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Potassium voltage-gated channel subfamily E member 1 (Delayed rectifier potassium channel subunit IsK) (IKs producing slow voltage-gated potassium channel subunit beta Mink) (Minimal potassium channel)

 KCNE1_HUMAN             Reviewed;         129 AA.
P15382; A5H1P2; Q8N709; Q91Z94;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
20-JUN-2018, entry version 188.
RecName: Full=Potassium voltage-gated channel subfamily E member 1;
AltName: Full=Delayed rectifier potassium channel subunit IsK;
AltName: Full=IKs producing slow voltage-gated potassium channel subunit beta Mink;
AltName: Full=Minimal potassium channel;
Name=KCNE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2730656; DOI=10.1016/0006-291X(89)91577-5;
Murai T., Kakizuka A., Takumi T., Ohkubo H., Nakanishi S.;
"Molecular cloning and sequence analysis of human genomic DNA encoding
a novel membrane protein which exhibits a slowly activating potassium
channel activity.";
Biochem. Biophys. Res. Commun. 161:176-181(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-38.
TISSUE=Leukocyte;
PubMed=7828904; DOI=10.1016/0378-1119(94)90685-8;
Lai L.P., Deng C.L., Moss A.J., Kass R.S., Liang C.S.;
"Polymorphism of the gene encoding a human minimal potassium ion
channel (minK).";
Gene 151:339-340(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cornea;
Rae J.L.;
"Delayed rectifier potassium channel subunit from human cornea
epithelium.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-32 AND
GLY-38.
TISSUE=Testis;
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).
[6]
TISSUE SPECIFICITY.
PubMed=9312006; DOI=10.1093/emboj/16.17.5472;
Chouabe C., Neyroud N., Guicheney P., Lazdunski M., Romey G.,
Barhanin J.;
"Properties of KvLQT1 K+ channel mutations in Romano-Ward and Jervell
and Lange-Nielsen inherited cardiac arrhythmias.";
EMBO J. 16:5472-5479(1997).
[7]
INTERACTION WITH KCNH2.
PubMed=9230439; DOI=10.1038/40882;
McDonald T.V., Yu Z., Ming Z., Palma E., Meyers M.B., Wang K.-W.,
Goldstein S.A.N., Fishman G.I.;
"A minK-HERG complex regulates the cardiac potassium current I(Kr).";
Nature 388:289-292(1997).
[8]
MUTAGENESIS OF LYS-69.
PubMed=11874988; DOI=10.1096/fj.01-0520hyp;
Abbott G.W., Goldstein S.A.N.;
"Disease-associated mutations in KCNE potassium channel subunits
(MiRPs) reveal promiscuous disruption of multiple currents and
conservation of mechanism.";
FASEB J. 16:390-400(2002).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19219384; DOI=10.1007/s00232-009-9154-8;
McCrossan Z.A., Roepke T.K., Lewis A., Panaghie G., Abbott G.W.;
"Regulation of the Kv2.1 potassium channel by MinK and MiRP1.";
J. Membr. Biol. 228:1-14(2009).
[10]
INTERACTION WITH KCNQ1, AND SUBCELLULAR LOCATION.
PubMed=20533308; DOI=10.1002/jcp.22265;
Roura-Ferrer M., Sole L., Oliveras A., Dahan R., Bielanska J.,
Villarroel A., Comes N., Felipe A.;
"Impact of KCNE subunits on KCNQ1 (Kv7.1) channel membrane surface
targeting.";
J. Cell. Physiol. 225:692-700(2010).
[11]
GLYCOSYLATION AT ASN-5 AND ASN-26, AND CHARACTERIZATION OF VARIANT
JLNS2 ILE-7.
PubMed=21676880; DOI=10.1074/jbc.M111.235168;
Bas T., Gao G.Y., Lvov A., Chandrasekhar K.D., Gilmore R.,
Kobertz W.R.;
"Post-translational N-glycosylation of type I transmembrane KCNE1
peptides: implications for membrane protein biogenesis and disease.";
J. Biol. Chem. 286:28150-28159(2011).
[12]
GLYCOSYLATION AT ASN-5 AND THR-7, AND MUTAGENESIS OF ASN-5; THR-6;
THR-7 AND SER-28.
