ID KCNQ1_HUMAN Reviewed; 676 AA. AC P51787; O00347; O60607; O94787; Q14D14; Q7Z6G9; Q92960; Q9UMN8; Q9UMN9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 3. DT 27-MAR-2024, entry version 234. DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 1 {ECO:0000305}; DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000305|PubMed:9312006}; DE AltName: Full=KQT-like 1 {ECO:0000305}; DE AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000305|PubMed:20533308}; GN Name=KCNQ1 {ECO:0000312|HGNC:HGNC:6294}; GN Synonyms=KCNA8 {ECO:0000312|HGNC:HGNC:6294}, KCNA9 GN {ECO:0000312|HGNC:HGNC:6294}, KVLQT1 {ECO:0000303|PubMed:9312006}; 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 1), FUNCTION, AND CHARACTERIZATION OF RP VARIANT LQT1 CYS-555. RC TISSUE=Kidney; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION (ISOFORM 2). RC TISSUE=Heart; RX PubMed=9305853; DOI=10.1074/jbc.272.39.24109; RA Jiang M., Tseng-Crank J., Tseng G.-N.; RT "Suppression of slow delayed rectifier current by a truncated isoform of RT KvLQT1 cloned from normal human heart."; RL J. Biol. Chem. 272:24109-24112(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANTS LQT1 RP ASN-242; HIS-250; SER-314 AND MET-587, AND VARIANT SER-643. RX PubMed=9799083; DOI=10.1007/s004390050819; RA Itoh T., Tanaka T., Nagai R., Kikuchi K., Ogawa S., Okada S., Yamagata S., RA Yano K., Yazaki Y., Nakamura Y.; RT "Genomic organization and mutational analysis of KVLQT1, a gene responsible RT for familial long QT syndrome."; RL Hum. Genet. 103:290-294(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND VARIANTS LQT1 RP MET-587 AND HIS-591. RX PubMed=10024302; DOI=10.1161/01.res.84.3.290; RA Neyroud N., Richard P., Vignier N., Donger C., Denjoy I., Demay L., RA Shkolnikova M., Pesce R., Chevalier P., Hainque B., Coumel P., Schwartz K., RA Guicheney P.; RT "Genomic organization of the KCNQ1 K+ channel gene and identification of C- RT terminal mutations in the long-QT syndrome."; RL Circ. Res. 84:290-297(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RA Seebohm G.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Heart; 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=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-129, AND FUNCTION. RX PubMed=9108097; DOI=10.1073/pnas.94.8.4017; RA Yang W.-P., Levesque P.C., Little W.A., Conder M.L., Shalaby F.Y., RA Blanar M.A.; RT "KvLQT1, a voltage-gated potassium channel responsible for human cardiac RT arrhythmias."; RL Proc. Natl. Acad. Sci. U.S.A. 94:4017-4021(1997). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-676, AND FUNCTION. RC TISSUE=Pancreas; RX PubMed=8900283; DOI=10.1038/384080a0; RA Sanguinetti M.C., Curran M.E., Zou A., Shen J., Spector P.S., RA Atkinson D.L., Keating M.T.; RT "Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) RT potassium channel."; RL Nature 384:80-83(1996). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-676. RX PubMed=8528244; DOI=10.1038/ng0196-17; RA Wang Q., Curran M.E., Splawski I., Burn T.C., Millholland J.M., RA Vanraay T.J., Shen J., Timothy K.W., Vincent G.M., de Jager T., RA Schwartz P.J., Towbin J.A., Moss A.J., Atkinson D.L., Landes G.M., RA Connors T.D., Keating M.T.; RT "Positional cloning of a novel potassium channel gene: KVLQT1 mutations RT cause cardiac arrhythmias."; RL Nat. Genet. 