KCNK3

KCNK3
Available structures PDB Ortholog search:PDBeRCSB List of PDB id codes 6RV2,6RV3,6RV4
Identifiers
Aliases	KCNK3,K2p3.1, OAT1, PPH4, TASK, TASK-1, TBAK1, potassium two pore domain channel subfamily K member 3, TASK1
External IDs	OMIM:603220;MGI:1100509;HomoloGene:1692;GeneCards:KCNK3;OMA:KCNK3 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p23.3 Start 26,692,722bp End 26,733,420bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 B1|5 16.68 cM Start 30,745,514bp End 30,782,615bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in left adrenal gland adrenal cortex left adrenal cortex right adrenal cortex beta cell lower lobe of lung right lung paraflocculus of cerebellum pons upper lobe of lung Top expressed in adrenal gland lobe of prostate brown adipose tissue myocardium of ventricle right ventricle cerebellar cortex facial motor nucleus lobe of cerebellum cardiac muscles tunica adventitia of aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function S100 protein binding potassium channel activity protein homodimerization activity open rectifier potassium channel activity potassium ion leak channel activity ion channel activity protein heterodimerization activity growth factor activity protein C-terminus binding protein binding Cellular component integral component of membrane membrane plasma membrane integral component of plasma membrane extracellular space Biological process cochlea development ion transport cellular response to zinc ion potassium ion transport ion transmembrane transport brain development cardiac conduction potassium ion transmembrane transport cellular response to hypoxia negative regulation of cytosolic calcium ion concentration chemical synaptic transmission stabilization of membrane potential regulation of signaling receptor activity Sources:Amigo/QuickGO
Orthologs Species Human Mouse Entrez 3777 16527 Ensembl ENSG00000171303 ENSMUSG00000049265 UniProt O14649 O35111 RefSeq (mRNA) NM_002246 NM_010608 RefSeq (protein) NP_002237 NP_034738 Location (UCSC) Chr 2: 26.69 – 26.73 Mb Chr 5: 30.75 – 30.78 Mb PubMedsearch
Wikidata
View/Edit Human View/Edit Mouse

Potassium channel subfamily K member 3is aproteinthat in humans is encoded by theKCNK3gene.

This gene encodes K_2P3.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K_2P3.1 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

Click on genes, proteins and metabolites below to link to respective articles.

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Nicotine Activity on Dopaminergic Neuronsedit

Interactions

KCNK3 has been shown tointeractwithYWHABandS100A10.

See also

• Tandem pore domain potassium channel

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.PMID11256078.S2CID9682396.
• Patel AJ, Honoré E, Lesage F, et al. (1999). "Inhalational anesthetics activate two-pore-domain background K+ channels".Nat. Neurosci.2(5): 422–6.doi:10.1038/8084.PMID10321245.S2CID23092576.
• Manjunath NA, Bray-Ward P, Goldstein SA, Gallagher PG (2000). "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".Cytogenet. Cell Genet.86(3–4): 242–3.doi:10.1159/000015349(inactive 2024-07-17).PMID10575216.S2CID9629583.{{cite journal}}:CS1 maint: DOI inactive as of July 2024 (link)
• Lopes CM, Gallagher PG, Buck ME, et al. (2000)."Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3".J. Biol. Chem.275(22): 16969–78.doi:10.1074/jbc.M001948200.PMID10748056.
• Ashmole I, Goodwin PA, Stanfield PR (2002). "TASK-5, a novel member of the tandem pore K+ channel family".Pflügers Arch.442(6): 828–33.doi:10.1007/s004240100620.PMID11680614.S2CID27704471.
• Talley EM, Bayliss DA (2002)."Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) potassium channels: volatile anesthetics and neurotransmitters share a molecular site of action".J. Biol. Chem.277(20): 17733–42.doi:10.1074/jbc.M200502200.PMID11886861.
• Buist SC, Cherrington NJ, Choudhuri S, et al. (2002). "Gender-specific and developmental influences on the expression of rat organic anion transporters".J. Pharmacol. Exp. Ther.301(1): 145–51.doi:10.1124/jpet.301.1.145.PMID11907168.
• Barbuti A, Ishii S, Shimizu T, et al. (2002). "Block of the background K(+) channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor".Am. J. Physiol. Heart Circ. Physiol.282(6): H2024–30.doi:10.1152/ajpheart.00956.2001.PMID12003807.
• Girard C, Tinel N, Terrenoire C, et al. (2002)."p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1".EMBO J.21(17): 4439–48.doi:10.1093/emboj/cdf469.PMC125412.PMID12198146.
• O'Kelly I, Butler MH, Zilberberg N, Goldstein SA (2002)."Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals".Cell.111(4): 577–88.doi:10.1016/S0092-8674(02)01040-1.PMID12437930.S2CID15898814.
• Aslamkhan A, Han YH, Walden R, et al. (2003). "Stoichiometry of organic anion/dicarboxylate exchange in membrane vesicles from rat renal cortex and hOAT1-expressing cells".Am. J. Physiol. Renal Physiol.285(4): F775–83.doi:10.1152/ajprenal.00140.2003.PMID12837685.
• Strebel K (2004)."HIV-1 Vpu: putting a channel to the TASK".Mol. Cell.14(2): 150–2.doi:10.1016/S1097-2765(04)00205-9.PMID15099514.
• Hsu K, Seharaseyon J, Dong P, et al. (2004)."Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel".Mol. Cell.14(2): 259–67.doi:10.1016/S1097-2765(04)00183-2.PMID15099524.
• 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.PMC11138546.PMID15197476.S2CID11439105.
• Bai X, Greenwood SL, Glazier JD, et al. (2005). "Localization of TASK and TREK, two-pore domain K+ channels, in human cytotrophoblast cells".J. Soc. Gynecol. Investig.12(2): 77–83.doi:10.1016/j.jsgi.2004.08.004.PMID15695101.S2CID20173840.

External links

• KCNK3+protein,+humanat the U.S. National Library of MedicineMedical Subject Headings(MeSH)

This article incorporates text from theUnited States National Library of Medicine,which is in thepublic domain.