PubMed=21669976; DOI=10.1113/jphysiol.2011.211284;
Chandrasekhar K.D., Lvov A., Terrenoire C., Gao G.Y., Kass R.S.,
Kobertz W.R.;
"O-glycosylation of the cardiac I(Ks) complex.";
J. Physiol. (Lond.) 589:3721-3730(2011).
[13]
MUTAGENESIS OF LYS-15; GLU-19 AND ARG-32, AND SITE GLU-19.
PubMed=26307551; DOI=10.1038/srep13399;
Sun P., Wu F., Wen M., Yang X., Wang C., Li Y., He S., Zhang L.,
Zhang Y., Tian C.;
"A distinct three-helix centipede toxin SSD609 inhibits I(ks) channels
by interacting with the KCNE1 auxiliary subunit.";
Sci. Rep. 5:13399-13399(2015).
[14]
STRUCTURE BY NMR.
PubMed=18611041; DOI=10.1021/bi800875q;
Kang C., Tian C., Soennichsen F.D., Smith J.A., Meiler J.,
George A.L. Jr., Vanoye C.G., Kim H.J., Sanders C.R.;
"Structure of KCNE1 and implications for how it modulates the KCNQ1
potassium channel.";
Biochemistry 47:7999-8006(2008).
[15]
VARIANT ASN-85.
PubMed=8899564; DOI=10.1006/jmcc.1996.0198;
Tesson F., Donger C., Denjoy I., Berthet M., Bennaceur M., Petit C.,
Coumel P., Schwartz K., Guicheney P.;
"Exclusion of KCNE1 (IsK) as a candidate gene for Jervell and Lange-
Nielsen syndrome.";
J. Mol. Cell. Cardiol. 28:2051-2055(1996).
[16]
VARIANT JLNS2 58-PRO-PRO-59.
PubMed=9328483; DOI=10.1093/hmg/6.12.2179;
Tyson J., Tranebjaerg L., Bellman S., Wren C., Taylor J.F.N.,
Bathen J., Aslaksen B., Soerland S.J., Lund O., Malcolm S.,
Pembrey M., Bhattacharya S., Bitner-Glindzicz M.;
"IsK and KvLQT1: mutation in either of the two subunits of the slow
component of the delayed rectifier potassium channel can cause Jervell
and Lange-Nielsen syndrome.";
Hum. Mol. Genet. 6:2179-2185(1997).
[17]
VARIANTS JLNS2 ILE-7 AND ASN-76.
PubMed=9354783; DOI=10.1038/ng1197-267;
Schulze-Bahr E., Wang Q., Wedekind H., Haverkamp W., Chen Q., Sun Y.,
Rubie C., Hordt M., Towbin J.A., Borggrefe M., Assmann G., Qu X.,
Somberg J.C., Breithardt G., Oberti C., Funke H.;
"KCNE1 mutations cause Jervell and Lange-Nielsen syndrome.";
Nat. Genet. 17:267-268(1997).
[18]
VARIANTS LQT5 LEU-74 AND ASN-76.
PubMed=9354802; DOI=10.1038/ng1197-338;
Splawski I., Tristani-Firouzi M., Lehmann M.H., Sanguinetti M.C.,
Keating M.T.;
"Mutations in the hminK gene cause long QT syndrome and suppress IKs
function.";
Nat. Genet. 17:338-340(1997).
[19]
VARIANT LQT5 ASN-76.
PubMed=9445165; DOI=10.1161/01.CIR.97.2.142;
Duggal P., Vesely M.R., Wattanasirichaigoon D., Villafane J.,
Kaushik V., Beggs A.H.;
"Mutation of the gene for IsK associated with both Jervell and Lange-
Nielsen and Romano-Ward forms of Long-QT syndrome.";
Circulation 97:142-146(1998).
[20]
VARIANTS JLNS2 PHE-47; HIS-51 AND ASN-76, AND VARIANT LQT5 ARG-87.
PubMed=10400998; DOI=10.1093/hmg/8.8.1499;
Bianchi L., Shen Z., Dennis A.T., Priori S.G., Napolitano C.,
Ronchetti E., Bryskin R., Schwartz P.J., Brown A.M.;
"Cellular dysfunction of LQT5-minK mutants: abnormalities of IKs, IKr
and trafficking in long QT syndrome.";
Hum. Mol. Genet. 8:1499-1507(1999).
