR |title=TASK-5, a novel member of the tandem pore K+ channel family. |journal=Pflügers Arch. |volume=442 |issue= 6 |pages= 828–33 |year= 2002 |pmid= 11680614 |doi=10.1007/s004240100620 |s2cid=27704471 }}
- {{cite journal |vauthors=Talley EM, Bayliss DA |title=Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) potassium channels: volatile anesthetics and neurotransmitters share a molecular site of action. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17733–42 |year= 2002 |pmid= 11886861 |doi= 10.1074/jbc.M200502200 |doi-access= free }}
- {{cite journal |vauthors=Buist SC, Cherrington NJ, Choudhuri S, etal |title=Gender-specific and developmental influences on the expression of rat organic anion transporters. |journal=J. Pharmacol. Exp. Ther. |volume=301 |issue= 1 |pages= 145–51 |year= 2002 |pmid= 11907168 |doi=10.1124/jpet.301.1.145 }}
- {{cite journal |vauthors=Barbuti A, Ishii S, Shimizu T, etal |title=Block of the background K(+) channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor. |journal=Am. J. Physiol. Heart Circ. Physiol. |volume=282 |issue= 6 |pages= H2024–30 |year= 2002 |pmid= 12003807 |doi= 10.1152/ajpheart.00956.2001 }}
- {{cite journal |vauthors=Girard C, Tinel N, Terrenoire C, etal |title=p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1. |journal=EMBO J. |volume=21 |issue= 17 |pages= 4439–48 |year= 2002 |pmid= 12198146 |doi=10.1093/emboj/cdf469 | pmc=125412 }}
- {{cite journal |vauthors=O'Kelly I, Butler MH, Zilberberg N, Goldstein SA |title=Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. |journal=Cell |volume=111 |issue= 4 |pages= 577–88 |year= 2002 |pmid= 12437930 |doi=10.1016/S0092-8674(02)01040-1 |s2cid=15898814 |doi-access=free }}
- {{cite journal |vauthors=Aslamkhan A, Han YH, Walden R, etal |title=Stoichiometry of organic anion/dicarboxylate exchange in membrane vesicles from rat renal cortex and hOAT1-expressing cells. |journal=Am. J. Physiol. Renal Physiol. |volume=285 |issue= 4 |pages= F775–83 |year= 2003 |pmid= 12837685 |doi= 10.1152/ajprenal.00140.2003 }}
- {{cite journal | author=Strebel K |title=HIV-1 Vpu: putting a channel to the TASK. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 150–2 |year= 2004 |pmid= 15099514 |doi=10.1016/S1097-2765(04)00205-9 |doi-access=free }}
- {{cite journal |vauthors=Hsu K, Seharaseyon J, Dong P, etal |title=Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 259–67 |year= 2004 |pmid= 15099524 |doi=10.1016/S1097-2765(04)00183-2 |doi-access=free }}
- {{cite journal |vauthors=Rusznák Z, Pocsai K, Kovács I, etal |title=Differential distribution of TASK-1, TASK-2 and TASK-3 immunoreactivities in the rat and human cerebellum. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 12 |pages= 1532–42 |year= 2004 |pmid= 15197476 |doi= 10.1007/s00018-004-4082-3 |s2cid=11439105 |pmc=11138546 }}
- {{cite journal |vauthors=Bai X, Greenwood SL, Glazier JD, etal |title=Localization of TASK and TREK, two-pore domain K+ channels, in human cytotrophoblast cells. |journal=J. Soc. Gynecol. Investig. |volume=12 |issue= 2 |pages= 77–83 |year= 2005 |pmid= 15695101 |doi= 10.1016/j.jsgi.2004.08.004 |s2cid=20173840 }}
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External links
- {{MeshName|KCNK3+protein,+human}}
{{NLM content}}
{{Ion channels|g3}}
{{membrane-protein-stub}}