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

 KCNK2_HUMAN             Reviewed;         426 AA.
O95069; A1Z1V3; A8K618; B2RCS4; B7ZL56; D3DTA5; Q5DP47; Q5DP48;
Q9NRT2; Q9UNE3;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
05-JUL-2017, entry version 147.
RecName: Full=Potassium channel subfamily K member 2;
AltName: Full=Outward rectifying potassium channel protein TREK-1;
AltName: Full=TREK-1 K(+) channel subunit;
AltName: Full=Two pore domain potassium channel TREK-1;
AltName: Full=Two pore potassium channel TPKC1;
Name=KCNK2; Synonyms=TREK, TREK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ACTIVATION.
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10784345; DOI=10.1007/s004249900235;
Meadows H.J., Benham C.D., Cairns W., Gloger I., Jennings C.,
Medhurst A.D., Murdock P., Chapman C.G.;
"Cloning, localisation and functional expression of the human
orthologue of the TREK-1 potassium channel.";
Pflugers Arch. 439:714-722(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Price L.A., Hellings S.E., Hayashi J.H., Pausch M.H.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING,
AND TISSUE SPECIFICITY.
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Heart;
Thomas D., Sullivan A.N., Goldstein S.A.;
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION, PHOSPHORYLATION AT SER-348, AND MUTAGENESIS OF SER-348.
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).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23169818; DOI=10.1126/scisignal.2003431;
Plant L.D., Zuniga L., Araki D., Marks J.D., Goldstein S.A.;
"SUMOylation silences heterodimeric TASK potassium channels containing
K2P1 subunits in cerebellar granule neurons.";
Sci. Signal. 5:RA84-RA84(2012).
[12]
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).
[13]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 41-315 IN COMPLEX WITH
POTASSIUM IONS, DISULFIDE BOND, GLYCOSYLATION AT ASN-110, AND SUBUNIT.
Structural genomics consortium (SGC);
"Crystal structure of human two pore domain potassium ion channel
TREK1 (K2P2.1).";
Submitted (JUN-2014) to the PDB data bank.
-!- FUNCTION: Ion channel that contributes to passive transmembrane
potassium transport (PubMed:23169818). 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:10784345, ECO:0000269|PubMed:11319556,
ECO:0000269|PubMed:23169818}.
-!- FUNCTION: Isoform 4: Does not display channel activity but reduces
the channel activity of isoform 1 and isoform 2 and reduces cell
surface expression of isoform 2. {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked (Ref.13). Heterodimer with
KCNK1; disulfide-linked (By similarity). Interacts with BVES; the
interaction enhances KCNK2 surface expression and is inhibited by
cAMP (PubMed:26642364). {ECO:0000250|UniProtKB:P97438,
ECO:0000269|PubMed:26642364, ECO:0000269|Ref.13}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:23169818}; Multi-pass membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:10784345}; Multi-pass membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 4: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=TREK-1b;
IsoId=O95069-1; Sequence=Displayed;
Name=2; Synonyms=TREK-1a;
IsoId=O95069-2; Sequence=VSP_024429;
Name=3; Synonyms=TREK-1c;
IsoId=O95069-3; Sequence=VSP_024428;
Name=4; Synonyms=TREK-1e;
IsoId=O95069-4; Sequence=VSP_024428, VSP_047567, VSP_047568;
-!- TISSUE SPECIFICITY: Isoform 4 is detected in kidney, adrenal gland
and brain where it is preferentially expressed in the amygdala but
not found in thalamus, hypothalamus, hippocampus or substantia
nigra. {ECO:0000269|PubMed:24196565}.
-!- DOMAIN: The C-terminal region of isoform 4 mediates its
intracellular retention. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-348 controls the reversible conversion
from a leak channel to a voltage-dependent channel.
{ECO:0000269|PubMed:11319556}.
-!- MISCELLANEOUS: Activated by volatile general anesthetics such as
chloroform, halothane and isoflurane.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000305}.
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EMBL; AF129399; AAD47569.1; -; mRNA.
EMBL; AF171068; AAF89743.1; -; mRNA.
EMBL; AF004711; AAD01203.1; -; mRNA.
EMBL; AY552980; AAT49015.2; -; mRNA.
EMBL; AY552981; AAT49016.1; -; mRNA.
EMBL; EF165334; ABM47413.1; -; mRNA.
EMBL; EF165335; ABM47414.1; -; mRNA.
EMBL; AK291483; BAF84172.1; -; mRNA.
EMBL; AK315249; BAG37671.1; -; mRNA.
EMBL; AC092804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL583830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93347.1; -; Genomic_DNA.
EMBL; CH471100; EAW93349.1; -; Genomic_DNA.
EMBL; BC069462; AAH69462.1; -; mRNA.
EMBL; BC101693; AAI01694.1; -; mRNA.
EMBL; BC101695; AAI01696.1; -; mRNA.
EMBL; BC143586; AAI43587.1; -; mRNA.