[21]
VARIANTS LQT5 HIS-32; TRP-98 AND THR-127.
PubMed=10973849; DOI=10.1161/01.CIR.102.10.1178;
Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S.G.,
Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M.,
Keating M.T.;
"Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A,
KCNE1, and KCNE2.";
Circulation 102:1178-1185(2000).
[22]
VARIANT LQT5 ILE-109.
PubMed=11692163; DOI=10.1007/s001090100249;
Schulze-Bahr E., Schwarz M., Hauenschild S., Wedekind H., Funke H.,
Haverkamp W., Breithardt W., Pongs O., Isbrandt D., Breithardt G.;
"A novel long-QT 5 gene mutation in the C-terminus (V109I) is
associated with a mild phenotype.";
J. Mol. Med. 79:504-509(2001).
[23]
VARIANT ASN-85.
PubMed=15051636; DOI=10.1161/01.CIR.0000125524.34234.13;
Westenskow P., Splawski I., Timothy K.W., Keating M.T.,
Sanguinetti M.C.;
"Compound mutations: a common cause of severe long-QT syndrome.";
Circulation 109:1834-1841(2004).
[24]
VARIANTS LQT5 HIS-36 AND SER-53.
PubMed=16414944; DOI=10.1001/jama.294.23.2975;
Napolitano C., Priori S.G., Schwartz P.J., Bloise R., Ronchetti E.,
Nastoli J., Bottelli G., Cerrone M., Leonardi S.;
"Genetic testing in the long QT syndrome: development and validation
of an efficient approach to genotyping in clinical practice.";
JAMA 294:2975-2980(2005).
[25]
VARIANTS GLY-38 AND ASN-85, AND CHARACTERIZATION OF VARIANT ASN-85.
PubMed=16823764; DOI=10.1002/humu.20360;
Van Laer L., Carlsson P.-I., Ottschytsch N., Bondeson M.-L.,
Konings A., Vandevelde A., Dieltjens N., Fransen E., Snyders D.,
Borg E., Raes A., Van Camp G.;
"The contribution of genes involved in potassium-recycling in the
inner ear to noise-induced hearing loss.";
Hum. Mutat. 27:786-795(2006).
[26]
VARIANTS LQT5 VAL-8; MET-10; LEU-28; HIS-32; SER-55; PRO-58; PRO-59;
CYS-67; HIS-67; MET-70; ASN-76; LYS-83 AND MET-125.
PubMed=19716085; DOI=10.1016/j.hrthm.2009.05.021;
Kapplinger J.D., Tester D.J., Salisbury B.A., Carr J.L.,
Harris-Kerr C., Pollevick G.D., Wilde A.A., Ackerman M.J.;
"Spectrum and prevalence of mutations from the first 2,500 consecutive
unrelated patients referred for the FAMILION long QT syndrome genetic
test.";
Heart Rhythm 6:1297-1303(2009).
[27]
CHARACTERIZATION OF VARIANTS LQT5 ILE-109 AND THR-127, AND MUTAGENESIS
OF 109-VAL--PRO-129.
PubMed=25037568; DOI=10.1242/jcs.147033;
Dvir M., Strulovich R., Sachyani D., Ben-Tal Cohen I., Haitin Y.,
Dessauer C., Pongs O., Kass R., Hirsch J.A., Attali B.;
"Long QT mutations at the interface between KCNQ1 helix C and KCNE1
disrupt I(KS) regulation by PKA and PIP(2).";
J. Cell Sci. 127:3943-3955(2014).
-!- FUNCTION: Ancillary protein that assembles as a beta subunit with
a voltage-gated potassium channel complex of pore-forming alpha
subunits. Modulates the gating kinetics and enhances stability of
the channel complex. Assembled with KCNB1 modulates the gating
characteristics of the delayed rectifier voltage-dependent
potassium channel KCNB1 (PubMed:19219384). Assembled with
KCNQ1/KVLQT1 is proposed to form the slowly activating delayed
rectifier cardiac potassium (IKs) channel. The outward current
reaches its steady state only after 50 seconds. Assembled with
KCNH2/HERG may modulate the rapidly activating component of the
delayed rectifying potassium current in heart (IKr).
{ECO:0000269|PubMed:19219384}.
-!- SUBUNIT: Interacts with KCNB1. Interacts with KCNC2 (By
similarity). Associates with KCNH2/HERG (PubMed:9230439).
