KCNK2_HUMAN
ID KCNK2_HUMAN Reviewed; 426 AA.
AC O95069; A1Z1V3; A8K618; B2RCS4; B7ZL56; D3DTA5; Q5DP47; Q5DP48; Q9NRT2;
AC Q9UNE3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Potassium channel subfamily K member 2;
DE AltName: Full=Outward rectifying potassium channel protein TREK-1;
DE AltName: Full=TREK-1 K(+) channel subunit;
DE AltName: Full=Two pore domain potassium channel TREK-1;
DE AltName: Full=Two pore potassium channel TPKC1;
GN Name=KCNK2; Synonyms=TREK, TREK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ACTIVATION.
RX PubMed=10321245; DOI=10.1038/8084;
RA Patel A.J., Honore E., Lesage F., Fink M., Romey G., Lazdunski M.;
RT "Inhalational anesthetics activate two-pore-domain background K+
RT channels.";
RL Nat. Neurosci. 2:422-426(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10784345; DOI=10.1007/s004249900235;
RA Meadows H.J., Benham C.D., Cairns W., Gloger I., Jennings C.,
RA Medhurst A.D., Murdock P., Chapman C.G.;
RT "Cloning, localisation and functional expression of the human orthologue of
RT the TREK-1 potassium channel.";
RL Pflugers Arch. 439:714-722(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Price L.A., Hellings S.E., Hayashi J.H., Pausch M.H.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=24196565; DOI=10.1007/s00424-013-1384-z;
RA Rinne S., Renigunta V., Schlichthorl G., Zuzarte M., Bittner S.,
RA Meuth S.G., Decher N., Daut J., Preisig-Muller R.;
RT "A splice variant of the two-pore domain potassium channel TREK-1 with only
RT one pore domain reduces the surface expression of full-length TREK-1
RT channels.";
RL Pflugers Arch. 466:1559-1570(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Heart;
RA Thomas D., Sullivan A.N., Goldstein S.A.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION, PHOSPHORYLATION AT SER-348, AND MUTAGENESIS OF SER-348.
RX PubMed=11319556; DOI=10.1038/87434;
RA Bockenhauer D., Zilberberg N., Goldstein S.A.;
RT "KCNK2: reversible conversion of a hippocampal potassium leak into a
RT voltage-dependent channel.";
RL Nat. Neurosci. 4:486-491(2001).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23169818; DOI=10.1126/scisignal.2003431;
RA Plant L.D., Zuniga L., Araki D., Marks J.D., Goldstein S.A.;
RT "SUMOylation silences heterodimeric TASK potassium channels containing K2P1
RT subunits in cerebellar granule neurons.";
RL Sci. Signal. 5:RA84-RA84(2012).
RN [12]
RP INTERACTION WITH BVES.
RX PubMed=26642364; DOI=10.1172/jci79562;
RA Schindler R.F., Scotton C., Zhang J., Passarelli C., Ortiz-Bonnin B.,
RA Simrick S., Schwerte T., Poon K.L., Fang M., Rinne S., Froese A.,
RA Nikolaev V.O., Grunert C., Mueller T., Tasca G., Sarathchandra P.,
RA Drago F., Dallapiccola B., Rapezzi C., Arbustini E., Di Raimo F.R.,
RA Neri M., Selvatici R., Gualandi F., Fattori F., Pietrangelo A., Li W.,
RA Jiang H., Xu X., Bertini E., Decher N., Wang J., Brand T., Ferlini A.;
RT "POPDC1S201F causes muscular dystrophy and arrhythmia by affecting protein
RT trafficking.";
RL J. Clin. Invest. 126:239-253(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 41-315 IN COMPLEX WITH POTASSIUM
RP IONS, DISULFIDE BOND, GLYCOSYLATION AT ASN-110, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human two pore domain potassium ion channel TREK1
RT (K2P2.1).";
RL Submitted (JUN-2014) to the PDB data bank.
CC -!- FUNCTION: Ion channel that contributes to passive transmembrane
CC potassium transport (PubMed:23169818). Reversibly converts between a
CC voltage-insensitive potassium leak channel and a voltage-dependent
CC outward rectifying potassium channel in a phosphorylation-dependent
CC manner (PubMed:11319556). In astrocytes, forms mostly heterodimeric
CC potassium channels with KCNK1, with only a minor proportion of
CC functional channels containing homodimeric KCNK2. In astrocytes, the
CC heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate
CC release in response to activation of G-protein coupled receptors, such
CC as F2R and CNR1 (By similarity). {ECO:0000250|UniProtKB:P97438,
CC ECO:0000269|PubMed:10784345, ECO:0000269|PubMed:11319556,
CC ECO:0000269|PubMed:23169818}.
