ID KCNE1_HUMAN Reviewed; 129 AA. AC P15382; A5H1P2; Q8N709; Q91Z94; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 07-APR-2021, entry version 206. DE RecName: Full=Potassium voltage-gated channel subfamily E member 1; DE AltName: Full=Delayed rectifier potassium channel subunit IsK; DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit beta Mink; DE AltName: Full=Minimal potassium channel; GN Name=KCNE1; 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 [GENOMIC DNA]. RX PubMed=2730656; DOI=10.1016/0006-291x(89)91577-5; RA Murai T., Kakizuka A., Takumi T., Ohkubo H., Nakanishi S.; RT "Molecular cloning and sequence analysis of human genomic DNA encoding a RT novel membrane protein which exhibits a slowly activating potassium channel RT activity."; RL Biochem. Biophys. Res. Commun. 161:176-181(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-38. RC TISSUE=Leukocyte; RX PubMed=7828904; DOI=10.1016/0378-1119(94)90685-8; RA Lai L.P., Deng C.L., Moss A.J., Kass R.S., Liang C.S.; RT "Polymorphism of the gene encoding a human minimal potassium ion channel RT (minK)."; RL Gene 151:339-340(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cornea; RA Rae J.L.; RT "Delayed rectifier potassium channel subunit from human cornea RT epithelium."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-32 AND GLY-38. RC TISSUE=Testis; 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 [6] RP TISSUE SPECIFICITY. RX PubMed=9312006; DOI=10.1093/emboj/16.17.5472; RA Chouabe C., Neyroud N., Guicheney P., Lazdunski M., Romey G., Barhanin J.; RT "Properties of KvLQT1 K+ channel mutations in Romano-Ward and Jervell and RT Lange-Nielsen inherited cardiac arrhythmias."; RL EMBO J. 16:5472-5479(1997). RN [7] RP INTERACTION WITH KCNH2. RX PubMed=9230439; DOI=10.1038/40882; RA McDonald T.V., Yu Z., Ming Z., Palma E., Meyers M.B., Wang K.-W., RA Goldstein S.A.N., Fishman G.I.; RT "A minK-HERG complex regulates the cardiac potassium current I(Kr)."; RL Nature 388:289-292(1997). RN [8] RP MUTAGENESIS OF LYS-69. RX PubMed=11874988; DOI=10.1096/fj.01-0520hyp; RA Abbott G.W., Goldstein S.A.N.; RT "Disease-associated mutations in KCNE potassium channel subunits (MiRPs) RT reveal promiscuous disruption of multiple currents and conservation of RT mechanism."; RL FASEB J. 16:390-400(2002). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=19219384; DOI=10.1007/s00232-009-9154-8; RA McCrossan Z.A., Roepke T.K., Lewis A., Panaghie G., Abbott G.W.; RT "Regulation of the Kv2.1 potassium channel by MinK and MiRP1."; RL J. Membr. Biol. 228:1-14(2009). RN [10] RP INTERACTION WITH KCNQ1, AND SUBCELLULAR LOCATION. RX PubMed=20533308; DOI=10.1002/jcp.22265; RA Roura-Ferrer M., Sole L., Oliveras A., Dahan R., Bielanska J., RA Villarroel A., Comes N., Felipe A.; RT "Impact of KCNE subunits on KCNQ1 (Kv7.1) channel membrane surface RT targeting."; RL J. Cell. Physiol. 