12:17-23(1996). RN [13] RP IDENTIFICATION OF C-TERMINAL ASSEMBLY DOMAIN. RX PubMed=10654932; DOI=10.1093/emboj/19.3.332; RA Schmitt N., Schwarz M., Peretz A., Abitbol I., Attali B., Pongs O.; RT "A recessive C-terminal Jervell and Lange-Nielsen mutation of the KCNQ1 RT channel impairs subunit assembly."; RL EMBO J. 19:332-340(2000). RN [14] RP INTERACTION WITH KCNE2, AND FUNCTION. RX PubMed=11101505; DOI=10.1093/emboj/19.23.6326; RA Tinel N., Diochot S., Borsotto M., Lazdunski M., Barhanin J.; RT "KCNE2 confers background current characteristics to the cardiac KCNQ1 RT potassium channel."; RL EMBO J. 19:6326-6330(2000). RN [15] RP FUNCTION. RX PubMed=10713961; DOI=10.1111/j.1469-7793.2000.t01-2-00349.x; RA Selyanko A.A., Hadley J.K., Wood I.C., Abogadie F.C., Jentsch T.J., RA Brown D.A.; RT "Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via RT M1 muscarinic acetylcholine receptors."; RL J. Physiol. (Lond.) 522:349-355(2000). RN [16] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10646604; DOI=10.1038/35003200; RA Schroeder B.C., Waldegger S., Fehr S., Bleich M., Warth R., Greger R., RA Jentsch T.J.; RT "A constitutively open potassium channel formed by KCNQ1 and KCNE3."; RL Nature 403:196-199(2000). RN [17] RP FUNCTION. RX PubMed=12324418; DOI=10.1016/s0006-3495(02)73961-1; RA Angelo K., Jespersen T., Grunnet M., Nielsen M.S., Klaerke D.A., RA Olesen S.P.; RT "KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 RT current."; RL Biophys. J. 83:1997-2006(2002). RN [18] RP INTERACTION WITH AKAP9, PHOSPHORYLATION AT SER-27, CHARACTERIZATION OF RP VARIANT LQT1 ASP-589, AND MUTAGENESIS OF SER-27; LEU-602 AND ILE-609. RX PubMed=11799244; DOI=10.1126/science.1066843; RA Marx S.O., Kurokawa J., Reiken S., Motoike H., D'Armiento J., Marks A.R., RA Kass R.S.; RT "Requirement of a macromolecular signaling complex for beta adrenergic RT receptor modulation of the KCNQ1-KCNE1 potassium channel."; RL Science 295:496-499(2002). RN [19] RP FUNCTION, DOMAIN, INTERACTION WITH KCNE4, AND MUTAGENESIS OF VAL-324; RP LYS-326; THR-327; ILE-328; SER-338 AND PHE-340. RX PubMed=19687231; DOI=10.1085/jgp.200910234; RA Vanoye C.G., Welch R.C., Daniels M.A., Manderfield L.J., Tapper A.R., RA Sanders C.R., George A.L. Jr.; RT "Distinct subdomains of the KCNQ1 S6 segment determine channel modulation RT by different KCNE subunits."; RL J. Gen. Physiol. 134:207-217(2009). RN [20] RP SUBCELLULAR LOCATION, AND INTERACTION WITH KCNE1; KCNE2; KCNE3; KCNE4 AND RP KCNE5. 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 [21] RP SUBCELLULAR LOCATION. RX PubMed=21228319; DOI=10.1152/ajpcell.00390.2010; RA Andersen M.N., Olesen S.P., Rasmussen H.B.; RT "Kv7.1 surface expression is regulated by epithelial cell polarization."; RL Am. J. Physiol. 