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Potassium channel subfamily K member 2 (Outward rectifying potassium channel protein TREK-1) (TREK-1 K( ) channel subunit) (Two pore potassium channel TPKC1)

 KCNK2_MOUSE             Reviewed;         426 AA.
P97438; Q4VQI2;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 3.
25-OCT-2017, entry version 141.
RecName: Full=Potassium channel subfamily K member 2;
AltName: Full=Outward rectifying potassium channel protein TREK-1;
AltName: Full=TREK-1 K(+) channel subunit {ECO:0000303|PubMed:10321245, ECO:0000303|PubMed:24496152};
AltName: Full=Two pore potassium channel TPKC1;
Name=Kcnk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=9003761;
Fink M., Duprat F., Lesage F., Reyes R., Romey G., Heurteaux C.,
Lazdunski M.;
"Cloning, functional expression and brain localization of a novel
unconventional outward rectifier K+ channel.";
EMBO J. 15:6854-6862(1996).
[2]
SEQUENCE REVISION.
Fink M., Duprat F., Lesage F., Reyes R., Romey G., Heurteaux C.,
Lazdunski M.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
STRAIN=BALB/cJ;
PubMed=16636285; DOI=10.1073/pnas.0600463103;
Honore E., Patel A.J., Chemin J., Suchyna T., Sachs F.;
"Desensitization of mechano-gated K2P channels.";
Proc. Natl. Acad. Sci. U.S.A. 103:6859-6864(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=10321245; DOI=10.1038/8084;
Patel A.J., Honore E., Lesage F., Fink M., Romey G., Lazdunski M.;
"Inhalational anesthetics activate two-pore-domain background K+
channels.";
Nat. Neurosci. 2:422-426(1999).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH BVES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22354168; DOI=10.1172/JCI59410;
Froese A., Breher S.S., Waldeyer C., Schindler R.F., Nikolaev V.O.,
Rinne S., Wischmeyer E., Schlueter J., Becher J., Simrick S.,
Vauti F., Kuhtz J., Meister P., Kreissl S., Torlopp A., Liebig S.K.,
Laakmann S., Mueller T.D., Neumann J., Stieber J., Ludwig A.,
Maier S.K., Decher N., Arnold H.H., Kirchhof P., Fabritz L., Brand T.;
"Popeye domain containing proteins are essential for stress-mediated
modulation of cardiac pacemaking in mice.";
J. Clin. Invest. 122:1119-1130(2012).
[8]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH KCNK1,
TISSUE SPECIFICITY, DISULFIDE BOND, AND MUTAGENESIS OF CYS-108.
PubMed=24496152; DOI=10.1038/ncomms4227;
Hwang E.M., Kim E., Yarishkin O., Woo D.H., Han K.S., Park N., Bae Y.,
Woo J., Kim D., Park M., Lee C.J., Park J.Y.;
"A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive
conductance in astrocytes.";
Nat. Commun. 5:3227-3227(2014).
[9]
INTERACTION WITH BVES.
PubMed=26642364; DOI=10.1172/JCI79562;
Schindler R.F., Scotton C., Zhang J., Passarelli C., Ortiz-Bonnin B.,
Simrick S., Schwerte T., Poon K.L., Fang M., Rinne S., Froese A.,
Nikolaev V.O., Grunert C., Mueller T., Tasca G., Sarathchandra P.,
Drago F., Dallapiccola B., Rapezzi C., Arbustini E., Di Raimo F.R.,
Neri M., Selvatici R., Gualandi F., Fattori F., Pietrangelo A., Li W.,
Jiang H., Xu X., Bertini E., Decher N., Wang J., Brand T., Ferlini A.;
"POPDC1S201F causes muscular dystrophy and arrhythmia by affecting
protein trafficking.";
J. Clin. Invest. 126:239-253(2016).
-!- FUNCTION: Ion channel that contributes to passive transmembrane
potassium transport. Reversibly converts between a voltage-
insensitive potassium leak channel and a voltage-dependent outward
rectifying potassium channel in a phosphorylation-dependent
manner. In astrocytes, forms mostly heterodimeric potassium
channels with KCNK1, with only a minor proportion of functional
channels containing homodimeric KCNK2 (PubMed:24496152). In
astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required
for rapid glutamate release in response to activation of G-protein
coupled receptors, such as F2R and CNR1 (PubMed:24496152).
{ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285,
ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9003761}.
-!- ENZYME REGULATION: Inhibited by barium (PubMed:9003761). Activated
by volatile general anesthetics such as chloroform, diethyl ether,
halothane and isoflurane (PubMed:10321245).
{ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:9003761}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Channel activation is extremely rapid (PubMed:9003761).
Single channel conductance is about 14 pS (PubMed:9003761).
{ECO:0000269|PubMed:9003761};
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:24496152).
Heterodimer with KCNK1; disulfide-linked (PubMed:24496152).
Interacts with BVES; the interaction enhances KCNK2 surface
expression and is inhibited by cAMP (PubMed:22354168,
PubMed:26642364). {ECO:0000269|PubMed:22354168,
ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:26642364,
ECO:0000305}.
-!- INTERACTION:
D3YVF0:Akap5; NbExp=4; IntAct=EBI-7091062, EBI-7091108;
Q6PHU5:Sort1; NbExp=4; IntAct=EBI-7091062, EBI-6985663;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285,
ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24496152}; Multi-
pass membrane protein {ECO:0000305}. Note=Location at the cell
membrane requires interaction with KCNK1. Is not detected at the
cell membrane when KCNK1 is absent. {ECO:0000269|PubMed:24496152}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:9003761}; Multi-pass membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=TREK-1b;
IsoId=P97438-1; Sequence=Displayed;
Name=2; Synonyms=TREK-1a;
IsoId=P97438-2; Sequence=VSP_053951;
-!- TISSUE SPECIFICITY: Detected in hippocampus astrocytes (at protein
level) (PubMed:24496152). High expression in brain and lung. Also
detected in kidney, heart and skeletal muscle. Not detected in
liver. In the brain, highest expression in olfactory bulb,
hippocampus and cerebellum. {ECO:0000269|PubMed:22354168,
ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9003761}.
-!- PTM: Phosphorylation at Ser-348 controls the reversible conversion
from a leak channel to a voltage-dependent channel. {ECO:0000250}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U73488; AAC53005.2; -; mRNA.
EMBL; AY736359; AAV48996.1; -; mRNA.
EMBL; AC121882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS48480.1; -. [P97438-1]
CCDS; CCDS48481.1; -. [P97438-2]
RefSeq; NP_001153322.1; NM_001159850.1. [P97438-1]
RefSeq; NP_034737.2; NM_010607.3. [P97438-2]
UniGene; Mm.33304; -.
UniGene; Mm.387016; -.
PDB; 5VK5; X-ray; 3.10 A; A/B=35-337.
PDB; 5VKN; X-ray; 3.00 A; A/B=35-337.
PDB; 5VKP; X-ray; 2.80 A; A/B=35-337.
PDBsum; 5VK5; -.
PDBsum; 5VKN; -.
PDBsum; 5VKP; -.
ProteinModelPortal; P97438; -.
SMR; P97438; -.
DIP; DIP-58579N; -.
IntAct; P97438; 3.
STRING; 10090.ENSMUSP00000078416; -.
TCDB; 1.A.1.9.1; the voltage-gated ion channel (vic) superfamily.
iPTMnet; P97438; -.
PhosphoSitePlus; P97438; -.
PaxDb; P97438; -.
PRIDE; P97438; -.
Ensembl; ENSMUST00000110920; ENSMUSP00000106545; ENSMUSG00000037624. [P97438-2]
Ensembl; ENSMUST00000192723; ENSMUSP00000141849; ENSMUSG00000037624. [P97438-2]
Ensembl; ENSMUST00000193319; ENSMUSP00000141891; ENSMUSG00000037624. [P97438-1]
GeneID; 16526; -.
