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Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK)

 KCNK4_RAT               Reviewed;         397 AA.
G3V8V5; Q924I4;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
16-NOV-2011, sequence version 1.
23-MAY-2018, entry version 50.
RecName: Full=Potassium channel subfamily K member 4;
AltName: Full=TWIK-related arachidonic acid-stimulated potassium channel protein;
Short=TRAAK;
Name=Kcnk4 {ECO:0000312|RGD:621449};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
[1] {ECO:0000312|EMBL:AAK60504.2}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAK60504.2};
PubMed=11374070; DOI=10.1007/s004240000496;
Kim Y., Bang H., Gnatenco C., Kim D.;
"Synergistic interaction and the role of C-terminus in the activation
of TRAAK K+ channels by pressure, free fatty acids and alkali.";
Pflugers Arch. 442:64-72(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=15677687; DOI=10.1113/jphysiol.2004.081059;
Kang D., Choe C., Kim D.;
"Thermosensitivity of the two-pore domain K+ channels TREK-2 and
TRAAK.";
J. Physiol. (Lond.) 564:103-116(2005).
-!- FUNCTION: Voltage-insensitive potassium channel (PubMed:11374070,
PubMed:15677687). Channel opening is triggered by mechanical
forces that deform the membrane, and by raising the intracellular
pH to basic levels (PubMed:11374070, PubMed:15677687). The channel
is inactive at 24 degrees Celsius (in vitro); raising the
temperature to 37 degrees Celsius increases the frequency of
channel opening, with a further increase in channel activity when
the temperature is raised to 42 degrees Celsius (PubMed:15677687).
Plays a role in the perception of pain caused by heat (By
similarity). Plays a role in the sensory perception of pain caused
by pressure (By similarity). {ECO:0000250|UniProtKB:O88454,
ECO:0000269|PubMed:11374070, ECO:0000269|PubMed:15677687}.
-!- ENZYME REGULATION: Activated by arachidonic acid.
{ECO:0000269|PubMed:11374070, ECO:0000269|PubMed:15677687}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000250|UniProtKB:Q9NYG8}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11374070};
Multi-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in brain, and at much lower levels in
liver, skeletal muscle and testis. {ECO:0000269|PubMed:11374070}.
-!- DOMAIN: Channel opening is brought about by a conformation change
that involves buckling of the second transmembrane helix and
affects the position and orientation of the fourth transmembrane
helix. {ECO:0000250|UniProtKB:Q9NYG8}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000255|RuleBase:RU003857}.
-----------------------------------------------------------------------
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EMBL; AF302842; AAK60504.2; -; mRNA.
EMBL; AABR06009566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473953; EDM12628.1; -; Genomic_DNA.
RefSeq; NP_446256.2; NM_053804.2.
RefSeq; XP_008758276.1; XM_008760054.2.
RefSeq; XP_008758277.1; XM_008760055.2.
RefSeq; XP_008758278.1; XM_008760056.2.
UniGene; Rn.46453; -.
ProteinModelPortal; G3V8V5; -.
SMR; G3V8V5; -.
STRING; 10116.ENSRNOP00000028704; -.
PaxDb; G3V8V5; -.
Ensembl; ENSRNOT00000028704; ENSRNOP00000028704; ENSRNOG00000021140.
GeneID; 116489; -.
KEGG; rno:116489; -.
CTD; 50801; -.
RGD; 621449; Kcnk4.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOVERGEN; HBG052234; -.
KO; K04915; -.
OMA; LDYPSEN; -.
OrthoDB; EOG091G0E3R; -.
PhylomeDB; G3V8V5; -.
TreeFam; TF313947; -.
Reactome; R-RNO-1299503; TWIK related potassium channel (TREK).
Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
PRO; PR:G3V8V5; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000021140; -.
Genevisible; G3V8V5; RN.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0034705; C:potassium channel complex; IEA:Ensembl.
GO; GO:0098782; F:mechanosensitived potassium channel activity; IDA:UniProtKB.
GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
GO; GO:0097604; F:temperature-gated cation channel activity; IDA:UniProtKB.
GO; GO:0071469; P:cellular response to alkaline pH; IDA:UniProtKB.
GO; GO:0071398; P:cellular response to fatty acid; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071502; P:cellular response to temperature stimulus; IDA:UniProtKB.
GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; ISS:UniProtKB.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
GO; GO:0050951; P:sensory perception of temperature stimulus; ISS:UniProtKB.
GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
InterPro; IPR003280; 2pore_dom_K_chnl.
InterPro; IPR008074; 2pore_dom_K_chnl_TRAAK.
InterPro; IPR013099; K_chnl_dom.
Pfam; PF07885; Ion_trans_2; 2.
PRINTS; PR01333; 2POREKCHANEL.
PRINTS; PR01691; TRAAKCHANNEL.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 397 Potassium channel subfamily K member 4.
/FTId=PRO_0000432591.
TOPO_DOM 1 3 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9NYG8}.
TRANSMEM 4 24 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.
TOPO_DOM 25 88 Extracellular.
{ECO:0000250|UniProtKB:Q9NYG8}.
INTRAMEM 89 103 Helical; Name=Pore helix 1.
{ECO:0000250|UniProtKB:Q9NYG8}.
INTRAMEM 104 110 {ECO:0000250|UniProtKB:Q9NYG8}.
TOPO_DOM 111 118 Extracellular.
{ECO:0000250|UniProtKB:Q9NYG8}.
TRANSMEM 119 151 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.
TOPO_DOM 152 173 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9NYG8}.
TRANSMEM 174 195 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.
TOPO_DOM 196 200 Extracellular.
{ECO:0000250|UniProtKB:Q9NYG8}.
INTRAMEM 201 214 Helical; Name=Pore helix 2.
{ECO:0000250|UniProtKB:Q9NYG8}.
INTRAMEM 215 220 {ECO:0000250|UniProtKB:Q9NYG8}.
TOPO_DOM 221 234 Extracellular.
{ECO:0000250|UniProtKB:Q9NYG8}.
TRANSMEM 235 261 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.
TOPO_DOM 262 397 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9NYG8}.
REGION 104 109 Selectivity filter 1.
{ECO:0000250|UniProtKB:Q9NYG8}.
REGION 213 218 Selectivity filter 2.
{ECO:0000250|UniProtKB:Q9NYG8}.
COMPBIAS 293 336 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 52 Interchain.
{ECO:0000250|UniProtKB:Q9NYG8}.
CONFLICT 25 25 Q -> Y (in Ref. 1; AAK60504).
{ECO:0000305}.
CONFLICT 196 196 E -> K (in Ref. 1; AAK60504).
{ECO:0000305}.
CONFLICT 202 202 E -> K (in Ref. 1; AAK60504).
{ECO:0000305}.
CONFLICT 251 251 L -> F (in Ref. 1; AAK60504).
{ECO:0000305}.
SEQUENCE 397 AA; 42920 MW; 5369F0841EE72831 CRC64;
MRSTTLLALL ALVLLYLVSG ALVFQALEQP HEQQVQKDLE DGRDQFLKDH PCVSQKNLEG
FIKLVAEALG GGANPETSWT NSSNHSSAWN LGSAFFFSGT IITTIGYGNI ALHTDAGRLF
CIFYALVGIP LFGMLLAGVG DRLGSSLRRG IGHIEAVFLK WHVPPGLVRM LSAVLFLLIG
CLLFVLTPTF VFSYMESWSK LEAIYFVIVT LTTVGFGDYV PGDGTGQNSP AYQPLVWFWI
LFGLAYFASV LTTIGNWLRA VSRRTRAEMG GLTAQAASWT GTVTARVTQR TGPSAPPPEK
EQPLLPSSLP APPAVAEPAH RPGSPAPAEK VETPPPTASA LDYPSENLAF IDESSDTQSE
RGCALPRAPR GRRRPNPTKK PSRPRGPGRL RDKAVPV


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