300:C814-C824(2011). RN [22] RP INTERACTION WITH NEDD4L AND USP2, UBIQUITINATED, DEUBIQUITINATED, AND RP SUBCELLULAR LOCATION. RX PubMed=22024150; DOI=10.1016/j.hrthm.2011.10.026; RA Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P., RA Abriel H., Jespersen T.; RT "Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated downregulation RT of KCNQ1 potassium channels."; RL Heart Rhythm 9:440-448(2012). RN [23] RP INTERACTION WITH AP2M1 AND NEDD4L, AND SUBCELLULAR LOCATION. RX PubMed=23529131; DOI=10.1113/jphysiol.2013.251678; RA Rapetti-Mauss R., O'Mahony F., Sepulveda F.V., Urbach V., Harvey B.J.; RT "Oestrogen promotes KCNQ1 potassium channel endocytosis and postendocytic RT trafficking in colonic epithelium."; RL J. Physiol. (Lond.) 591:2813-2831(2013). RN [24] RP INTERACTION WITH KCNQ5, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=24855057; DOI=10.1161/atvbaha.114.303801; RA Oliveras A., Roura-Ferrer M., Sole L., de la Cruz A., Prieto A., RA Etxebarria A., Manils J., Morales-Cano D., Condom E., Soler C., RA Cogolludo A., Valenzuela C., Villarroel A., Comes N., Felipe A.; RT "Functional assembly of Kv7.1/Kv7.5 channels with emerging properties on RT vascular muscle physiology."; RL Arterioscler. Thromb. Vasc. Biol. 34:1522-1530(2014). RN [25] RP FUNCTION, INTERACTION WITH SLC5A3, AND MUTAGENESIS OF ARG-231. RX PubMed=24595108; DOI=10.1126/scisignal.2005025; RA Abbott G.W., Tai K.K., Neverisky D.L., Hansler A., Hu Z., Roepke T.K., RA Lerner D.J., Chen Q., Liu L., Zupan B., Toth M., Haynes R., Huang X., RA Demirbas D., Buccafusca R., Gross S.S., Kanda V.A., Berry G.T.; RT "KCNQ1, KCNE2, and Na+-coupled solute transporters form reciprocally RT regulating complexes that affect neuronal excitability."; RL Sci. Signal. 7:ra22-ra22(2014). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 574-622, INTERACTION WITH CALM, RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-589; ALA-590 AND ASN-593, RP CHARACTERIZATION OF VARIANT LQT1 ASP-589, AND TETRAMERIZATION. RX PubMed=18165683; DOI=10.1074/jbc.m707541200; RA Wiener R., Haitin Y., Shamgar L., Fernandez-Alonso M.C., Martos A., RA Chomsky-Hecht O., Rivas G., Attali B., Hirsch J.A.; RT "The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit RT assembly and protein interaction."; RL J. Biol. Chem. 283:5815-5830(2008). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 583-611, SUBUNIT, AND COILED-COIL. RX PubMed=19693805; DOI=10.1002/pro.224; RA Xu Q., Minor D.L. Jr.; RT "Crystal structure of a trimeric form of the K(V)7.1 (KCNQ1) A-domain tail RT coiled-coil reveals structural plasticity and context dependent changes in RT a putative coiled-coil trimerization motif."; RL Protein Sci. 18:2100-2114(2009). RN [28] {ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C} RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 352-539 IN COMPLEX WITH CALM AND RP CALCIUM, FUNCTION, INTERACTION WITH CALM, DOMAIN, AND MUTAGENESIS OF RP ILE-375 AND VAL-516. RX PubMed=25441029; DOI=10.1016/j.str.2014.07.016; RA Sachyani D., Dvir M., Strulovich R., Tria G., Tobelaim W., Peretz A., RA Pongs O., Svergun D., Attali B., Hirsch J.A.; RT "Structural basis of a Kv7.1 potassium channel gating module: studies of RT the intracellular c-terminal domain in complex with calmodulin."; RL Structure 22:1582-1594(2014). RN [29] RP CHARACTERIZATION OF VARIANTS LQT1 PRO-178; PHE-273 AND ILE-312. RX PubMed=9323054; DOI=10.1161/01.cir.96.6.1733; RA Shalaby F.Y., Levesque P.C., Yang W.