KCNK3

Protein-coding gene in the species Homo sapiens
KCNK3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

6RV2, 6RV3, 6RV4

Identifiers
AliasesKCNK3, K2p3.1, OAT1, PPH4, TASK, TASK-1, TBAK1, potassium two pore domain channel subfamily K member 3, TASK1
External IDsOMIM: 603220 MGI: 1100509 HomoloGene: 1692 GeneCards: KCNK3
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for KCNK3
Genomic location for KCNK3
Band2p23.3Start26,692,722 bp[1]
End26,733,420 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for KCNK3
Genomic location for KCNK3
Band5 B1|5 16.68 cMStart30,745,514 bp[2]
End30,782,615 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left adrenal gland

  • adrenal cortex

  • lower lobe of lung

  • right lung

  • pons

  • upper lobe of lung

  • upper lobe of left lung

  • cerebellar vermis

  • body of pancreas

  • frontal pole
Top expressed in
  • adrenal gland

  • brown adipose tissue

  • myocardium of ventricle

  • right ventricle

  • cerebellar cortex

  • facial motor nucleus

  • cardiac muscles

  • cerebellar vermis

  • interventricular septum

  • left ventricle
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
SpeciesHumanMouse
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 MbChr 5: 30.75 – 30.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.[5][6][7][8]

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.[8]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.[§ 1]

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NicotineDopaminergic_WP1602go to articlego to articlego to articleGo to articlego to articleGo to articleGo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articleGo to articlego to articlego to articlego to articlego to articleGo to articleGo to articlego to articleGo to articleGo to articleGo to articlego to articleGo to articleGo to articleGo to articlego to articlego to articlego to articlego to articlego to articlego to articleGo to articlego to articleGo to articleGo to articlego to articlego to articleGo to articlego to articleGo to articleGo to articlego to article
|alt=Nicotine Activity on Dopaminergic Neurons edit]]
Nicotine Activity on Dopaminergic Neurons edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".

Interactions

KCNK3 has been shown to interact with YWHAB[9] and S100A10.[10]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171303 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000049265 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Duprat F, Lesage F, Fink M, Reyes R, Heurteaux C, Lazdunski M (Dec 1997). "TASK, a human background K+ channel to sense external pH variations near physiological pH". EMBO J. 16 (17): 5464–71. doi:10.1093/emboj/16.17.5464. PMC 1170177. PMID 9312005.
  6. ^ Lesage F, Lazdunski M (Oct 1998). "Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK (KCNK3) to chromosomes 1q41 and 2p23". Genomics. 51 (3): 478–9. doi:10.1006/geno.1998.5397. PMID 9721223.
  7. ^ 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. S2CID 7356601.
  8. ^ a b "Entrez Gene: KCNK3 potassium channel, subfamily K, member 3".
  9. ^ O'Kelly, Ita; Butler Margaret H; Zilberberg Noam; Goldstein Steve A N (Nov 2002). "Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals". Cell. 111 (4). United States: 577–88. doi:10.1016/S0092-8674(02)01040-1. ISSN 0092-8674. PMID 12437930. S2CID 15898814.
  10. ^ Girard, Christophe; Tinel Norbert; Terrenoire Cécile; Romey Georges; Lazdunski Michel; Borsotto Marc (Sep 2002). "p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1". EMBO J. 21 (17). England: 4439–48. doi:10.1093/emboj/cdf469. ISSN 0261-4189. PMC 125412. PMID 12198146.

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. S2CID 9682396.
  • 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. PMID 10321245. S2CID 23092576.
  • 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. PMID 10575216. S2CID 9629583.
  • 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. PMID 10748056.
  • 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. PMID 11680614. S2CID 27704471.
  • 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. PMID 11886861.
  • 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. PMID 11907168.
  • 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. PMID 12003807.
  • 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. PMC 125412. PMID 12198146.
  • 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. PMID 12437930. S2CID 15898814.
  • 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. PMID 12837685.
  • 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. PMID 15099514.
  • 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. PMID 15099524.
  • 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. S2CID 11439105.
  • 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. PMID 15695101. S2CID 20173840.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl: Chloride channel
H+: Proton channel
M+: CNG cation channel
M+: TRP cation channel
H2O (+ solutes): Porin
Cytoplasm: Gap junction
By gating mechanism
Ion channel class
see also disorders
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