KEGG; mmu:16526; -.
UCSC; uc007eak.2; mouse. [P97438-1]
UCSC; uc011wyj.2; mouse. [P97438-2]
CTD; 3776; -.
MGI; MGI:109366; Kcnk2.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000013106; -.
HOVERGEN; HBG052234; -.
InParanoid; P97438; -.
KO; K04913; -.
OMA; AINVMKW; -.
OrthoDB; EOG091G0E3R; -.
PhylomeDB; P97438; -.
Reactome; R-MMU-1299503; TWIK related potassium channel (TREK).
PRO; PR:P97438; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000037624; -.
CleanEx; MM_KCNK2; -.
ExpressionAtlas; P97438; baseline and differential.
Genevisible; P97438; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0097449; C:astrocyte projection; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:MGI.
GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
GO; GO:0003231; P:cardiac ventricle development; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0090102; P:cochlea development; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IEA:Ensembl.
GO; GO:0006813; P:potassium ion transport; IDA:MGI.
GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0030322; P:stabilization of membrane potential; TAS:MGI.
InterPro; IPR003280; 2pore_dom_K_chnl.
InterPro; IPR003976; 2pore_dom_K_chnl_TREK.
InterPro; IPR013099; K_chnl_dom.
Pfam; PF07885; Ion_trans_2; 2.
PRINTS; PR01333; 2POREKCHANEL.
PRINTS; PR01499; TREKCHANNEL.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Potassium; Potassium channel; Potassium transport;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 426 Potassium channel subfamily K member 2.
/FTId=PRO_0000101743.
TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
INTRAMEM 144 170 Pore-forming; Name=Pore-forming 1.
{ECO:0000255}.
TRANSMEM 172 192 Helical. {ECO:0000255}.
TOPO_DOM 193 222 Cytoplasmic. {ECO:0000255}.
TRANSMEM 223 243 Helical. {ECO:0000255}.
INTRAMEM 253 283 Pore-forming; Name=Pore-forming 2.
{ECO:0000255}.
TRANSMEM 288 308 Helical. {ECO:0000255}.
TOPO_DOM 309 426 Cytoplasmic. {ECO:0000255}.
REGION 369 426 Required for basal channel activity.
REGION 393 426 Essential for chloroform and halothane
sensitivity.
MOD_RES 348 348 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 108 108 Interchain.
{ECO:0000269|PubMed:24496152}.
VAR_SEQ 2 16 Missing (in isoform 2).
{ECO:0000303|PubMed:9003761}.
/FTId=VSP_053951.
MUTAGEN 108 108 C->S: Abolishes formation of a disulfide-
linked heterodimer with KCNK1.
{ECO:0000269|PubMed:24496152}.
CONFLICT 78 78 T -> A (in Ref. 2; AAC53005).
{ECO:0000305}.
SEQUENCE 426 AA; 46844 MW; 8C298C01F5BDB61A CRC64;
MLASASRERP GYTAGVAAPD LLDPKSAAQN SKPRLSFSSK PTVLASRVES DSAINVMKWK
TVSTIFLVVV LYLIIGATVF KALEQPQEIS QRTTIVIQKQ TFIAQHACVN STELDELIQQ
IVAAINAGII PLGNSSNQVS HWDLGSSFFF AGTVITTIGF GNISPRTEGG KIFCIIYALL
GIPLFGFLLA GVGDQLGTIF GKGIAKVEDT FIKWNVSQTK IRIISTIIFI LFGCVLFVAL
PAVIFKHIEG WSALDAIYFV VITLTTIGFG DYVAGGSDIE YLDFYKPVVW FWILVGLAYF
AAVLSMIGDW LRVISKKTKE EVGEFRAHAA EWTANVTAEF KETRRRLSVE IYDKFQRATS
VKRKLSAELA GNHNQELTPC RRTLSVNHLT SEREVLPPLL KAESIYLNGL TPHCAGEDIA
VIENMK


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