-P., Little W.A., Conder M.L., RA Jenkins-West T., Blanar M.A.; RT "Dominant-negative KvLQT1 mutations underlie the LQT1 form of long QT RT syndrome."; RL Circulation 96:1733-1736(1997). RN [30] RP REVIEW ON VARIANTS. RX PubMed=10704188; RX DOI=10.1002/(sici)1096-8628(19990924)89:3<137::aid-ajmg4>3.3.co;2-3; RA Tranebjaerg L., Bathen J., Tyson J., Bitner-Glindzicz M.; RT "Jervell and Lange-Nielsen syndrome: a Norwegian perspective."; RL Am. J. Med. Genet. 89:137-146(1999). RN [31] RP VARIANTS LQT1 SER-314 AND VAL-341. RX PubMed=8872472; DOI=10.1093/hmg/5.9.1319; RA Russell M.W., Dick M. II, Collins F.S., Brody L.C.; RT "KVLQT1 mutations in three families with familial or sporadic long QT RT syndrome."; RL Hum. Mol. Genet. 5:1319-1324(1996). RN [32] RP VARIANT LQT1 VAL-341. RX PubMed=8818942; DOI=10.1136/jmg.33.7.567; RA de Jager T., Corbett C.H., Badenhorst J.C., Brink P.A., Corfield V.A.; RT "Evidence of a long QT founder gene with varying phenotypic expression in RT South African families."; RL J. Med. Genet. 33:567-573(1996). RN [33] RP VARIANTS LQT1 MET-254 AND MET-417. RA Wedekind H., Schulze-Bahr E., Lange S., Rubie C., Haverkamp W., Hoerdt M., RA Borggrefe M., Assmann G., Breithardt G., Funke H.; RT "A severe form of long-QT syndrome caused by KVLQT1 mutations located in RT cis (Abstract #2051)."; RL Am. J. Hum. Genet. Suppl. 61:A350-A350(1997). RN [34] RP VARIANTS LQT1 THR-178; MET-313; ARG-325 AND PRO-366. RX PubMed=9024139; DOI=10.1161/01.cir.95.3.565; RA Tanaka T., Nagai R., Tomoike H., Takata S., Yano K., Yabuta K., Haneda N., RA Nakano O., Shibata A., Sawayama T., Kasai H., Yazaki Y., Nakamura Y.; RT "Four novel KVLQT1 and four novel HERG mutations in familial long-QT RT syndrome."; RL Circulation 95:565-567(1997). RN [35] RP VARIANTS LQT1 ARG-168; CYS-174; GLN-190; MET-254; LYS-261; ASP-269; RP ARG-309; SER-314; SER-315; ALA-320; ARG-325; VAL-341; PHE-342; VAL-344; RP THR-371 AND CYS-555. RX PubMed=9386136; DOI=10.1161/01.cir.96.9.2778; RA Donger C., Denjoy I., Berthet M., Neyroud N., Cruaud C., Bennaceur M., RA Chivoret G., Schwartz K., Coumel P., Guicheney P.; RT "KVLQT1 C-terminal missense mutation causes a forme fruste long-QT RT syndrome."; RL Circulation 96:2778-2781(1997). RN [36] RP VARIANT LQT1 ARG-216. RX PubMed=9272155; DOI=10.1007/s004390050516; RA van den Berg M.H., Wilde A.A.M., Robles de Medina E.O., Meyer H., RA Geelen J.L.M.C., Jongbloed R.J.E., Wellens H.J., Geraedts J.P.M.; RT "The long QT syndrome: a novel missense mutation in the S6 region of the RT KVLQT1 gene."; RL Hum. Genet. 100:356-361(1997). RN [37] RP VARIANT LQT1 ASN-317. RX PubMed=9302275; DOI=10.1093/hmg/6.11.1943; RA Wollnik B., Schroeder B.C., Kubisch C., Esperer H.D., Wieacker P., RA Jentsch T.J.; RT "Pathophysiological mechanisms of dominant and recessive KVLQT1 K+ channel RT mutations found in inherited cardiac arrhythmias."; RL Hum. Mol. Genet. 