225:692-700(2010). RN [11] RP GLYCOSYLATION AT ASN-5 AND ASN-26, AND CHARACTERIZATION OF VARIANT JLNS2 RP ILE-7. RX PubMed=21676880; DOI=10.1074/jbc.m111.235168; RA Bas T., Gao G.Y., Lvov A., Chandrasekhar K.D., Gilmore R., Kobertz W.R.; RT "Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: RT implications for membrane protein biogenesis and disease."; RL J. Biol. Chem. 286:28150-28159(2011). RN [12] RP GLYCOSYLATION AT ASN-5 AND THR-7, AND MUTAGENESIS OF ASN-5; THR-6; THR-7 RP AND SER-28. RX PubMed=21669976; DOI=10.1113/jphysiol.2011.211284; RA Chandrasekhar K.D., Lvov A., Terrenoire C., Gao G.Y., Kass R.S., RA Kobertz W.R.; RT "O-glycosylation of the cardiac I(Ks) complex."; RL J. Physiol. (Lond.) 589:3721-3730(2011). RN [13] RP MUTAGENESIS OF LYS-15; GLU-19 AND ARG-32, AND SITE GLU-19. RX PubMed=26307551; DOI=10.1038/srep13399; RA Sun P., Wu F., Wen M., Yang X., Wang C., Li Y., He S., Zhang L., Zhang Y., RA Tian C.; RT "A distinct three-helix centipede toxin SSD609 inhibits I(ks) channels by RT interacting with the KCNE1 auxiliary subunit."; RL Sci. Rep. 5:13399-13399(2015). RN [14] RP STRUCTURE BY NMR. RX PubMed=18611041; DOI=10.1021/bi800875q; RA Kang C., Tian C., Soennichsen F.D., Smith J.A., Meiler J., George A.L. Jr., RA Vanoye C.G., Kim H.J., Sanders C.R.; RT "Structure of KCNE1 and implications for how it modulates the KCNQ1 RT potassium channel."; RL Biochemistry 47:7999-8006(2008). RN [15] RP VARIANT ASN-85. RX PubMed=8899564; DOI=10.1006/jmcc.1996.0198; RA Tesson F., Donger C., Denjoy I., Berthet M., Bennaceur M., Petit C., RA Coumel P., Schwartz K., Guicheney P.; RT "Exclusion of KCNE1 (IsK) as a candidate gene for Jervell and Lange-Nielsen RT syndrome."; RL J. Mol. Cell. Cardiol. 28:2051-2055(1996). RN [16] RP VARIANT JLNS2 58-PRO-PRO-59. RX PubMed=9328483; DOI=10.1093/hmg/6.12.2179; RA Tyson J., Tranebjaerg L., Bellman S., Wren C., Taylor J.F.N., Bathen J., RA Aslaksen B., Soerland S.J., Lund O., Malcolm S., Pembrey M., RA Bhattacharya S., Bitner-Glindzicz M.; RT "IsK and KvLQT1: mutation in either of the two subunits of the slow RT component of the delayed rectifier potassium channel can cause Jervell and RT Lange-Nielsen syndrome."; RL Hum. Mol. Genet. 6:2179-2185(1997). RN [17] RP VARIANTS JLNS2 ILE-7 AND ASN-76. RX PubMed=9354783; DOI=10.1038/ng1197-267; RA Schulze-Bahr E., Wang Q., Wedekind H., Haverkamp W., Chen Q., Sun Y., RA Rubie C., Hordt M., Towbin J.A., Borggrefe M., Assmann G., Qu X., RA Somberg J.C., Breithardt G., Oberti C., Funke H.; RT "KCNE1 mutations cause Jervell and Lange-Nielsen syndrome."; RL Nat. Genet. 17:267-268(1997). RN [18] RP VARIANTS LQT5 LEU-74 AND ASN-76. RX PubMed=9354802; DOI=10.1038/ng1197-338; RA Splawski I., Tristani-Firouzi M., Lehmann M.H., Sanguinetti M.C., RA Keating M.T.; RT "Mutations in the hminK gene cause long QT syndrome and suppress IKs RT function."; RL Nat. Genet. 17:338-340(1997). RN [19] RP VARIANT LQT5 ASN-76. RX PubMed=9445165; DOI=10.1161/01.cir.97.2.142; RA Duggal P., Vesely M.R., Wattanasirichaigoon D., Villafane J., Kaushik V., RA Beggs A.H.; RT "Mutation of the gene for IsK associated with both Jervell and Lange- RT Nielsen and Romano-Ward forms of Long-QT syndrome."; RL Circulation 97:142-146(1998). RN [20] RP VARIANTS JLNS2 PHE-47; HIS-51 AND ASN-76, AND VARIANT LQT5 ARG-87. RX PubMed=10400998; DOI=10.1093/hmg/8.8.1499; RA Bianchi L., Shen Z., Dennis A.T., Priori S.G., Napolitano C., Ronchetti E., RA Bryskin R., Schwartz P.J., Brown A.M.; RT "Cellular dysfunction of LQT5-minK mutants: abnormalities of IKs, IKr and RT trafficking in long QT syndrome."; RL Hum. Mol. Genet. 