CC -!- FUNCTION: [Isoform 4]: Does not display channel activity but reduces
CC the channel activity of isoform 1 and isoform 2 and reduces cell
CC surface expression of isoform 2. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Ref.13). Heterodimer with KCNK1;
CC disulfide-linked (By similarity). Interacts with BVES; the interaction
CC enhances KCNK2 surface expression and is inhibited by cAMP
CC (PubMed:26642364). {ECO:0000250|UniProtKB:P97438,
CC ECO:0000269|PubMed:26642364, ECO:0000269|Ref.13}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:10784345}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=TREK-1b;
CC IsoId=O95069-1; Sequence=Displayed;
CC Name=2; Synonyms=TREK-1a;
CC IsoId=O95069-2; Sequence=VSP_024429;
CC Name=3; Synonyms=TREK-1c;
CC IsoId=O95069-3; Sequence=VSP_024428;
CC Name=4; Synonyms=TREK-1e;
CC IsoId=O95069-4; Sequence=VSP_024428, VSP_047567, VSP_047568;
CC -!- TISSUE SPECIFICITY: Isoform 4 is detected in kidney, adrenal gland and
CC brain where it is preferentially expressed in the amygdala but not
CC found in thalamus, hypothalamus, hippocampus or substantia nigra.
CC {ECO:0000269|PubMed:24196565}.
CC -!- DOMAIN: The C-terminal region of isoform 4 mediates its intracellular
CC retention. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-348 controls the reversible conversion from
CC a leak channel to a voltage-dependent channel.
CC {ECO:0000269|PubMed:11319556}.
CC -!- MISCELLANEOUS: Activated by volatile general anesthetics such as
CC chloroform, halothane and isoflurane.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
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DR EMBL; AF129399; AAD47569.1; -; mRNA.
DR EMBL; AF171068; AAF89743.1; -; mRNA.
DR EMBL; AF004711; AAD01203.1; -; mRNA.
DR EMBL; AY552980; AAT49015.2; -; mRNA.
DR EMBL; AY552981; AAT49016.1; -; mRNA.
DR EMBL; EF165334; ABM47413.1; -; mRNA.
DR EMBL; EF165335; ABM47414.1; -; mRNA.
DR EMBL; AK291483; BAF84172.1; -; mRNA.
DR EMBL; AK315249; BAG37671.1; -; mRNA.
DR EMBL; AC092804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93347.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93349.1; -; Genomic_DNA.
DR EMBL; BC069462; AAH69462.1; -; mRNA.
DR EMBL; BC101693; AAI01694.1; -; mRNA.
DR EMBL; BC101695; AAI01696.1; -; mRNA.
DR EMBL; BC143586; AAI43587.1; -; mRNA.
DR CCDS; CCDS31024.1; -. [O95069-2]
DR CCDS; CCDS41466.1; -. [O95069-3]
DR CCDS; CCDS41467.1; -. [O95069-1]
DR RefSeq; NP_001017424.1; NM_001017424.2. [O95069-3]
DR RefSeq; NP_001017425.2; NM_001017425.2. [O95069-1]
DR RefSeq; NP_055032.1; NM_014217.3. [O95069-2]
DR RefSeq; XP_016856737.1; XM_017001248.1. [O95069-3]
DR PDB; 4TWK; X-ray; 2.60 A; A/B=41-315.
DR PDBsum; 4TWK; -.
DR AlphaFoldDB; O95069; -.
DR SMR; O95069; -.
DR BioGRID; 109977; 1.
DR STRING; 9606.ENSP00000394033; -.
DR BindingDB; O95069; -.
DR ChEMBL; CHEMBL2321615; -.
DR DrugBank; DB00204; Dofetilide.
DR DrugBank; DB04855; Dronedarone.
DR DrugCentral; O95069; -.
DR GuidetoPHARMACOLOGY; 514; -.
DR GlyGen; O95069; 2 sites.
DR iPTMnet; O95069; -.
DR PhosphoSitePlus; O95069; -.
DR BioMuta; KCNK2; -.
DR jPOST; O95069; -.
DR MassIVE; O95069; -.
DR PaxDb; O95069; -.
DR PeptideAtlas; O95069; -.
DR PRIDE; O95069; -.
DR Antibodypedia; 34619; 126 antibodies from 20 providers.
DR DNASU; 3776; -.
DR Ensembl; ENST00000391894.6; ENSP00000375764.2; ENSG00000082482.14. [O95069-2]
DR Ensembl; ENST00000391895.6; ENSP00000375765.2; ENSG00000082482.14. [O95069-3]
DR Ensembl; ENST00000444842.7; ENSP00000394033.2; ENSG00000082482.14. [O95069-1]
DR Ensembl; ENST00000467031.5; ENSP00000420203.1; ENSG00000082482.14. [O95069-4]
DR GeneID; 3776; -.