6:1943-1949(1997). RN [38] RP VARIANT LQT1 VAL-341. RX PubMed=9570196; DOI=10.1161/01.cir.97.13.1264; RA Li H., Chen Q., Moss A.J., Robinson J.L., Goytia V., Perry J.C., RA Vincent G.M., Priori S.G., Lehmann M.H., Denfield S.W., Duff D., Kaine S., RA Shimizu W., Schwartz P.J., Wang Q., Towbin J.A.; RT "New mutations in the KVLQT1 potassium channel that cause long-QT RT syndrome."; RL Circulation 97:1264-1269(1998). RN [39] RP VARIANT LQT1 THR-300. RX PubMed=9641694; DOI=10.1161/01.cir.97.24.2420; RA Priori S.G., Schwartz P.J., Napolitano C., Bianchi L., Dennis A.T., RA de Fusco M., Brown A.M., Casari G.; RT "A recessive variant of the Romano-Ward Long-QT syndrome?"; RL Circulation 97:2420-2425(1998). RN [40] RP VARIANT JLNS1 SER-305. RX PubMed=9781056; DOI=10.1038/sj.ejhg.5200165; RA Neyroud N., Denjoy I., Donger C., Gary F., Villain E., Leenhardt A., RA Benali K., Schwartz K., Coumel P., Guicheney P.; RT "Heterozygous mutation in the pore of potassium channel gene KvLQT1 causes RT an apparently normal phenotype in long QT syndrome."; RL Eur. J. Hum. Genet. 6:129-133(1998). RN [41] RP VARIANTS LQT1 ARG-168; SER-314; CYS-315; ASN-318; PRO-353 AND TRP-366. RX PubMed=9693036; DOI=10.1006/geno.1998.5361; RA Splawski I., Shen J., Timothy K.W., Vincent G.M., Lehmann M.H., RA Keating M.T.; RT "Genomic structure of three long QT syndrome genes: KVLQT1, HERG, and RT KCNE1."; RL Genomics 51:86-97(1998). RN [42] RP VARIANTS LQT1 ILE-311 AND ASN-317. RX PubMed=9482580; RX DOI=10.1002/(sici)1098-1004(1998)11:2<158::aid-humu9>3.0.co;2-f; RA Saarinen K., Swan H., Kainulainen K., Toivonen L., Viitasalo M., RA Kontula K.; RT "Molecular genetics of the long QT syndrome: two novel mutations of the RT KVLQT1 gene and phenotypic expression of the mutant gene in a large RT kindred."; RL Hum. Mutat. 11:158-165(1998). RN [43] RP VARIANT LQT1 PHE-339 DEL. RX PubMed=9702906; DOI=10.1203/00006450-199808000-00002; RA Ackerman M.J., Schroeder J.J., Berry R., Schaid D.J., Porter C.-B.J., RA Michels V.V., Thibodeau S.N.; RT "A novel mutation in KVLQT1 is the molecular basis of inherited long QT RT syndrome in a near-drowning patient's family."; RL Pediatr. Res. 44:148-153(1998). RN [44] RP VARIANT JLNS1 HIS-243. RX PubMed=10090886; DOI=10.1086/302346; RA Mohammad-Panah R., Demolombe S., Neyroud N., Guicheney P., Kyndt F., RA van den Hoff M., Baro I., Escande D.; RT "Mutations in a dominant-negative isoform correlate with phenotype in RT inherited cardiac arrhythmias."; RL Am. J. Hum. Genet. 64:1015-1023(1999). RN [45] RP VARIANT LQT1 HIS-174. RX PubMed=10367071; RA Denjoy I., Lupoglazoff J.M., Donger C., Berthet M., Richard P., Neyroud N., RA Villain E., Lucet V., Coumel P., Guicheney P.; RT "Congenital long QT syndrome. The value of genetics in prognostic RT evaluation."; RL Arch. Mal. Coeur Vaiss. 