Interacts with KNCQ1; targets the complex KNCQ1-KCNE1 to the
membrane raft (PubMed:20533308). The complex KNCQ1-KNCE1 interacts
with the scolopendra toxin SSD609 (PubMed:26307551).
{ECO:0000250|UniProtKB:P15383, ECO:0000269|PubMed:20533308,
ECO:0000269|PubMed:9230439}.
-!- INTERACTION:
P51787:KCNQ1; NbExp=4; IntAct=EBI-7043557, EBI-359667;
A6HIS0:Tcap (xeno); NbExp=3; IntAct=EBI-7043557, EBI-8784724;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19219384};
Single-pass type I membrane protein {ECO:0000305}. Apical cell
membrane {ECO:0000250|UniProtKB:P15383}. Membrane raft
{ECO:0000269|PubMed:20533308}. Note=Colocalizes with KCNB1 at the
plasma membrane (By similarity). Targets to the membrane raft when
associated with KCNQ1 (PubMed:20533308).
{ECO:0000250|UniProtKB:P15383, ECO:0000269|PubMed:20533308}.
-!- TISSUE SPECIFICITY: Expressed in lung, kidney, testis, ovaries,
small intestine, peripheral blood leukocytes. Expressed in the
heart (PubMed:19219384). Not detected in pancreas, spleen,
prostate and colon. Restrictively localized in the apical membrane
portion of epithelial cells. {ECO:0000269|PubMed:19219384,
ECO:0000269|PubMed:9312006}.
-!- PTM: Phosphorylation inhibits the potassium current.
{ECO:0000250}.
-!- PTM: N-glycosylation at Asn-26 occurs post-translationally, and
requires prior cotranslational glycosylation at Asn-5.
{ECO:0000269|PubMed:21669976, ECO:0000269|PubMed:21676880}.
-!- DISEASE: Jervell and Lange-Nielsen syndrome 2 (JLNS2)
[MIM:612347]: An autosomal recessive disorder characterized by
congenital deafness, prolongation of the QT interval, syncopal
attacks due to ventricular arrhythmias, and a high risk of sudden
death. {ECO:0000269|PubMed:10400998, ECO:0000269|PubMed:21676880,
ECO:0000269|PubMed:9328483, ECO:0000269|PubMed:9354783}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Long QT syndrome 5 (LQT5) [MIM:613695]: A heart disorder
characterized by a prolonged QT interval on the ECG and
polymorphic ventricular arrhythmias. They cause syncope and sudden
death in response to exercise or emotional stress, and can present
with a sentinel event of sudden cardiac death in infancy.
{ECO:0000269|PubMed:10400998, ECO:0000269|PubMed:10973849,
ECO:0000269|PubMed:11692163, ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:25037568,
ECO:0000269|PubMed:9354802, ECO:0000269|PubMed:9445165}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the potassium channel KCNE family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH36452.1; Type=Erroneous termination; Positions=106; Note=Translated as Cys.; Evidence={ECO:0000305};
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EMBL; M26685; AAA36129.1; -; Genomic_DNA.
EMBL; L33815; AAA63905.1; -; Genomic_DNA.
EMBL; L28168; AAA58418.1; -; mRNA.
EMBL; AF135188; AAD25096.1; -; mRNA.
EMBL; DQ784803; ABQ01238.1; -; Genomic_DNA.
EMBL; BC036452; AAH36452.1; ALT_SEQ; mRNA.
CCDS; CCDS13636.1; -.
PIR; A32447; A32447.
RefSeq; NP_000210.2; NM_000219.5.
RefSeq; NP_001121140.1; NM_001127668.3.
RefSeq; NP_001121141.1; NM_001127669.3.
RefSeq; NP_001121142.1; NM_001127670.3.
RefSeq; NP_001257331.1; NM_001270402.2.
RefSeq; NP_001257332.1; NM_001270403.2.
RefSeq; NP_001257333.1; NM_001270404.2.
RefSeq; NP_001257334.1; NM_001270405.2.
UniGene; Hs.121495; -.
UniGene; Hs.745384; -.
PDB; 2K21; NMR; -; A=1-129.
PDBsum; 2K21; -.
DisProt; DP00796; -.
ProteinModelPortal; P15382; -.