8:1499-1507(1999). RN [21] RP VARIANTS LQT5 HIS-32; TRP-98 AND THR-127. RX PubMed=10973849; DOI=10.1161/01.cir.102.10.1178; RA Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S.G., RA Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M., RA Keating M.T.; RT "Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, RT KCNE1, and KCNE2."; RL Circulation 102:1178-1185(2000). RN [22] RP VARIANT LQT5 ILE-109. RX PubMed=11692163; DOI=10.1007/s001090100249; RA Schulze-Bahr E., Schwarz M., Hauenschild S., Wedekind H., Funke H., RA Haverkamp W., Breithardt W., Pongs O., Isbrandt D., Breithardt G.; RT "A novel long-QT 5 gene mutation in the C-terminus (V109I) is associated RT with a mild phenotype."; RL J. Mol. Med. 79:504-509(2001). RN [23] RP VARIANT ASN-85. RX PubMed=15051636; DOI=10.1161/01.cir.0000125524.34234.13; RA Westenskow P., Splawski I., Timothy K.W., Keating M.T., Sanguinetti M.C.; RT "Compound mutations: a common cause of severe long-QT syndrome."; RL Circulation 109:1834-1841(2004). RN [24] RP VARIANTS LQT5 HIS-36 AND SER-53. RX PubMed=16414944; DOI=10.1001/jama.294.23.2975; RA Napolitano C., Priori S.G., Schwartz P.J., Bloise R., Ronchetti E., RA Nastoli J., Bottelli G., Cerrone M., Leonardi S.; RT "Genetic testing in the long QT syndrome: development and validation of an RT efficient approach to genotyping in clinical practice."; RL JAMA 294:2975-2980(2005). RN [25] RP VARIANTS GLY-38 AND ASN-85, AND CHARACTERIZATION OF VARIANT ASN-85. RX PubMed=16823764; DOI=10.1002/humu.20360; RA Van Laer L., Carlsson P.-I., Ottschytsch N., Bondeson M.-L., Konings A., RA Vandevelde A., Dieltjens N., Fransen E., Snyders D., Borg E., Raes A., RA Van Camp G.; RT "The contribution of genes involved in potassium-recycling in the inner ear RT to noise-induced hearing loss."; RL Hum. Mutat. 27:786-795(2006). RN [26] RP VARIANTS LQT5 VAL-8; MET-10; LEU-28; HIS-32; SER-55; PRO-58; PRO-59; RP CYS-67; HIS-67; MET-70; ASN-76; LYS-83 AND MET-125. RX PubMed=19716085; DOI=10.1016/j.hrthm.2009.05.021; RA Kapplinger J.D., Tester D.J., Salisbury B.A., Carr J.L., Harris-Kerr C., RA Pollevick G.D., Wilde A.A., Ackerman M.J.; RT "Spectrum and prevalence of mutations from the first 2,500 consecutive RT unrelated patients referred for the FAMILION long QT syndrome genetic RT test."; RL Heart Rhythm 6:1297-1303(2009). RN [27] RP CHARACTERIZATION OF VARIANTS LQT5 ILE-109 AND THR-127, AND MUTAGENESIS OF RP 109-VAL--PRO-129. RX PubMed=25037568; DOI=10.1242/jcs.147033; RA Dvir M., Strulovich R., Sachyani D., Ben-Tal Cohen I., Haitin Y., RA Dessauer C., Pongs O., Kass R., Hirsch J.A., Attali B.; RT "Long QT mutations at the interface between KCNQ1 helix C and KCNE1 disrupt RT I(KS) regulation by PKA and PIP(2)."; RL J. Cell Sci. 127:3943-3955(2014). CC -!- FUNCTION: Ancillary protein that assembles as a beta subunit with a CC voltage-gated potassium channel complex of pore-forming alpha subunits. CC Modulates the gating kinetics and enhances stability of the channel CC complex. Assembled with KCNB1 modulates the gating characteristics of CC the delayed rectifier voltage-dependent potassium channel KCNB1 CC (PubMed:19219384). Assembled with KCNQ1/KVLQT1 is proposed to form the CC slowly activating delayed rectifier cardiac potassium (IKs) channel. CC The outward current reaches its steady state only after 50 seconds. CC Assembled with KCNH2/HERG may modulate the rapidly activating component CC of the delayed rectifying potassium current in heart (IKr). CC {ECO:0000269|PubMed:19219384}. CC -!