92:557-563(1999). RN [46] RP VARIANTS LQT1 LEU-225; CYS-281 AND CYS-315. RX PubMed=9927399; DOI=10.1161/01.cir.99.4.529; RA Priori S.G., Napolitano C., Schwartz P.J.; RT "Low penetrance in the long-QT syndrome: clinical impact."; RL Circulation 99:529-533(1999). RN [47] RP VARIANT LQT1 THR-525. RX PubMed=10482963; DOI=10.1038/sj.ejhg.5200323; RA Larsen L.A., Fosdal I., Andersen P.S., Kanters J.K., Vuust J., Wettrell G., RA Christiansen M.; RT "Recessive Romano-Ward syndrome associated with compound heterozygosity for RT two mutations in the KVLQT1 gene."; RL Eur. J. Hum. Genet. 7:724-728(1999). RN [48] RP VARIANTS LQT1 SER-184; ARG-189; SER-314; SER-315; ARG-345; PRO-373 AND RP ARG-392. RX PubMed=10220144; RX DOI=10.1002/(sici)1098-1004(1999)13:4<301::aid-humu7>3.0.co;2-v; RA Jongbloed R.J.E., Wilde A.A.M., Geelen J.L.M.C., Doevendans P., Schaap C., RA van Langen I., van Tintelen J.P., Cobben J.M., Beaufort-Krol G.C.M., RA Geraedts J.P.M., Smeets H.J.M.; RT "Novel KCNQ1 and HERG missense mutations in Dutch long-QT families."; RL Hum. Mutat. 13:301-310(1999). RN [49] RP VARIANT LQT1 CYS-157. RX PubMed=10220146; RX DOI=10.1002/(sici)1098-1004(1999)13:4<318::aid-humu9>3.0.co;2-f; RA Larsen L.A., Christiansen M., Vuust J., Andersen P.S.; RT "High-throughput single-strand conformation polymorphism analysis by RT automated capillary electrophoresis: robust multiplex analysis and pattern- RT based identification of allelic variants."; RL Hum. Mutat. 13:318-327(1999). RN [50] RP CHARACTERIZATION OF VARIANTS LQT1 CYS-243; ARG-248 AND LYS-261. RX PubMed=10409658; DOI=10.1074/jbc.274.30.21063; RA Franqueza L., Lin M., Shen J., Keating M.T., Sanguinetti M.C.; RT "Long QT syndrome-associated mutations in the S4-S5 linker of KvLQT1 RT potassium channels modify gating and interaction with minK subunits."; RL J. Biol. Chem. 274:21063-21070(1999). RN [51] RP ERRATUM OF PUBMED:10409658. RA Franqueza L., Lin M., Shen J., Keating M.T., Sanguinetti M.C.; RL J. Biol. Chem. 274:25188-25188(1999). RN [52] RP VARIANTS LQT1 GLN-190; TRP-533 AND TRP-539, VARIANT JLNS1 HIS-243, RP CHARACTERIZATION OF VARIANTS LQT1 GLN-190; TRP-533 AND TRP-539, AND RP CHARACTERIZATION OF VARIANT JLNS1 HIS-243. RX PubMed=10728423; DOI=10.1016/s0008-6363(99)00411-3; RA Chouabe C., Neyroud N., Richard P., Denjoy I., Hainque B., Romey G., RA Drici M.-D., Guicheney P., Barhanin J.; RT "Novel mutations in KvLQT1 that affect Iks activation through interactions RT with Isk."; RL Cardiovasc. Res. 45:971-980(2000). RN [53] RP VARIANTS LQT1 CYS-111; LYS-160; ARG-168; HIS-174; SER-179; SER-184; RP PRO-194; LEU-225; CYS-243; ARG-248; MET-254; PRO-266; ASP-269; PHE-273; RP ILE-310; ILE-312; ARG-325; GLU-341; VAL-341; TRP-349; GLN-366; ILE-391; RP ARG-448; PHE-566; CYS-583 AND GLN-594. 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 [54] RP VARIANTS LQT1 PRO-191; SER-275; LEU-277 AND VAL-306. RX PubMed=12442276; DOI=10.1002/humu.9085; RA Liu W., Yang J., Hu D., Kang C., Li C., Zhang S., Li P., Chen Z., Qin X., RA Ying K., Li Y., Li Y., Li Z., Cheng X., Li L., Qi Y., Chen S., Wang Q.; RT "KCNQ1 and KCNH2 mutations associated with long QT syndrome in a Chinese RT population."; RL Hum. Mutat. 20:475-476(2002). RN [55] RP VARIANT ATFB3 GLY-140. RX PubMed=12522251; DOI=10.1126/science.1077771; RA Chen Y.-H., Xu S.-J., Bendahhou S., Wang X.-L., Wang Y., Xu W.-Y., RA Jin H.-W., Sun H., Su X.