KCNK4: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Potassium channel subfamily K member 4''' is a [[protein]] that in humans is encoded by the ''KCNK4'' [[gene]].<ref name="pmid10767409">{{cite journal |vauthors=Lesage F, Maingret F, Lazdunski M | title = Cloning and expression of human TRAAK, a polyunsaturated fatty acids-activated and mechano-sensitive K(+) channel | journal = FEBS Lett | volume = 471 | issue = 2–3 | pages = 137–40 |date=May 2000 | pmid = 10767409 | pmc =  | doi =10.1016/S0014-5793(00)01388-0  }}</ref><ref name="pmid16382106">{{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 | pmc = | doi = 10.1124/pr.57.4.12 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: KCNK4 potassium channel, subfamily K, member 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50801| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Potassium channel, subfamily K, member 4
| HGNCid = 6279
| Symbol = KCNK4
| AltSymbols =; K2p4.1; TRAAK; TRAAK1
| OMIM = 605720
| ECnumber = 
| Homologene = 7391
| MGIid = 1298234
| GeneAtlas_image1 = PBB_GE_KCNK4_219883_at_tn.png
| Function = {{GNF_GO|id=GO:0005244 |text = voltage-gated ion channel activity}} {{GNF_GO|id=GO:0005267 |text = potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 50801
    | Hs_Ensembl = ENSG00000182450
    | Hs_RefseqProtein = NP_201567
    | Hs_RefseqmRNA = NM_033310
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 63815770
    | Hs_GenLoc_end = 63828817
    | Hs_Uniprot = Q9NYG8
    | Mm_EntrezGene = 16528
    | Mm_Ensembl = ENSMUSG00000024957
    | Mm_RefseqmRNA = NM_008431
    | Mm_RefseqProtein = NP_032457
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 6992734
    | Mm_GenLoc_end = 7001559
    | Mm_Uniprot = Q0VD85
  }}
}}
'''Potassium channel, subfamily K, member 4''', also known as '''KCNK4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNK4 potassium channel, subfamily K, member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50801| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Potassium channel]]s 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 K<sub>2P</sub>4.1 protein, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K<sub>2P</sub>4.1 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.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
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-terminus|C-terminal]] of TRAAK has a charged cluster that is important in maintaining the mechanosensitive properties of the channel.<ref>{{Cite journal
| summary_text = 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 one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. The encoded protein 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.<ref name="entrez">{{cite web | title = Entrez Gene: KCNK4 potassium channel, subfamily K, member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50801| accessdate = }}</ref>
|vauthors=Patel AJ, Honoré E, Lesage F, Fink M, Romey G, Lazdunski M | title = Inhalational anesthetics activate two-pore-domain background K+ channels
}}
| journal = Nature Neuroscience
| volume = 2
| issue = 5
| pages = 422–426
| doi = 10.1038/8084
| year = 1999
| pmid = 10321245
}}</ref>
 
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.<ref name = "pmid9628867">{{Cite journal
|vauthors=Fink M, Lesage F, Duprat F, Heurteaux C, Reyes R, Fosset M, Lazdunski M | doi = 10.1093/emboj/17.12.3297
| title = A neuronal two P domain K+ channel stimulated by arachidonic acid and polyunsaturated fatty acids
| journal = The EMBO Journal
| volume = 17
| issue = 12
| pages = 3297–3308
| pmc = 1170668
| year = 1998
| pmid = 9628867
}}</ref>  The highest levels of TRAAK expression are in the [[olfactory system]], [[cerebral cortex]], [[hippocampal formation]], [[habenula]], [[basal ganglia]], and [[cerebellum]].<ref name = "pmid9628867"/>  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.<ref>{{Cite journal
|vauthors=Vandorpe DH, Morris CE | title = Stretch activation of the Aplysia S-channel
| journal = The Journal of membrane biology
| volume = 127
| issue = 3
| pages = 205–214
| year = 1992
| pmid = 1495087
}}</ref><ref>{{Cite journal
|vauthors=Maingret F, Fosset M, Lesage F, Lazdunski M, Honoré E | title = TRAAK is a mammalian neuronal mechano-gated K+ channel
| journal = The Journal of Biological Chemistry
| volume = 274
| issue = 3
| pages = 1381–1387
| year = 1999
| pmid = 9880510
| doi=10.1074/jbc.274.3.1381
}}</ref>