SMR; P15382; -.
BioGrid; 109955; 23.
ComplexPortal; CPX-3072; Voltage-gated potassium channel complex variant 1.
ComplexPortal; CPX-3271; KCNQ1-KCNE1 I(Ks) channel complex.
CORUM; P15382; -.
IntAct; P15382; 4.
MINT; P15382; -.
STRING; 9606.ENSP00000337255; -.
BindingDB; P15382; -.
ChEMBL; CHEMBL4872; -.
DrugBank; DB04957; Azimilide.
DrugBank; DB00808; Indapamide.
iPTMnet; P15382; -.
PhosphoSitePlus; P15382; -.
BioMuta; KCNE1; -.
DMDM; 116416; -.
PaxDb; P15382; -.
PeptideAtlas; P15382; -.
PRIDE; P15382; -.
ProteomicsDB; 53134; -.
DNASU; 3753; -.
Ensembl; ENST00000337385; ENSP00000337255; ENSG00000180509.
Ensembl; ENST00000399284; ENSP00000382225; ENSG00000180509.
Ensembl; ENST00000399286; ENSP00000382226; ENSG00000180509.
Ensembl; ENST00000399289; ENSP00000382228; ENSG00000180509.
Ensembl; ENST00000416357; ENSP00000416258; ENSG00000180509.
Ensembl; ENST00000432085; ENSP00000412498; ENSG00000180509.
Ensembl; ENST00000611936; ENSP00000478215; ENSG00000180509.
Ensembl; ENST00000621601; ENSP00000483895; ENSG00000180509.
GeneID; 3753; -.
KEGG; hsa:3753; -.
UCSC; uc002ytz.5; human.
CTD; 3753; -.
DisGeNET; 3753; -.
EuPathDB; HostDB:ENSG00000180509.11; -.
GeneCards; KCNE1; -.
GeneReviews; KCNE1; -.
HGNC; HGNC:6240; KCNE1.
MalaCards; KCNE1; -.
MIM; 176261; gene.
MIM; 612347; phenotype.
MIM; 613695; phenotype.
neXtProt; NX_P15382; -.
OpenTargets; ENSG00000180509; -.
Orphanet; 334; Familial atrial fibrillation.
Orphanet; 90647; Jervell and Lange-Nielsen syndrome.
Orphanet; 101016; Romano-Ward syndrome.
PharmGKB; PA211; -.
eggNOG; ENOG410IY71; Eukaryota.
eggNOG; ENOG410Y1SF; LUCA.
GeneTree; ENSGT00510000048994; -.
HOGENOM; HOG000113207; -.
HOVERGEN; HBG052226; -.
InParanoid; P15382; -.
KO; K04894; -.
OMA; ALYILMV; -.
OrthoDB; EOG091G0UDJ; -.
PhylomeDB; P15382; -.
TreeFam; TF335976; -.
Reactome; R-HSA-5576890; Phase 3 - rapid repolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
SIGNOR; P15382; -.
ChiTaRS; KCNE1; human.
EvolutionaryTrace; P15382; -.
GeneWiki; KCNE1; -.
GenomeRNAi; 3753; -.
PRO; PR:P15382; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000180509; -.
CleanEx; HS_KCNE1; -.
ExpressionAtlas; P15382; baseline and differential.
Genevisible; P15382; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005764; C:lysosome; HDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
GO; GO:0031433; F:telethonin binding; IPI:BHF-UCL.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL.
GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
GO; GO:0086011; P:membrane repolarization during action potential; IDA:BHF-UCL.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IDA:BHF-UCL.
GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:BHF-UCL.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0071435; P:potassium ion export; IDA:BHF-UCL.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
InterPro; IPR000369; K_chnl_KCNE.
InterPro; IPR005424; K_chnl_volt-dep_bsu_KCNE1.
PANTHER; PTHR15282; PTHR15282; 1.
Pfam; PF02060; ISK_Channel; 1.
PRINTS; PR01604; KCNE1CHANNEL.
PRINTS; PR00168; KCNECHANNEL.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Deafness;
Disease mutation; Glycoprotein; Ion channel; Ion transport;
Long QT syndrome; Membrane; Phosphoprotein; Polymorphism; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 129 Potassium voltage-gated channel subfamily
E member 1.
/FTId=PRO_0000144278.