-Y., Zhuang Q.-N., Yang Y.-Q., Li Y.-B., Liu Y., RA Xu H.-J., Li X.-F., Ma N., Mou C.-P., Chen Z., Barhanin J., Huang W.; RT "KCNQ1 gain-of-function mutation in familial atrial fibrillation."; RL Science 299:251-254(2003). RN [56] RP VARIANT SQT2 LEU-307, AND CHARACTERIZATION OF VARIANT SQT2 LEU-307. RX PubMed=15159330; DOI=10.1161/01.cir.0000130409.72142.fe; RA Bellocq C., van Ginneken A.C.G., Bezzina C.R., Alders M., Escande D., RA Mannens M.M.A.M., Baro I., Wilde A.A.M.; RT "Mutation in the KCNQ1 gene leading to the short QT-interval syndrome."; RL Circulation 109:2394-2397(2004). RN [57] RP VARIANTS LQT1 71-ALA--PRO-73 DEL; THR-73; GLY-115; TYR-122; ILE-133; RP PHE-136; LYS-160; ARG-168; CYS-174; GLN-190; PHE-204; LEU-225; ASN-235; RP ASN-242; CYS-243; MET-254; 254-VAL--PHE-256 DEL; CYS-259; LEU-259; ASP-261; RP PRO-266; SER-269; ASP-269; PHE-273; ARG-273; SER-276 DEL; LEU-277; HIS-278; RP LYS-290; ASP-292; CYS-293; VAL-302; ARG-304; SER-305; ILE-312; SER-314; RP ARG-314; ASP-314; CYS-315; ARG-316; ALA-322; PHE-339 DEL; VAL-341; SER-343; RP GLU-344; VAL-344; GLU-345; TRP-349; PRO-353; ARG-362; TRP-366; HIS-374; RP SER-380; TYR-389; TRP-452; GLY-524; GLU-526; TRP-539; LEU-546; CYS-555; RP HIS-555; TYR-566; SER-567; ARG-568; MET-587; THR-590; HIS-591; GLN-594; RP MET-619 AND SER-626. RX PubMed=15840476; DOI=10.1016/j.hrthm.2005.01.020; RA Tester D.J., Will M.L., Haglund C.M., Ackerman M.J.; RT "Compendium of cardiac channel mutations in 541 consecutive unrelated RT patients referred for long QT syndrome genetic testing."; RL Heart Rhythm 2:507-517(2005). RN [58] RP VARIANTS LQT1 THR-46; PHE-137; LYS-146; ASP-173; PRO-174; TRP-190; PRO-192; RP HIS-202; MET-204; PHE-209; MET-215; HIS-231; PRO-239; LEU-254; ARG-258; RP ASN-258; VAL-262; ASP-272; TRP-277; GLU-280; GLU-287; THR-302; ASP-308; RP GLU-316; MET-322; ARG-343; LEU-343; PRO-349; ARG-350; SER-351; THR-360; RP ASP-372; MET-393; GLY-518; PRO-518; ASP-548; ALA-554; THR-567; LEU-573; RP HIS-583 AND ASP-586. 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 [59] RP VARIANTS LQT1 CYS-231; PRO-243; CYS-259; HIS-259; PHE-273; SER-314; RP GLU-316; VAL-341; VAL-344 AND SER-626. RX PubMed=16922724; DOI=10.1111/j.1399-0004.2006.00671.x; RA Millat G., Chevalier P., Restier-Miron L., Da Costa A., Bouvagnet P., RA Kugener B., Fayol L., Gonzalez Armengod C., Oddou B., Chanavat V., RA Froidefond E., Perraudin R., Rousson R., Rodriguez-Lafrasse C.; RT "Spectrum of pathogenic mutations and associated polymorphisms in a cohort RT of 44 unrelated patients with long QT syndrome."; RL Clin. Genet. 70:214-227(2006). RN [60] RP VARIANT JLNS1 MET-322, AND VARIANT LQT1 MET-322. RX PubMed=18400097; DOI=10.1186/1471-2350-9-24; RA Zhang S., Yin K., Ren X., Wang P., Zhang S., Cheng L., Yang J., Liu J.Y., RA Liu M., Wang Q.K.; RT "Identification of a novel KCNQ1 mutation associated with both Jervell and RT Lange-Nielsen and Romano-Ward forms of long QT syndrome in a Chinese RT family."; RL BMC Med. Genet. 