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

 KCNK2_RAT               Reviewed;         426 AA.
Q920B6; A3QR52; Q3MMY3; Q5DNW4; Q5DNW5;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 110.
RecName: Full=Potassium channel subfamily K member 2 {ECO:0000250|UniProtKB:O95069};
AltName: Full=Outward rectifying potassium channel protein TREK-1 {ECO:0000250|UniProtKB:O95069};
AltName: Full=Stretch-activated potassium channel TREK-1 {ECO:0000303|PubMed:16248991};
AltName: Full=TREK-1 K(+) channel subunit {ECO:0000250|UniProtKB:O95069};
AltName: Full=Two pore domain potassium channel TREK-1 {ECO:0000303|PubMed:24196565};
AltName: Full=Two pore potassium channel TPKC1 {ECO:0000250|UniProtKB:O95069};
Name=Kcnk2 {ECO:0000312|EMBL:AAU06141.1,
ECO:0000312|Ensembl:ENSRNOP00000003684, ECO:0000312|RGD:621448};
Synonyms=Trek {ECO:0000312|EMBL:ABD64605.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL01159.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Brain {ECO:0000312|EMBL:AAL01159.1};
PubMed=11319556;
Bockenhauer D., Zilberberg N., Goldstein S.A.;
"KCNK2: reversible conversion of a hippocampal potassium leak into a
voltage-dependent channel.";
Nat. Neurosci. 4:486-491(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL95708.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=Wistar {ECO:0000312|EMBL:AAL95708.1};
PubMed=11897838; DOI=10.1113/jphysiol.2001.013432;
Gu W., Schlichthorl G., Hirsch J.R., Engels H., Karschin C.,
Karschin A., Derst C., Steinlein O.K., Daut J.;
"Expression pattern and functional characteristics of two novel splice
variants of the two-pore-domain potassium channel TREK-2.";
J. Physiol. (Lond.) 539:657-668(2002).
[3] {ECO:0000305, ECO:0000312|EMBL:AAU25945.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
ACTIVATION.
PubMed=16248991; DOI=10.1016/j.cardiores.2005.08.018;
Tao Li X., Dyachenko V., Zuzarte M., Putzke C., Preisig-Muller R.,
Isenberg G., Daut J.;
"The stretch-activated potassium channel TREK-1 in rat cardiac
ventricular muscle.";
Cardiovasc. Res. 69:86-97(2006).
[4] {ECO:0000305, ECO:0000312|EMBL:ABD64605.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
PubMed=24196565; DOI=10.1007/s00424-013-1384-z;
Rinne S., Renigunta V., Schlichthorl G., Zuzarte M., Bittner S.,
Meuth S.G., Decher N., Daut J., Preisig-Muller R.;
"A splice variant of the two-pore domain potassium channel TREK-1 with
only one pore domain reduces the surface expression of full-length
TREK-1 channels.";
Pflugers Arch. 466:1559-1570(2014).
[5] {ECO:0000305, ECO:0000312|EMBL:AAU06141.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Wistar {ECO:0000312|EMBL:AAU06141.1};
Li Z.B., Wang X.L.;
"Possible role of TREK-1 in temperature regulation.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000312|Ensembl:ENSRNOP00000003684}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000312|Ensembl:ENSRNOP00000003684};
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).
[7] {ECO:0000305, ECO:0000312|EMBL:AAU06141.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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
(PubMed:11319556). In astrocytes, forms mostly heterodimeric
potassium channels with KCNK1, with only a minor proportion of
functional channels containing homodimeric KCNK2. 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 (By similarity).
{ECO:0000250|UniProtKB:P97438, ECO:0000269|PubMed:11319556}.
-!- FUNCTION: Isoform 5: Does not display channel activity but reduces
the channel activity of isoform 1, isoform 2 and isoform 4 and
reduces cell surface expression of isoform 2.
{ECO:0000269|PubMed:24196565}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer
with KCNK1; disulfide-linked (By similarity). Interacts with BVES;
the interaction enhances KCNK2 surface expression and is inhibited
by cAMP (By similarity). {ECO:0000250|UniProtKB:O95069,
ECO:0000250|UniProtKB:P97438}.
-!- INTERACTION:
P50150:GNG4 (xeno); NbExp=3; IntAct=EBI-6530063, EBI-6395970;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:24196565}; Multi-pass membrane protein
{ECO:0000269|PubMed:24196565}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:24196565}; Multi-pass membrane protein
{ECO:0000269|PubMed:24196565}.
-!- SUBCELLULAR LOCATION: Isoform 5: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:24196565}; Multi-pass membrane protein
{ECO:0000269|PubMed:24196565}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:11319556, ECO:0000269|PubMed:11897838};
Synonyms=TREK-1b {ECO:0000303|PubMed:24196565};
IsoId=Q920B6-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:16248991}; Synonyms=TREK-1a
{ECO:0000303|PubMed:24196565};
IsoId=Q920B6-2; Sequence=VSP_053954;
Name=3 {ECO:0000269|PubMed:24196565}; Synonyms=TREK-1c
{ECO:0000303|PubMed:24196565};
IsoId=Q920B6-3; Sequence=VSP_053952;
Name=4 {ECO:0000269|PubMed:24196565}; Synonyms=TREK-1d
{ECO:0000303|PubMed:24196565};
IsoId=Q920B6-4; Sequence=VSP_053953;
Name=5 {ECO:0000269|PubMed:24196565}; Synonyms=TREK-1e
{ECO:0000303|PubMed:24196565};
IsoId=Q920B6-5; Sequence=VSP_053954, VSP_053955, VSP_053956;
-!- TISSUE SPECIFICITY: Expressed in cardiomyocytes (at protein