TRANSMEM 44 66 Helical. {ECO:0000255}.
TOPO_DOM 67 129 Cytoplasmic. {ECO:0000255}.
REGION 109 129 interaction with KCNQ1 C-terminus.
{ECO:0000269|PubMed:25037568}.
SITE 19 19 Interacts with the scolopendra toxin
SSD609. {ECO:0000269|PubMed:26307551}.
MOD_RES 102 102 Phosphoserine; by PKC. {ECO:0000250}.
CARBOHYD 5 5 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21669976,
ECO:0000269|PubMed:21676880}.
CARBOHYD 7 7 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:21669976}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21676880}.
VARIANT 7 7 T -> I (in JLNS2; impairs glycosylation
at N-5; dbSNP:rs28933384).
{ECO:0000269|PubMed:21676880,
ECO:0000269|PubMed:9354783}.
/FTId=VAR_008897.
VARIANT 8 8 A -> V (in LQT5; unknown pathological
significance; dbSNP:rs199473348).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074908.
VARIANT 10 10 T -> M (in LQT5; unknown pathological
significance; dbSNP:rs144917638).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074909.
VARIANT 28 28 S -> L (in LQT5; unknown pathological
significance; dbSNP:rs199473350).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074910.
VARIANT 32 32 R -> H (in LQT5; unknown pathological
significance; dbSNP:rs17857111).
{ECO:0000269|PubMed:10973849,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_009906.
VARIANT 36 36 R -> H (in LQT5; unknown pathological
significance; dbSNP:rs199473351).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074911.
VARIANT 38 38 S -> G (in dbSNP:rs1805127).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16823764,
ECO:0000269|PubMed:7828904}.
/FTId=VAR_001558.
VARIANT 47 47 V -> F (in JLNS2; dbSNP:rs199473353).
{ECO:0000269|PubMed:10400998}.
/FTId=VAR_008898.
VARIANT 51 51 L -> H (in JLNS2).
{ECO:0000269|PubMed:10400998}.
/FTId=VAR_008899.
VARIANT 52 52 G -> A (in dbSNP:rs17173509).
/FTId=VAR_048024.
VARIANT 53 53 F -> S (in LQT5; unknown pathological
significance; dbSNP:rs199473355).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074912.
VARIANT 55 55 G -> S (in LQT5; unknown pathological
significance; dbSNP:rs199473644).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074913.
VARIANT 58 59 TL -> PP (in JLNS2; dbSNP:rs281865421).
/FTId=VAR_001559.
VARIANT 58 58 T -> P (in LQT5; unknown pathological
significance; dbSNP:rs147187721).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074914.
VARIANT 59 59 L -> P (in LQT5; unknown pathological
significance; dbSNP:rs141813529).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074915.
VARIANT 67 67 R -> C (in LQT5; unknown pathological
significance; dbSNP:rs199473645).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074916.
VARIANT 67 67 R -> H (in LQT5; unknown pathological
significance; dbSNP:rs79654911).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074917.
VARIANT 70 70 K -> M (in LQT5; unknown pathological
significance; dbSNP:rs199473646).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074918.
VARIANT 74 74 S -> L (in LQT5; dbSNP:rs74315446).
{ECO:0000269|PubMed:9354802}.
/FTId=VAR_008900.
VARIANT 76 76 D -> N (in LQT5 and JLNS2; suppresses
KCNQ1 currents markedly;
dbSNP:rs74315445).
{ECO:0000269|PubMed:10400998,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9354783,
ECO:0000269|PubMed:9354802,
ECO:0000269|PubMed:9445165}.
/FTId=VAR_008901.
VARIANT 83 83 E -> K (in LQT5; unknown pathological
significance; dbSNP:rs199473360).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074919.
VARIANT 85 85 D -> N (predisposes to acquired LQT5
susceptibility; shows a significant
difference in current density and
midpoint potential compared to the wild-
type channel; dbSNP:rs1805128).
{ECO:0000269|PubMed:15051636,
ECO:0000269|PubMed:16823764,
ECO:0000269|PubMed:8899564}.
/FTId=VAR_008902.
VARIANT 87 87 W -> R (in LQT5; dbSNP:rs199473361).
{ECO:0000269|PubMed:10400998}.
/FTId=VAR_008903.
VARIANT 98 98 R -> W (in LQT5; dbSNP:rs199473362).