- SUBUNIT: Interacts with KCNB1. Interacts with KCNC2 (By similarity). CC Associates with KCNH2/HERG (PubMed:9230439). Interacts with KNCQ1; CC targets the complex KNCQ1-KCNE1 to the membrane raft (PubMed:20533308). CC The complex KNCQ1-KNCE1 interacts with the scolopendra toxin SSD609 CC (PubMed:26307551). {ECO:0000250|UniProtKB:P15383, CC ECO:0000269|PubMed:20533308, ECO:0000269|PubMed:9230439}. CC -!- INTERACTION: CC P15382; P51787: KCNQ1; NbExp=4; IntAct=EBI-7043557, EBI-359667; CC P15382; A6HIS0: Tcap; Xeno; NbExp=3; IntAct=EBI-7043557, EBI-8784724; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19219384}; CC Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane CC {ECO:0000250|UniProtKB:P15383}. Membrane raft CC {ECO:0000269|PubMed:20533308}. Note=Colocalizes with KCNB1 at the CC plasma membrane (By similarity). Targets to the membrane raft when CC associated with KCNQ1 (PubMed:20533308). {ECO:0000250|UniProtKB:P15383, CC ECO:0000269|PubMed:20533308}. CC -!- TISSUE SPECIFICITY: Expressed in lung, kidney, testis, ovaries, small CC intestine, peripheral blood leukocytes. Expressed in the heart CC (PubMed:19219384). Not detected in pancreas, spleen, prostate and CC colon. Restrictively localized in the apical membrane portion of CC epithelial cells. {ECO:0000269|PubMed:19219384, CC ECO:0000269|PubMed:9312006}. CC -!- PTM: Phosphorylation inhibits the potassium current. {ECO:0000250}. CC -!- PTM: N-glycosylation at Asn-26 occurs post-translationally, and CC requires prior cotranslational glycosylation at Asn-5. CC {ECO:0000269|PubMed:21669976, ECO:0000269|PubMed:21676880}. CC -!- DISEASE: Jervell and Lange-Nielsen syndrome 2 (JLNS2) [MIM:612347]: An CC autosomal recessive disorder characterized by congenital deafness, CC prolongation of the QT interval, syncopal attacks due to ventricular CC arrhythmias, and a high risk of sudden death. CC {ECO:0000269|PubMed:10400998, ECO:0000269|PubMed:21676880, CC ECO:0000269|PubMed:9328483, ECO:0000269|PubMed:9354783}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Long QT syndrome 5 (LQT5) [MIM:613695]: A heart disorder CC characterized by a prolonged QT interval on the ECG and polymorphic CC ventricular arrhythmias. They cause syncope and sudden death in CC response to exercise or emotional stress, and can present with a CC sentinel event of sudden cardiac death in infancy. CC {ECO:0000269|PubMed:10400998, ECO:0000269|PubMed:10973849, CC ECO:0000269|PubMed:11692163, ECO:0000269|PubMed:16414944, CC ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:25037568, CC ECO:0000269|PubMed:9354802, ECO:0000269|PubMed:9445165}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the potassium channel KCNE family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH36452.