CCDS; CCDS31024.1; -. [O95069-2]
CCDS; CCDS41466.1; -. [O95069-3]
CCDS; CCDS41467.1; -. [O95069-1]
RefSeq; NP_001017424.1; NM_001017424.2. [O95069-3]
RefSeq; NP_001017425.2; NM_001017425.2. [O95069-1]
RefSeq; NP_055032.1; NM_014217.3. [O95069-2]
RefSeq; XP_016856737.1; XM_017001248.1. [O95069-3]
UniGene; Hs.497745; -.
PDB; 4TWK; X-ray; 2.60 A; A/B=41-315.
PDBsum; 4TWK; -.
ProteinModelPortal; O95069; -.
SMR; O95069; -.
STRING; 9606.ENSP00000394033; -.
BindingDB; O95069; -.
ChEMBL; CHEMBL2321615; -.
DrugBank; DB00204; Dofetilide.
DrugBank; DB04855; Dronedarone.
GuidetoPHARMACOLOGY; 514; -.
iPTMnet; O95069; -.
PhosphoSitePlus; O95069; -.
BioMuta; KCNK2; -.
PaxDb; O95069; -.
PeptideAtlas; O95069; -.
PRIDE; O95069; -.
Ensembl; ENST00000391894; ENSP00000375764; ENSG00000082482. [O95069-2]
Ensembl; ENST00000391895; ENSP00000375765; ENSG00000082482. [O95069-3]
Ensembl; ENST00000444842; ENSP00000394033; ENSG00000082482. [O95069-1]
Ensembl; ENST00000467031; ENSP00000420203; ENSG00000082482. [O95069-4]
GeneID; 3776; -.
KEGG; hsa:3776; -.
UCSC; uc001hkq.4; human. [O95069-1]
CTD; 3776; -.
DisGeNET; 3776; -.
GeneCards; KCNK2; -.
HGNC; HGNC:6277; KCNK2.
HPA; HPA056054; -.
MIM; 603219; gene.
neXtProt; NX_O95069; -.
OpenTargets; ENSG00000082482; -.
PharmGKB; PA30059; -.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000137657; -.
HOVERGEN; HBG052234; -.
InParanoid; O95069; -.
KO; K04913; -.
OMA; AINVMKW; -.
OrthoDB; EOG091G0E3R; -.
PhylomeDB; O95069; -.
TreeFam; TF313947; -.
Reactome; R-HSA-1299503; TWIK related potassium channel (TREK).
Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
ChiTaRS; KCNK2; human.
GeneWiki; KCNK2; -.
GenomeRNAi; 3776; -.
PRO; PR:O95069; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000082482; -.
CleanEx; HS_KCNK2; -.
ExpressionAtlas; O95069; baseline and differential.
Genevisible; O95069; HS.
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:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0019870; F:potassium channel inhibitor activity; ISS:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
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; IEA:Ensembl.
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:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
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; 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;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endoplasmic reticulum; 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_0000101742.
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 193 223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 224 244 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}.
REGION 378 426 Essential for chloroform and halothane
sensitivity. {ECO:0000250}.
MOD_RES 348 348 Phosphoserine; by PKA.
{ECO:0000269|PubMed:11319556}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4TWK, ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 108 108 Interchain. {ECO:0000244|PDB:4TWK}.
VAR_SEQ 1 16 MLPSASRERPGYRAGV -> MMNPRAKRDFYL (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_024428.
VAR_SEQ 2 16 Missing (in isoform 2).
{ECO:0000303|PubMed:10321245,
ECO:0000303|PubMed:10784345,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_024429.
VAR_SEQ 213 232 KWNVSQTKIRIISTIIFILF -> VDPILNIWTSISLSCGS
GSL (in isoform 4).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_047567.
VAR_SEQ 233 426 Missing (in isoform 4).
{ECO:0000303|PubMed:24196565}.
/FTId=VSP_047568.
MUTAGEN 348 348 S->A: Mimics non-phosphorylated state and
has no effect on leak channel activity.
{ECO:0000269|PubMed:11319556}.
MUTAGEN 348 348 S->D: Phosphomimetic mutant which causes
switch to voltage-dependent outward
rectifier channel activity.
{ECO:0000269|PubMed:11319556}.
CONFLICT 309 311 DWL -> RLV (in Ref. 3; AAD01203).
{ECO:0000305}.
CONFLICT 391 391 S -> N (in Ref. 1; AAD47569).
{ECO:0000305}.
CONFLICT 411 411 T -> A (in Ref. 3; AAD01203).
{ECO:0000305}.
HELIX 54 105 {ECO:0000244|PDB:4TWK}.
HELIX 111 127 {ECO:0000244|PDB:4TWK}.
TURN 133 137 {ECO:0000244|PDB:4TWK}.
STRAND 141 143 {ECO:0000244|PDB:4TWK}.
HELIX 144 155 {ECO:0000244|PDB:4TWK}.
HELIX 168 213 {ECO:0000244|PDB:4TWK}.
HELIX 218 237 {ECO:0000244|PDB:4TWK}.
HELIX 242 247 {ECO:0000244|PDB:4TWK}.
HELIX 253 264 {ECO:0000244|PDB:4TWK}.
HELIX 287 315 {ECO:0000244|PDB:4TWK}.
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


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