==See also==
==See also==
Line 58: Line 50:


==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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 }}
| citations =
*{{cite journal  | author=Chapman CG |title=Cloning, localisation and functional expression of a novel human, cerebellum specific, two pore domain potassium channel |journal=Brain Res. Mol. Brain Res. |volume=82 |issue= 1–2 |pages= 74–83 |year= 2001 |pmid= 11042359 |doi=10.1016/S0169-328X(00)00183-2 |name-list-format=vanc| author2=Meadows HJ  | author3=Godden RJ  | display-authors=3 | last4=Campbell  | first4=DA  | last5=Duckworth  | first5=M | last6=Kelsell  | first6=RE  | last7=Murdock  | first7=PR  | last8=Randall  | first8=AD  | last9=Rennie  | first9=GI }}
*{{cite journal  | author=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=  }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Goldstein SA, Bayliss DA, Kim D, ''et al.'' |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 |year= 2006 |pmid= 16382106 |doi= 10.1124/pr.57.4.12 }}
*{{cite journal  | author=Meadows HJ |title=The neuroprotective agent sipatrigine (BW619C89) potently inhibits the human tandem pore-domain K(+) channels TREK-1 and TRAAK |journal=Brain Res. |volume=892 |issue= 1 |pages= 94–101 |year= 2001 |pmid= 11172753 |doi=10.1016/S0006-8993(00)03239-X  |name-list-format=vanc| author2=Chapman CG  | author3=Duckworth DM  | display-authors=3  | last4=Kelsell  | first4=R.E.  | last5=Murdock  | first5=P.R.  | last6=Nasir  | first6=S.  | last7=Rennie  | first7=G.  | last8=Randall  | first8=A.D. }}
*{{cite journal | author=Lesage F, Maingret F, Lazdunski M |title=Cloning and expression of human TRAAK, a polyunsaturated fatty acids-activated and mechano-sensitive K(+) channel. |journal=FEBS Lett. |volume=471 |issue= 2-3 |pages= 137-40 |year= 2000 |pmid= 10767409 |doi= }}
*{{cite journal  | author=Wiemann S |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072  |name-list-format=vanc| author2=Weil B  | author3=Wellenreuther R  | display-authors=3  | last4=Gassenhuber  | first4=J  | last5=Glassl  | first5=S  | last6=Ansorge  | first6=W  | last7=Böcher  | first7=M  | last8=Blöcker  | first8=H  | last9=Bauersachs  | first9=S }}
*{{cite journal | author=Chapman CG, Meadows HJ, Godden RJ, ''et al.'' |title=Cloning, localisation and functional expression of a novel human, cerebellum specific, two pore domain potassium channel. |journal=Brain Res. Mol. Brain Res. |volume=82 |issue= 1-2 |pages= 74-83 |year= 2001 |pmid= 11042359 |doi=  }}
*{{cite journal  | author=Simpson JC |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 | pmc=1083732  |name-list-format=vanc| author2=Wellenreuther R  | author3=Poustka A  | display-authors=3  | last4=Pepperkok  | first4=R  | last5=Wiemann  | first5=S }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  |vauthors=Ozaita A, Vega-Saenz de Miera E |title=Cloning of two transcripts, HKT4.1a and HKT4.1b, from the human two-pore K+ channel gene KCNK4. Chromosomal localization, tissue distribution and functional expression |journal=Brain Res. Mol. Brain Res. |volume=102 |issue= 1–2 |pages= 18–27 |year= 2003 |pmid= 12191490 |doi=10.1016/S0169-328X(02)00157-2 }}
*{{cite journal  | author=Meadows HJ, Chapman CG, Duckworth DM, ''et al.'' |title=The neuroprotective agent sipatrigine (BW619C89) potently inhibits the human tandem pore-domain K(+) channels TREK-1 and TRAAK. |journal=Brain Res. |volume=892 |issue= 1 |pages= 94-101 |year= 2001 |pmid= 11172753 |doi=  }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  |vauthors=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 | pmc=395752 }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  |vauthors=Harinath S, Sikdar SK |title=Trichloroethanol enhances the activity of recombinant human TREK-1 and TRAAK channels |journal=Neuropharmacology |volume=46 |issue= 5 |pages= 750–60 |year= 2004 |pmid= 14996553 |doi= 10.1016/j.neuropharm.2003.11.023 }}