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M26685; AAA36129.1; -; Genomic_DNA. DR EMBL; L33815; AAA63905.1; -; Genomic_DNA. DR EMBL; L28168; AAA58418.1; -; mRNA. DR EMBL; AF135188; AAD25096.1; -; mRNA. DR EMBL; DQ784803; ABQ01238.1; -; Genomic_DNA. DR EMBL; BC036452; AAH36452.1; ALT_SEQ; mRNA. DR CCDS; CCDS13636.1; -. DR PIR; A32447; A32447. DR RefSeq; NP_000210.2; NM_000219.5. DR RefSeq; NP_001121140.1; NM_001127668.3. DR RefSeq; NP_001121141.1; NM_001127669.3. DR RefSeq; NP_001121142.1; NM_001127670.3. DR RefSeq; NP_001257331.1; NM_001270402.2. DR RefSeq; NP_001257332.1; NM_001270403.2. DR RefSeq; NP_001257333.1; NM_001270404.2. DR RefSeq; NP_001257334.1; NM_001270405.2. DR PDB; 2K21; NMR; -; A=1-129. DR PDBsum; 2K21; -. DR BMRB; P15382; -. DR SMR; P15382; -. DR BioGRID; 109955; 23. DR ComplexPortal; CPX-3072; Voltage-gated potassium channel complex variant 1. DR ComplexPortal; CPX-3271; KCNQ1-KCNE1 I(Ks) channel complex. DR CORUM; P15382; -. DR IntAct; P15382; 4. DR MINT; P15382; -. DR STRING; 9606.ENSP00000337255; -. DR BindingDB; P15382; -. DR ChEMBL; CHEMBL4872; -. DR DrugBank; DB04957; Azimilide. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01069; Promethazine. DR GlyGen; P15382; 3 sites. DR iPTMnet; P15382; -. DR PhosphoSitePlus; P15382; -. DR BioMuta; KCNE1; -. DR DMDM; 116416; -. DR PaxDb; P15382; -. DR PRIDE; P15382; -. DR ProteomicsDB; 53134; -. DR Antibodypedia; 22953; 262 antibodies. DR DNASU; 3753; -. DR Ensembl; ENST00000337385; ENSP00000337255; ENSG00000180509. DR Ensembl; ENST00000399284; ENSP00000382225; ENSG00000180509. DR Ensembl; ENST00000399286; ENSP00000382226; ENSG00000180509. DR Ensembl; ENST00000399289; ENSP00000382228; ENSG00000180509. DR Ensembl; ENST00000416357; ENSP00000416258; ENSG00000180509. DR Ensembl; ENST00000432085; ENSP00000412498; ENSG00000180509. DR Ensembl; ENST00000611936; ENSP00000478215; ENSG00000180509. DR Ensembl; ENST00000621601; ENSP00000483895; ENSG00000180509. DR GeneID; 3753; -. DR KEGG; hsa:3753; -. DR UCSC; uc002ytz.5; human. DR CTD; 3753; -. DR DisGeNET; 3753; -. DR GeneCards; KCNE1; -. DR GeneReviews; KCNE1; -. DR HGNC; HGNC:6240; KCNE1. DR HPA; ENSG00000180509; Tissue enhanced (fallopian). DR MalaCards; KCNE1; -. DR MIM; 176261; gene. DR MIM; 612347; phenotype. DR MIM; 613695; phenotype. DR neXtProt; NX_P15382; -. DR OpenTargets; ENSG00000180509; -. DR Orphanet; 334; Familial atrial fibrillation. DR Orphanet; 90647; Jervell and Lange-Nielsen syndrome. DR Orphanet; 101016; Romano-Ward syndrome. DR PharmGKB; PA211; -. DR VEuPathDB; HostDB:ENSG00000180509.11; -. DR eggNOG; ENOG502SG7D; Eukaryota. DR GeneTree; ENSGT00940000154497; -. DR HOGENOM; CLU_159026_0_0_1; -. DR InParanoid; P15382; -. DR OMA; ESCRACY; -. DR OrthoDB; 1452030at2759; -. DR PhylomeDB; P15382; -. DR TreeFam; TF335976; -. DR PathwayCommons; P15382; -. DR Reactome; R-HSA-5576890; Phase 3 - rapid repolarisation. DR Reactome; R-HSA-5576893; Phase 2 - plateau phase. DR SIGNOR; P15382; -. DR BioGRID-ORCS; 3753; 7 hits in 983 CRISPR screens. DR ChiTaRS; KCNE1; human. DR EvolutionaryTrace; P15382; -. DR GeneWiki; KCNE1; -. DR GenomeRNAi; 3753; -. DR Pharos; P15382; Tbio. DR PRO; PR:P15382; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P15382; protein. DR Bgee; ENSG00000180509; Expressed in blood and 104 other tissues. DR ExpressionAtlas; P15382; baseline and differential. DR Genevisible; P15382; HS. DR GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005764; C:lysosome; HDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL. DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL. DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB. DR GO; GO:0044325; F:ion channel binding; IBA:GO_Central. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB. DR GO; GO:0031433; F:telethonin binding; IPI:BHF-UCL. DR GO; GO:0061337; P:cardiac conduction; TAS:Reactome. DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL. DR GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL. DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL. DR GO; GO:0086011; P:membrane repolarization during action potential; IDA:BHF-UCL. DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IDA:BHF-UCL. DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IMP:BHF-UCL. DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB. DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:BHF-UCL. DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL. DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:BHF-UCL. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL. DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL. DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:BHF-UCL. DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL. DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc. DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL. DR DisProt; DP00796; -. DR InterPro; IPR000369; K_chnl_KCNE. DR InterPro; IPR005424; K_chnl_volt-dep_bsu_KCNE1. DR PANTHER; PTHR15282; PTHR15282; 1. DR Pfam; PF02060; ISK_Channel; 1. DR PRINTS; PR01604; KCNE1CHANNEL. DR PRINTS; PR00168; KCNECHANNEL. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Deafness; Disease variant; Glycoprotein; KW Ion channel; Ion transport; Long QT syndrome; Membrane; Phosphoprotein; KW Potassium; Potassium channel; Potassium transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..129 FT /note="Potassium voltage-gated channel subfamily E member FT 1" FT /id="PRO_0000144278" FT TRANSMEM 44..66 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 67..129 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 109..129 FT /note="interaction with KCNQ1 C-terminus" FT /evidence="ECO:0000269|PubMed:25037568" FT SITE 19 FT /note="Interacts with the scolopendra toxin SSD609" FT /evidence="ECO:0000269|PubMed:26307551" FT MOD_RES 102 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250" FT CARBOHYD 5 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21669976, FT ECO:0000269|PubMed:21676880" FT CARBOHYD 7 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:21669976" FT CARBOHYD 26 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21676880" FT VARIANT 7 FT /note="T -> I (in JLNS2; impairs glycosylation at N-5; FT dbSNP:rs28933384)" FT /evidence="ECO:0000269|PubMed:21676880, FT ECO:0000269|PubMed:9354783" FT /id="VAR_008897" FT VARIANT 8 FT /note="A -> V (in LQT5; unknown pathological significance; FT dbSNP:rs199473348)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074908" FT VARIANT 10 FT /note="T -> M (in LQT5; unknown pathological significance; FT dbSNP:rs144917638)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074909" FT VARIANT 28 FT /note="S -> L (in LQT5; unknown pathological significance; FT dbSNP:rs199473350)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074910" FT VARIANT 32 FT /note="R -> H (in LQT5; unknown pathological significance; FT