DR KEGG; hsa:3776; -.
DR MANE-Select; ENST00000444842.7; ENSP00000394033.2; NM_001017425.3; NP_001017425.2.
DR UCSC; uc001hkq.4; human. [O95069-1]
DR CTD; 3776; -.
DR DisGeNET; 3776; -.
DR GeneCards; KCNK2; -.
DR HGNC; HGNC:6277; KCNK2.
DR HPA; ENSG00000082482; Tissue enriched (adrenal).
DR MIM; 603219; gene.
DR neXtProt; NX_O95069; -.
DR OpenTargets; ENSG00000082482; -.
DR PharmGKB; PA30059; -.
DR VEuPathDB; HostDB:ENSG00000082482; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000156560; -.
DR HOGENOM; CLU_022504_10_0_1; -.
DR InParanoid; O95069; -.
DR OMA; TSQISHW; -.
DR PhylomeDB; O95069; -.
DR TreeFam; TF313947; -.
DR PathwayCommons; O95069; -.
DR Reactome; R-HSA-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
DR SignaLink; O95069; -.
DR BioGRID-ORCS; 3776; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; KCNK2; human.
DR GeneWiki; KCNK2; -.
DR GenomeRNAi; 3776; -.
DR Pharos; O95069; Tclin.
DR PRO; PR:O95069; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95069; protein.
DR Bgee; ENSG00000082482; Expressed in stromal cell of endometrium and 103 other tissues.
DR ExpressionAtlas; O95069; baseline and differential.
DR Genevisible; O95069; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0097449; C:astrocyte projection; IEA:Ensembl.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
DR GO; GO:0003231; P:cardiac ventricle development; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003976; 2pore_dom_K_chnl_TREK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01499; TREKCHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Potassium channel subfamily K member 2"
FT /id="PRO_0000101742"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 144..170
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 253..283
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 354..426
FT /note="Required for basal channel activity"
FT /evidence="ECO:0000250"
FT REGION 378..426
FT /note="Essential for chloroform and halothane sensitivity"
FT /evidence="ECO:0000250"
FT MOD_RES 348
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:11319556"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0007744|PDB:4TWK"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108
FT /note="Interchain"
FT /evidence="ECO:0007744|PDB:4TWK"
FT VAR_SEQ 1..16
FT /note="MLPSASRERPGYRAGV -> MMNPRAKRDFYL (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_024428"
FT VAR_SEQ 2..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10321245,
FT ECO:0000303|PubMed:10784345, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024429"
FT VAR_SEQ 213..232
FT /note="KWNVSQTKIRIISTIIFILF -> VDPILNIWTSISLSCGSGSL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_047567"
FT VAR_SEQ 233..426
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_047568"
FT MUTAGEN 348
FT /note="S->A: Mimics non-phosphorylated state and has no
FT effect on leak channel activity."
FT /evidence="ECO:0000269|PubMed:11319556"
FT MUTAGEN 348
FT /note="S->D: Phosphomimetic mutant which causes switch to
FT voltage-dependent outward rectifier channel activity."
FT /evidence="ECO:0000269|PubMed:11319556"
FT CONFLICT 309..311
FT /note="DWL -> RLV (in Ref. 3; AAD01203)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="S -> N (in Ref. 1; AAD47569)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="T -> A (in Ref. 3; AAD01203)"
FT /evidence="ECO:0000305"
FT HELIX 54..105
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:4TWK"
FT TURN 133..137
FT /evidence="ECO:0007829|PDB:4TWK"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 168..213
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 218..237
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:4TWK"
FT HELIX 287..315
FT /evidence="ECO:0007829|PDB:4TWK"
SQ SEQUENCE 426 AA; 47093 MW; DB10382B1803DA13 CRC64;
MLPSASRERP GYRAGVAAPD LLDPKSAAQN SKPRLSFSTK PTVLASRVES DTTINVMKWK
TVSTIFLVVV LYLIIGATVF KALEQPHEIS QRTTIVIQKQ TFISQHSCVN STELDELIQQ
IVAAINAGII PLGNTSNQIS HWDLGSSFFF AGTVITTIGF GNISPRTEGG KIFCIIYALL
GIPLFGFLLA GVGDQLGTIF GKGIAKVEDT FIKWNVSQTK IRIISTIIFI LFGCVLFVAL
PAIIFKHIEG WSALDAIYFV VITLTTIGFG DYVAGGSDIE YLDFYKPVVW FWILVGLAYF
AAVLSMIGDW LRVISKKTKE EVGEFRAHAA EWTANVTAEF KETRRRLSVE IYDKFQRATS
IKRKLSAELA GNHNQELTPC RRTLSVNHLT SERDVLPPLL KTESIYLNGL TPHCAGEEIA
VIENIK