*{{cite journal  | author=Ozaita A, Vega-Saenz de Miera E |title=Cloning of two transcripts, HKT4.1a and HKT4.1b, from the human two-pore K+ channel gene KCNK4. Chromosomal localization, tissue distribution and functional expression. |journal=Brain Res. Mol. Brain Res. |volume=102 |issue= 1-2 |pages= 18-27 |year= 2003 |pmid= 12191490 |doi=  }}
*{{cite journal  | author=Wiemann S |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930  |name-list-format=vanc| author2=Arlt D  | author3=Huber W  | display-authors=3  | last4=Wellenreuther  | first4=R  | last5=Schleeger  | first5=S  | last6=Mehrle  | first6=A  | last7=Bechtel  | first7=S  | last8=Sauermann  | first8=M  | last9=Korf  | first9=U }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Kimura K |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129  |name-list-format=vanc| author2=Wakamatsu A  | author3=Suzuki Y  | display-authors=3  | last4=Ota  | first4=T  | last5=Nishikawa  | first5=T  | last6=Yamashita  | first6=R  | last7=Yamamoto  | first7=J  | last8=Sekine  | first8=M  | last9=Tsuritani  | first9=K }}
*{{cite journal  | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
*{{cite journal  | author=Mehrle A |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 | pmc=1347501  |name-list-format=vanc| author2=Rosenfelder H  | author3=Schupp I  | display-authors=3  | last4=Del Val  | first4=C  | last5=Arlt  | first5=D  | last6=Hahne  | first6=F  | last7=Bechtel  | first7=S  | last8=Simpson  | first8=J  | last9=Hofmann  | first9=O }}
*{{cite journal  | author=Harinath S, Sikdar SK |title=Trichloroethanol enhances the activity of recombinant human TREK-1 and TRAAK channels. |journal=Neuropharmacology |volume=46 |issue= 5 |pages= 750-60 |year= 2004 |pmid= 14996553 |doi= 10.1016/j.neuropharm.2003.11.023 }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
}}
{{refend}}
{{refend}}


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* {{MeshName|KCNK4+protein,+human}}
* {{MeshName|KCNK4+protein,+human}}


{{membrane-protein-stub}}
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{{NLM content}}
{{Ion channels}}
{{Ion channels|g3}}
 
[[Category:Ion channels]]
[[Category:Ion channels]]
{{WikiDoc Sources}}

Revision as of 06:16, 2 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

Potassium channel subfamily K member 4 is a protein that in humans is encoded by the KCNK4 gene.[1][2][3]

Function

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.[3]

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.[4]

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.[5] The highest levels of TRAAK expression are in the olfactory system, cerebral cortex, hippocampal formation, habenula, basal ganglia, and cerebellum.[5] 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.[6][7]

See also

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: KCNK4 potassium channel, subfamily K, member 4".
  4. ↑ 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.
  5. ↑ 5.0 5.1 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.
  6. ↑ Vandorpe DH, Morris CE (1992). "Stretch activation of the Aplysia S-channel". The Journal of membrane biology. 127 (3): 205–214. PMID 1495087.
  7. ↑ 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.

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