dbSNP:rs17857111)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:19716085" FT /id="VAR_009906" FT VARIANT 36 FT /note="R -> H (in LQT5; unknown pathological significance; FT dbSNP:rs199473351)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074911" FT VARIANT 38 FT /note="S -> G (in dbSNP:rs1805127)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16823764, ECO:0000269|PubMed:7828904" FT /id="VAR_001558" FT VARIANT 47 FT /note="V -> F (in JLNS2; dbSNP:rs199473353)" FT /evidence="ECO:0000269|PubMed:10400998" FT /id="VAR_008898" FT VARIANT 51 FT /note="L -> H (in JLNS2)" FT /evidence="ECO:0000269|PubMed:10400998" FT /id="VAR_008899" FT VARIANT 52 FT /note="G -> A (in dbSNP:rs17173509)" FT /id="VAR_048024" FT VARIANT 53 FT /note="F -> S (in LQT5; unknown pathological significance; FT dbSNP:rs199473355)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074912" FT VARIANT 55 FT /note="G -> S (in LQT5; unknown pathological significance; FT dbSNP:rs199473644)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074913" FT VARIANT 58..59 FT /note="TL -> PP (in JLNS2; dbSNP:rs281865421)" FT /id="VAR_001559" FT VARIANT 58 FT /note="T -> P (in LQT5; unknown pathological significance; FT dbSNP:rs147187721)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074914" FT VARIANT 59 FT /note="L -> P (in LQT5; unknown pathological significance; FT dbSNP:rs141813529)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074915" FT VARIANT 67 FT /note="R -> C (in LQT5; unknown pathological significance; FT dbSNP:rs199473645)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074916" FT VARIANT 67 FT /note="R -> H (in LQT5; unknown pathological significance; FT dbSNP:rs79654911)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074917" FT VARIANT 70 FT /note="K -> M (in LQT5; unknown pathological significance; FT dbSNP:rs199473646)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074918" FT VARIANT 74 FT /note="S -> L (in LQT5; dbSNP:rs74315446)" FT /evidence="ECO:0000269|PubMed:9354802" FT /id="VAR_008900" FT VARIANT 76 FT /note="D -> N (in LQT5 and JLNS2; suppresses KCNQ1 currents FT markedly; dbSNP:rs74315445)" FT /evidence="ECO:0000269|PubMed:10400998, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9354783, FT ECO:0000269|PubMed:9354802, ECO:0000269|PubMed:9445165" FT /id="VAR_008901" FT VARIANT 83 FT /note="E -> K (in LQT5; unknown pathological significance; FT dbSNP:rs199473360)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074919" FT VARIANT 85 FT /note="D -> N (predisposes to acquired LQT5 susceptibility; FT shows a significant difference in current density and FT midpoint potential compared to the wild-type channel; FT dbSNP:rs1805128)" FT /evidence="ECO:0000269|PubMed:15051636, FT ECO:0000269|PubMed:16823764, ECO:0000269|PubMed:8899564" FT /id="VAR_008902" FT VARIANT 87 FT /note="W -> R (in LQT5; dbSNP:rs199473361)" FT /evidence="ECO:0000269|PubMed:10400998" FT /id="VAR_008903" FT VARIANT 98 FT /note="R -> W (in LQT5; dbSNP:rs199473362)" FT /evidence="ECO:0000269|PubMed:10973849" FT /id="VAR_009907" FT VARIANT 109 FT /note="V -> I (in LQT5; mild phenotype; unknown FT pathological significance; no effect on KCNQ1 C-terminus FT interaction; increases cAMP-mediated up-regulation of the FT I(KS) current; no effect on phosphorylation at