level). Expressed in various brain regions including the lateral
olfactory tract, piriform cortex of the forebrain, paraventricular
and anteromedial thalamic nuclei, brainstem, caudate putamen,
nucleus accumbens, neocortex and interpeduncular nucleus. Isoform
5 is expressed in brain and kidney. {ECO:0000269|PubMed:11897838,
ECO:0000269|PubMed:16248991, ECO:0000269|PubMed:24196565}.
-!- DOMAIN: The C-terminal region of isoform 5 mediates its
intracellular retention. {ECO:0000269|PubMed:24196565}.
-!- PTM: Phosphorylation at Ser-348 controls the reversible conversion
from a leak channel to a voltage-dependent channel.
{ECO:0000250|UniProtKB:O95069}.
-!- MISCELLANEOUS: Activated by arachadonic acid, mechanical
stretching and intracellular acidification.
{ECO:0000269|PubMed:16248991}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000255}.
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EMBL; AF325671; AAL01159.1; -; mRNA.
EMBL; AF385402; AAL95708.1; -; mRNA.
EMBL; AY727922; AAU25945.1; -; mRNA.
EMBL; AY555072; AAT64134.1; -; mRNA.
EMBL; AY555073; AAT64135.1; -; mRNA.
EMBL; DQ403851; ABD64605.1; -; mRNA.
EMBL; AY695826; AAU06141.1; -; mRNA.
EMBL; AABR06076806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06076807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06076808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06076809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473985; EDL94961.1; -; Genomic_DNA.
EMBL; CH473985; EDL94962.1; -; Genomic_DNA.
RefSeq; NP_742038.2; NM_172041.2.
RefSeq; NP_742039.1; NM_172042.1. [Q920B6-1]
RefSeq; XP_006250495.1; XM_006250433.3. [Q920B6-4]
RefSeq; XP_006250496.1; XM_006250434.3. [Q920B6-2]
UniGene; Rn.21984; -.
ProteinModelPortal; Q920B6; -.
SMR; Q920B6; -.
IntAct; Q920B6; 9.
STRING; 10116.ENSRNOP00000003684; -.
ChEMBL; CHEMBL3817718; -.
PaxDb; Q920B6; -.
PRIDE; Q920B6; -.
Ensembl; ENSRNOT00000003684; ENSRNOP00000003684; ENSRNOG00000002653. [Q920B6-1]
Ensembl; ENSRNOT00000077282; ENSRNOP00000068842; ENSRNOG00000002653. [Q920B6-3]
GeneID; 170899; -.
KEGG; rno:170899; -.
UCSC; RGD:621448; rat. [Q920B6-1]
CTD; 3776; -.
RGD; 621448; Kcnk2.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000013106; -.
HOVERGEN; HBG052234; -.
InParanoid; Q920B6; -.
KO; K04913; -.
OMA; AINVMKW; -.
OrthoDB; EOG091G0E3R; -.
PhylomeDB; Q920B6; -.
TreeFam; TF313947; -.
Reactome; R-RNO-1299503; TWIK related potassium channel (TREK).
PRO; PR:Q920B6; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000002653; -.
Genevisible; Q920B6; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0097449; C:astrocyte projection; IDA:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0044305; C:calyx of Held; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; IDA:UniProtKB.
GO; GO:0003231; P:cardiac ventricle development; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0090102; P:cochlea development; IEP:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:RGD.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IMP:RGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
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;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Ion channel;
Ion transport; Membrane; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 426 Potassium channel subfamily K member 2.
/FTId=PRO_0000426718.
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 354 426 Required for basal channel activity.
{ECO:0000250|UniProtKB:P97438}.
REGION 378 426 Essential for chloroform and halothane
sensitivity.
{ECO:0000250|UniProtKB:P97438}.
MOD_RES 348 348 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O95069}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 108 108 Interchain.
{ECO:0000250|UniProtKB:P97438}.
VAR_SEQ 1 16 MLASASRERPGYTAGV -> MMNPRAKRSVYL (in
isoform 3).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_053952.
VAR_SEQ 1 15 MLASASRERPGYTAG -> MGA (in isoform 4).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_053953.
VAR_SEQ 2 16 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:16248991,
ECO:0000303|PubMed:24196565}.
/FTId=VSP_053954.
VAR_SEQ 213 241 KWNVSQTKIRIISTIIFILFGCVLFVALP -> VGRTLNIW
TSTSSSCGSGSSLGWPTLRLF (in isoform 5).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_053955.
VAR_SEQ 242 426 Missing (in isoform 5).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_053956.
CONFLICT 416 416 A -> R (in Ref. 4; ABD64605).
{ECO:0000305}.
SEQUENCE 426 AA; 46912 MW; CACDA05BBE95FDBC CRC64;
MLASASRERP GYTAGVAAPD LLDPKSAAQN SKPRLSFSAK PTVLASRVES DSAINVMKWK
TVSTIFLVVV LYLIIGATVF KALEQPQEIS QRTTIVIQKQ NFIAQHACVN STELDELIQQ
IVTAINAGII PLGNNSNQVS 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 TPHCAAEDIA
VIENMK


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18-003-42631 Cyclic GMP gated potassium channel - Potassium voltage-gated channel. shaker-related subfamily. member 10 Polyclonal 0.1 mg Protein A
18-662-20074 Potassium voltage-gated channel subfamily C member 1 - Voltage-gated potassium channel subunit Kv3.1; Kv4; NGK2; RAW2 Polyclonal 0.1 ml


 

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