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Available structures
PDBOrtholog search: PDBe RCSB
AliasesKCNK4, K2p4.1, TRAAK, TRAAK1, potassium two pore domain channel subfamily K member 4, FHEIG
External IDsOMIM: 605720 MGI: 1298234 HomoloGene: 7391 GeneCards: KCNK4
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for KCNK4
Genomic location for KCNK4
Band11q13.1Start64,291,302 bp[1]
End64,300,031 bp[1]
RNA expression pattern
PBB GE KCNK4 219883 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 11: 64.29 – 64.3 MbChr 19: 6.92 – 6.93 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Potassium channel subfamily K member 4 is a protein that in humans is encoded by the KCNK4 gene.[5][6][7]


Potassium channels play a role in many cellular processes including maintenance of the action potential, muscle contraction, hormone secretion, osmotic regulation, and ion flow. This gene encodes the K2P4.1 protein, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P4.1 homodimerizes and functions as an outwardly rectifying channel. It is expressed primarily in neural tissues and is stimulated by membrane stretch and polyunsaturated fatty acids.[7]

KCNK4 protein channels are also called TRAAK channels. TRAAK channels are found in mammalian neurons and are part of a protein family of weakly inward rectifying potassium channels. This subfamily of potassium channels is mechanically gated. The C-terminal of TRAAK has a charged cluster that is important in maintaining the mechanosensitive properties of the channel.[8]

TRAAK is only expressed in neuronal tissue, and can be found in the brain, spinal cord, and retina, which suggests that it has a function beyond mechanotransduction in terms of neuronal excitability.[9] The highest levels of TRAAK expression are in the olfactory system, cerebral cortex, hippocampal formation, habenula, basal ganglia, and cerebellum.[9] TRAAK channels are mechanically activated when there is a convex curvature in the membrane that alters the channel’s activity. TRAAK channels are thought to have a role in axonal pathfinding, growth cone motility, and neurite elongation, as well as possibly having a role in touch or pain detection.[10][11]

See also


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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000182450 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024957 - 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. ^ Lesage F, Maingret F, Lazdunski M (May 2000). "Cloning and expression of human TRAAK, a polyunsaturated fatty acids-activated and mechano-sensitive K(+) channel". FEBS Lett. 471 (2–3): 137–40. doi:10.1016/S0014-5793(00)01388-0. PMID 10767409.
  6. ^ 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.
  7. ^ a b "Entrez Gene: KCNK4 potassium channel, subfamily K, member 4".
  8. ^ Patel AJ, Honoré E, Lesage F, Fink M, Romey G, Lazdunski M (1999). "Inhalational anesthetics activate two-pore-domain background K+ channels". Nature Neuroscience. 2 (5): 422–426. doi:10.1038/8084. PMID 10321245.
  9. ^ a b Fink M, Lesage F, Duprat F, Heurteaux C, Reyes R, Fosset M, Lazdunski M (1998). "A neuronal two P domain K+ channel stimulated by arachidonic acid and polyunsaturated fatty acids". The EMBO Journal. 17 (12): 3297–3308. doi:10.1093/emboj/17.12.3297. PMC 1170668. PMID 9628867.
  10. ^ Vandorpe DH, Morris CE (1992). "Stretch activation of the Aplysia S-channel". The Journal of Membrane Biology. 127 (3): 205–214. doi:10.1007/bf00231508. PMID 1495087.
  11. ^ Maingret F, Fosset M, Lesage F, Lazdunski M, Honoré E (1999). "TRAAK is a mammalian neuronal mechano-gated K+ channel". The Journal of Biological Chemistry. 274 (3): 1381–1387. doi:10.1074/jbc.274.3.1381. PMID 9880510.

Further reading

External links

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