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Protein

Potassium channel subfamily K member 4

Gene

Kcnk4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity2 Publications

Enzyme regulationi

Activated by arachidonic acid.2 Publications

GO - Molecular functioni

  • mechanically-gated potassium channel activity Source: UniProtKB
  • potassium channel activity Source: UniProtKB
  • temperature-gated cation channel activity Source: UniProtKB

GO - Biological processi

  • cellular response to alkaline pH Source: UniProtKB
  • cellular response to fatty acid Source: UniProtKB
  • cellular response to mechanical stimulus Source: Ensembl
  • cellular response to temperature stimulus Source: UniProtKB
  • detection of mechanical stimulus involved in sensory perception of touch Source: UniProtKB
  • memory Source: RGD
  • potassium ion transmembrane transport Source: UniProtKB
  • sensory perception of pain Source: UniProtKB
  • sensory perception of temperature stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiR-RNO-1299503. TWIK related potassium channel (TREK).

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel subfamily K member 4
Alternative name(s):
TWIK-related arachidonic acid-stimulated potassium channel protein
Short name:
TRAAK
Gene namesi
Name:Kcnk4Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621449. Kcnk4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33CytoplasmicBy similarity
Transmembranei4 – 2421HelicalBy similarityAdd
BLAST
Topological domaini25 – 8864ExtracellularBy similarityAdd
BLAST
Intramembranei89 – 10315Helical; Name=Pore helix 1By similarityAdd
BLAST
Intramembranei104 – 1107By similarity
Topological domaini111 – 1188ExtracellularBy similarity
Transmembranei119 – 15133HelicalBy similarityAdd
BLAST
Topological domaini152 – 17322CytoplasmicBy similarityAdd
BLAST
Transmembranei174 – 19522HelicalBy similarityAdd
BLAST
Topological domaini196 – 2005ExtracellularBy similarity
Intramembranei201 – 21414Helical; Name=Pore helix 2By similarityAdd
BLAST
Intramembranei215 – 2206By similarity
Topological domaini221 – 23414ExtracellularBy similarityAdd
BLAST
Transmembranei235 – 26127HelicalBy similarityAdd
BLAST
Topological domaini262 – 397136CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Potassium channel subfamily K member 4PRO_0000432591Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 – 52InterchainBy similarity
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiG3V8V5.

Expressioni

Tissue specificityi

Detected in brain, and at much lower levels in liver, skeletal muscle and testis.1 Publication

Gene expression databases

GenevisibleiG3V8V5. RN.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028704.

Structurei

3D structure databases

ProteinModelPortaliG3V8V5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 1096Selectivity filter 1By similarity
Regioni213 – 2186Selectivity filter 2By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi293 – 33644Pro-richPROSITE-ProRule annotationAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the two pore domain potassium channel (TC 1.A.1.8) family. [View classification]UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1418. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118858.
HOVERGENiHBG052234.
KOiK04915.
OMAiLDYPSEN.
OrthoDBiEOG77M8NK.
PhylomeDBiG3V8V5.
TreeFamiTF313947.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR008074. 2pore_dom_K_chnl_TRAAK.
IPR013099. K_chnl_dom.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PRINTSiPR01333. 2POREKCHANEL.
PR01691. TRAAKCHANNEL.

Sequencei

Sequence statusi: Complete.

G3V8V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSTTLLALL ALVLLYLVSG ALVFQALEQP HEQQVQKDLE DGRDQFLKDH
60 70 80 90 100
PCVSQKNLEG FIKLVAEALG GGANPETSWT NSSNHSSAWN LGSAFFFSGT
110 120 130 140 150
IITTIGYGNI ALHTDAGRLF CIFYALVGIP LFGMLLAGVG DRLGSSLRRG
160 170 180 190 200
IGHIEAVFLK WHVPPGLVRM LSAVLFLLIG CLLFVLTPTF VFSYMESWSK
210 220 230 240 250
LEAIYFVIVT LTTVGFGDYV PGDGTGQNSP AYQPLVWFWI LFGLAYFASV
260 270 280 290 300
LTTIGNWLRA VSRRTRAEMG GLTAQAASWT GTVTARVTQR TGPSAPPPEK
310 320 330 340 350
EQPLLPSSLP APPAVAEPAH RPGSPAPAEK VETPPPTASA LDYPSENLAF
360 370 380 390
IDESSDTQSE RGCALPRAPR GRRRPNPTKK PSRPRGPGRL RDKAVPV
Length:397
Mass (Da):42,920
Last modified:November 16, 2011 - v1
Checksum:i5369F0841EE72831
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251Q → Y in AAK60504 (PubMed:11374070).Curated
Sequence conflicti196 – 1961E → K in AAK60504 (PubMed:11374070).Curated
Sequence conflicti202 – 2021E → K in AAK60504 (PubMed:11374070).Curated
Sequence conflicti251 – 2511L → F in AAK60504 (PubMed:11374070).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302842 mRNA. Translation: AAK60504.2.
AABR06009566 Genomic DNA. No translation available.
CH473953 Genomic DNA. Translation: EDM12628.1.
RefSeqiNP_446256.2. NM_053804.2.
XP_008758276.1. XM_008760054.1.
XP_008758277.1. XM_008760055.1.
XP_008758278.1. XM_008760056.1.
UniGeneiRn.46453.

Genome annotation databases

EnsembliENSRNOT00000028704; ENSRNOP00000028704; ENSRNOG00000021140.
GeneIDi116489.
KEGGirno:116489.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302842 mRNA. Translation: AAK60504.2.
AABR06009566 Genomic DNA. No translation available.
CH473953 Genomic DNA. Translation: EDM12628.1.
RefSeqiNP_446256.2. NM_053804.2.
XP_008758276.1. XM_008760054.1.
XP_008758277.1. XM_008760055.1.
XP_008758278.1. XM_008760056.1.
UniGeneiRn.46453.

3D structure databases

ProteinModelPortaliG3V8V5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028704.

Proteomic databases

PaxDbiG3V8V5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028704; ENSRNOP00000028704; ENSRNOG00000021140.
GeneIDi116489.
KEGGirno:116489.

Organism-specific databases

CTDi50801.
RGDi621449. Kcnk4.

Phylogenomic databases

eggNOGiKOG1418. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118858.
HOVERGENiHBG052234.
KOiK04915.
OMAiLDYPSEN.
OrthoDBiEOG77M8NK.
PhylomeDBiG3V8V5.
TreeFamiTF313947.

Enzyme and pathway databases

ReactomeiR-RNO-1299503. TWIK related potassium channel (TREK).

Miscellaneous databases

PROiG3V8V5.

Gene expression databases

GenevisibleiG3V8V5. RN.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR008074. 2pore_dom_K_chnl_TRAAK.
IPR013099. K_chnl_dom.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PRINTSiPR01333. 2POREKCHANEL.
PR01691. TRAAKCHANNEL.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Synergistic interaction and the role of C-terminus in the activation of TRAAK K+ channels by pressure, free fatty acids and alkali."
    Kim Y., Bang H., Gnatenco C., Kim D.
    Pflugers Arch. 442:64-72(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Sprague-DawleyImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    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.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. "Thermosensitivity of the two-pore domain K+ channels TREK-2 and TRAAK."
    Kang D., Choe C., Kim D.
    J. Physiol. (Lond.) 564:103-116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiKCNK4_RAT
AccessioniPrimary (citable) accession number: G3V8V5
Secondary accession number(s): Q924I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 2015
Last sequence update: November 16, 2011
Last modified: June 8, 2016
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.