KCNK4_RAT
ID KCNK4_RAT Reviewed; 397 AA.
AC G3V8V5; Q924I4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Potassium channel subfamily K member 4;
DE AltName: Full=TWIK-related arachidonic acid-stimulated potassium channel protein;
DE Short=TRAAK;
GN Name=Kcnk4 {ECO:0000312|RGD:621449};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:AAK60504.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAK60504.2};
RX PubMed=11374070; DOI=10.1007/s004240000496;
RA Kim Y., Bang H., Gnatenco C., Kim D.;
RT "Synergistic interaction and the role of C-terminus in the activation of
RT TRAAK K+ channels by pressure, free fatty acids and alkali.";
RL Pflugers Arch. 442:64-72(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15677687; DOI=10.1113/jphysiol.2004.081059;
RA Kang D., Choe C., Kim D.;
RT "Thermosensitivity of the two-pore domain K+ channels TREK-2 and TRAAK.";
RL J. Physiol. (Lond.) 564:103-116(2005).
CC -!- FUNCTION: Voltage-insensitive potassium channel (PubMed:11374070,
CC PubMed:15677687). Channel opening is triggered by mechanical forces
CC that deform the membrane, and by raising the intracellular pH to basic
CC levels (PubMed:11374070, PubMed:15677687). The channel is inactive at
CC 24 degrees Celsius (in vitro); raising the temperature to 37 degrees
CC Celsius increases the frequency of channel opening, with a further
CC increase in channel activity when the temperature is raised to 42
CC degrees Celsius (PubMed:15677687). Plays a role in the perception of
CC pain caused by heat (By similarity). Plays a role in the sensory
CC perception of pain caused by pressure (By similarity).
CC {ECO:0000250|UniProtKB:O88454, ECO:0000269|PubMed:11374070,
CC ECO:0000269|PubMed:15677687}.
CC -!- ACTIVITY REGULATION: Activated by arachidonic acid.
CC {ECO:0000269|PubMed:11374070, ECO:0000269|PubMed:15677687}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q9NYG8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11374070};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain, and at much lower levels in
CC liver, skeletal muscle and testis. {ECO:0000269|PubMed:11374070}.
CC -!- DOMAIN: Channel opening is brought about by a conformation change that
CC involves buckling of the second transmembrane helix and affects the
CC position and orientation of the fourth transmembrane helix.
CC {ECO:0000250|UniProtKB:Q9NYG8}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000255|RuleBase:RU003857}.
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DR EMBL; AF302842; AAK60504.2; -; mRNA.
DR EMBL; AABR06009566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473953; EDM12628.1; -; Genomic_DNA.
DR RefSeq; NP_446256.2; NM_053804.2.
DR RefSeq; XP_008758276.1; XM_008760054.2.
DR RefSeq; XP_008758277.1; XM_008760055.2.
DR RefSeq; XP_008758278.1; XM_008760056.2.
DR AlphaFoldDB; G3V8V5; -.
DR SMR; G3V8V5; -.
DR STRING; 10116.ENSRNOP00000028704; -.
DR GlyGen; G3V8V5; 1 site.
DR PaxDb; G3V8V5; -.
DR ABCD; G3V8V5; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000028704; ENSRNOP00000028704; ENSRNOG00000021140.
DR GeneID; 116489; -.
DR KEGG; rno:116489; -.
DR CTD; 50801; -.
DR RGD; 621449; Kcnk4.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000160310; -.
DR HOGENOM; CLU_022504_1_1_1; -.
DR InParanoid; G3V8V5; -.
DR OMA; ISNHSAW; -.
DR OrthoDB; 616474at2759; -.
DR PhylomeDB; G3V8V5; -.
DR TreeFam; TF313947; -.
DR Reactome; R-RNO-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:G3V8V5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000021140; Expressed in frontal cortex and 9 other tissues.
DR Genevisible; G3V8V5; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0034705; C:potassium channel complex; ISO:RGD.
DR GO; GO:0098782; F:mechanosensitived potassium channel activity; IDA:UniProtKB.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0097604; F:temperature-gated cation channel activity; IDA:UniProtKB.
DR GO; GO:0071469; P:cellular response to alkaline pH; IDA:UniProtKB.
DR GO; GO:0071398; P:cellular response to fatty acid; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IDA:UniProtKB.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0050951; P:sensory perception of temperature stimulus; ISS:UniProtKB.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR008074; 2pore_dom_K_chnl_TRAAK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01691; TRAAKCHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..397
FT /note="Potassium channel subfamily K member 4"
FT /id="PRO_0000432591"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TOPO_DOM 25..88
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT INTRAMEM 89..103
FT /note="Helical; Name=Pore helix 1"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT INTRAMEM 104..110
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TOPO_DOM 111..118
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TRANSMEM 119..151
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TOPO_DOM 152..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TOPO_DOM 196..200
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT INTRAMEM 201..214
FT /note="Helical; Name=Pore helix 2"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT INTRAMEM 215..220
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TOPO_DOM 221..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TRANSMEM 235..261
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT TOPO_DOM 262..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT REGION 104..109
FT /note="Selectivity filter 1"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT REGION 213..218
FT /note="Selectivity filter 2"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT REGION 282..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9NYG8"
FT CONFLICT 25
FT /note="Q -> Y (in Ref. 1; AAK60504)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="E -> K (in Ref. 1; AAK60504)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> K (in Ref. 1; AAK60504)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="L -> F (in Ref. 1; AAK60504)"
FT /evidence="ECO:0000305"
SQ 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