{ECO:0000269|PubMed:10973849}.
/FTId=VAR_009907.
VARIANT 109 109 V -> I (in LQT5; mild phenotype; no
effect on KCNQ1 C-terminus interaction;
increases cAMP-mediated up-regulation of
the I(KS) current; no effect on
phosphorylation at S27;
dbSNP:rs77442996).
{ECO:0000269|PubMed:11692163,
ECO:0000269|PubMed:25037568}.
/FTId=VAR_012802.
VARIANT 125 125 T -> M (in LQT5; unknown pathological
significance; dbSNP:rs142511345).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074920.
VARIANT 127 127 P -> T (in LQT5; moderately reduces I(KS)
current density; no change of the voltage
dependence of channel activation;
markedly reduces interaction with KCNQ1
C-terminus; no effect on plasma membrane
localization; loss of cAMP-mediated up-
regulation of the I(KS) current; no
effect on interaction with AKAP9; impairs
phosphorylation at S-27 during cAMP-
dependent stimulation;
dbSNP:rs199473647).
{ECO:0000269|PubMed:10973849,
ECO:0000269|PubMed:25037568}.
/FTId=VAR_009908.
MUTAGEN 5 5 N->Q: No measurable effect on assembly
with KCNQ1 or cell surface expression of
the KCNE1/KCNQ1 channel complex, and loss
of glycosylation at N-5; when associated
with T-28. {ECO:0000269|PubMed:21669976}.
MUTAGEN 6 6 T->F: No measurable effect on assembly
with KCNQ1 or cell surface expression of
the KCNE1/KCNQ1 channel complex. Loss of
glycosylation at T-7.
{ECO:0000269|PubMed:21669976}.
MUTAGEN 7 7 T->A: 50% reduction of cell surface
expression of the KCNE1/KCNQ1 channel
complex, and loss of glycosylation at N-5
and T-7; when associated with T-28.
{ECO:0000269|PubMed:21669976}.
MUTAGEN 15 15 K->D: No change in inhibition of the
complex KCNQ1-KCNE1 by the scolopendra
toxin SSD609.
{ECO:0000269|PubMed:26307551}.
MUTAGEN 19 19 E->K: Loss inhibition of the complex
KCNQ1-KCNE1 by the scolopendra toxin
SSD609. {ECO:0000269|PubMed:26307551}.
MUTAGEN 28 28 S->T: No measurable effect on assembly
with KCNQ1 or cell surface expression of
the KCNE1/KCNQ1 channel complex, and loss
of glycosylation at N-5; when associated
with Q-5. 50% reduction of cell surface
expression of the KCNE1/KCNQ1 channel
complex, and loss of glycosylation at N-5
and T-7; when associated with A-7.
{ECO:0000269|PubMed:21669976}.
MUTAGEN 32 32 R->D: Increase in inhibition of the
complex KCNQ1-KCNE1 by the scolopendra
toxin SSD609.
{ECO:0000269|PubMed:26307551}.
MUTAGEN 69 69 K->H: Lowers current 2-fold and leads to
faster deactivation of KCNQ1/KCNE1
channel. {ECO:0000269|PubMed:11874988}.
MUTAGEN 109 129 Missing: Totally suppressed interaction
with KCNQ1 C-terminus.
{ECO:0000269|PubMed:25037568}.
HELIX 4 9 {ECO:0000244|PDB:2K21}.
HELIX 13 22 {ECO:0000244|PDB:2K21}.
HELIX 30 32 {ECO:0000244|PDB:2K21}.
HELIX 46 71 {ECO:0000244|PDB:2K21}.
TURN 77 81 {ECO:0000244|PDB:2K21}.
TURN 84 86 {ECO:0000244|PDB:2K21}.
HELIX 92 105 {ECO:0000244|PDB:2K21}.
STRAND 114 116 {ECO:0000244|PDB:2K21}.
SEQUENCE 129 AA; 14675 MW; 5442D70929D4E87E CRC64;
MILSNTTAVT PFLTKLWQET VQQGGNMSGL ARRSPRSSDG KLEALYVLMV LGFFGFFTLG
IMLSYIRSKK LEHSNDPFNV YIESDAWQEK DKAYVQARVL ESYRSCYVVE NHLAIEQPNT
HLPETKPSP


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