KCNK3
| KCNK3 | |||
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Gene ontology | |||
| Molecular function | |||
| Cellular component | |||
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| Sources:Amigo / QuickGO | |||
Ensembl | |||||||||
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| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr 2: 26.69 – 26.73 Mb | Chr 5: 30.75 – 30.78 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/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]
Nicotine Activity on Dopaminergic Neurons edit
- ^ The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".
Interactions
KCNK3 has been shown to
See also
- Tandem pore domain potassium channel
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000171303 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000049265 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 9312005.
- PMID 9721223.
- S2CID 7356601.
- ^ a b "Entrez Gene: KCNK3 potassium channel, subfamily K, member 3".
- S2CID 15898814.
- 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 12837685.
- Strebel K (2004). "HIV-1 Vpu: putting a channel to the TASK". Mol. Cell. 14 (2): 150–2. 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. 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. 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. S2CID 20173840.
External links
- KCNK3+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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