S27; FT dbSNP:rs77442996)" FT /evidence="ECO:0000269|PubMed:11692163, FT ECO:0000269|PubMed:25037568" FT /id="VAR_012802" FT VARIANT 125 FT /note="T -> M (in LQT5; unknown pathological significance; FT dbSNP:rs142511345)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074920" FT VARIANT 127 FT /note="P -> T (in LQT5; moderately reduces I(KS) current FT density; no change of the voltage dependence of channel FT activation; markedly reduces interaction with KCNQ1 C- FT terminus; no effect on plasma membrane localization; loss FT of cAMP-mediated up-regulation of the I(KS) current; no FT effect on interaction with AKAP9; impairs phosphorylation FT at S-27 during cAMP-dependent stimulation; FT dbSNP:rs199473647)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:25037568" FT /id="VAR_009908" FT MUTAGEN 5 FT /note="N->Q: No measurable effect on assembly with KCNQ1 or FT cell surface expression of the KCNE1/KCNQ1 channel complex, FT and loss of glycosylation at N-5; when associated with T- FT 28." FT /evidence="ECO:0000269|PubMed:21669976" FT MUTAGEN 6 FT /note="T->F: No measurable effect on assembly with KCNQ1 or FT cell surface expression of the KCNE1/KCNQ1 channel complex. FT Loss of glycosylation at T-7." FT /evidence="ECO:0000269|PubMed:21669976" FT MUTAGEN 7 FT /note="T->A: 50% reduction of cell surface expression of FT the KCNE1/KCNQ1 channel complex, and loss of glycosylation FT at N-5 and T-7; when associated with T-28." FT /evidence="ECO:0000269|PubMed:21669976" FT MUTAGEN 15 FT /note="K->D: No change in inhibition of the complex KCNQ1- FT KCNE1 by the scolopendra toxin SSD609." FT /evidence="ECO:0000269|PubMed:26307551" FT MUTAGEN 19 FT /note="E->K: Loss inhibition of the complex KCNQ1-KCNE1 by FT the scolopendra toxin SSD609." FT /evidence="ECO:0000269|PubMed:26307551" FT MUTAGEN 28 FT /note="S->T: No measurable effect on assembly with KCNQ1 or FT cell surface expression of the KCNE1/KCNQ1 channel complex, FT and loss of glycosylation at N-5; when associated with Q-5. FT 50% reduction of cell surface expression of the KCNE1/KCNQ1 FT channel complex, and loss of glycosylation at N-5 and T-7; FT when associated with A-7." FT /evidence="ECO:0000269|PubMed:21669976" FT MUTAGEN 32 FT /note="R->D: Increase in inhibition of the complex KCNQ1- FT KCNE1 by the scolopendra toxin SSD609." FT /evidence="ECO:0000269|PubMed:26307551" FT MUTAGEN 69 FT /note="K->H: Lowers current 2-fold and leads to faster FT deactivation of KCNQ1/KCNE1 channel." FT /evidence="ECO:0000269|PubMed:11874988" FT MUTAGEN 109..129 FT /note="Missing: Totally suppressed interaction with KCNQ1 FT C-terminus." FT /evidence="ECO:0000269|PubMed:25037568" FT HELIX 4..9 FT /evidence="ECO:0007744|PDB:2K21" FT HELIX 13..22 FT /evidence="ECO:0007744|PDB:2K21" FT HELIX 30..32 FT /evidence="ECO:0007744|PDB:2K21" FT HELIX 46..71 FT /evidence="ECO:0007744|PDB:2K21" FT TURN 77..81 FT /evidence="ECO:0007744|PDB:2K21" FT TURN 84..86 FT /evidence="ECO:0007744|PDB:2K21" FT HELIX 92..105 FT /evidence="ECO:0007744|PDB:2K21" FT STRAND 114..116 FT /evidence="ECO:0007744|PDB:2K21" SQ SEQUENCE 129 AA; 14675 MW; 5442D70929D4E87E CRC64; MILSNTTAVT PFLTKLWQET VQQGGNMSGL ARRSPRSSDG KLEALYVLMV LGFFGFFTLG IMLSYIRSKK LEHSNDPFNV YIESDAWQEK DKAYVQARVL ESYRSCYVVE NHLAIEQPNT HLPETKPSP //