9:24-24(2008). RN [61] RP VARIANT JLNS1 PHE-248, AND CHARACTERIZATION OF VARIANT JLNS1 PHE-248. RX PubMed=18441444; DOI=10.1253/circj.72.687; RA Ohno S., Kubota T., Yoshida H., Tsuji K., Makiyama T., Yamada S., Kuga K., RA Yamaguchi I., Kita T., Horie M.; RT "A novel mutation associated with Jervell and Lange-Nielsen syndrome in a RT Japanese family."; RL Circ. J. 72:687-693(2008). RN [62] RP INVOLVEMENT IN T2D. RX PubMed=18711367; DOI=10.1038/ng.207; RA Yasuda K., Miyake K., Horikawa Y., Hara K., Osawa H., Furuta H., Hirota Y., RA Mori H., Jonsson A., Sato Y., Yamagata K., Hinokio Y., Wang H.Y., RA Tanahashi T., Nakamura N., Oka Y., Iwasaki N., Iwamoto Y., Yamada Y., RA Seino Y., Maegawa H., Kashiwagi A., Takeda J., Maeda E., Shin H.D., RA Cho Y.M., Park K.S., Lee H.K., Ng M.C., Ma R.C., So W.Y., Chan J.C., RA Lyssenko V., Tuomi T., Nilsson P., Groop L., Kamatani N., Sekine A., RA Nakamura Y., Yamamoto K., Yoshida T., Tokunaga K., Itakura M., Makino H., RA Nanjo K., Kadowaki T., Kasuga M.; RT "Variants in KCNQ1 are associated with susceptibility to type 2 diabetes RT mellitus."; RL Nat. Genet. 40:1092-1097(2008). RN [63] RP INVOLVEMENT IN T2D. RX PubMed=18711366; DOI=10.1038/ng.208; RA Unoki H., Takahashi A., Kawaguchi T., Hara K., Horikoshi M., Andersen G., RA Ng D.P., Holmkvist J., Borch-Johnsen K., Jorgensen T., Sandbaek A., RA Lauritzen T., Hansen T., Nurbaya S., Tsunoda T., Kubo M., Babazono T., RA Hirose H., Hayashi M., Iwamoto Y., Kashiwagi A., Kaku K., Kawamori R., RA Tai E.S., Pedersen O., Kamatani N., Kadowaki T., Kikkawa R., Nakamura Y., RA Maeda S.; RT "SNPs in KCNQ1 are associated with susceptibility to type 2 diabetes in RT East Asian and European populations."; RL Nat. Genet. 40:1098-1102(2008). RN [64] RP INVOLVEMENT IN T2D. RX PubMed=24390345; DOI=10.1038/nature12828; RG The SIGMA Type 2 Diabetes Consortium; RT "Sequence variants in SLC16A11 are a common risk factor for type 2 diabetes RT in Mexico."; RL Nature 506:97-101(2014). RN [65] RP VARIANTS LQT1 THR-46; ILE-265; SER-296; VAL-302; GLU-316; SER-339; GLY-360; RP TYR-455 AND LEU-546, AND CHARACTERIZATION OF VARIANTS LQT1 THR-46; ILE-265; RP SER-296; VAL-302; GLU-316; SER-339; GLY-360; TYR-455 AND LEU-546. RX PubMed=19808498; DOI=10.1161/circep.109.850149; RA Yang T., Chung S.K., Zhang W., Mullins J.G., McCulley C.H., Crawford J., RA MacCormick J., Eddy C.A., Shelling A.N., French J.K., Yang P., RA Skinner J.R., Roden D.M., Rees M.I.; RT "Biophysical properties of 9 KCNQ1 mutations associated with long-QT RT syndrome."; RL Circ. Arrhythm. Electrophysiol. 2:417-426(2009). RN [66] RP VARIANTS LQT1 VAL-2; SER-7; THR-46; 64-PRO--PRO-70 DEL; PHE-66; THR-73; RP CYS-111; LEU-117; LEU-127; ILE-133; PRO-134; ALA-144; MET-153; MET-162; RP ARG-168; MET-172; CYS-174; HIS-174; THR-178; SER-179; HIS-184; ARG-186; RP GLN-190; LEU-190; TRP-195; VAL-198; ALA-199; MET-204; MET-215; MET-224; RP LEU-225; CYS-231; HIS-231; ASN-235; GLY-241; ASN-242; CYS-243; PRO-250; RP MET-254; CYS-259; LEU-259; VAL-262; PRO-266; SER-268; ASP-269; SER-269; RP ASP-272; PHE-273; VAL-274; LEU-277; PRO-277; GLU-280; CYS-281; PRO-282; RP GLY-283; ASP-292; CYS-293; GLU-302; VAL-302; PRO-303; ARG-305; SER-305; RP ARG-306; ILE-312; CYS-314; SER-314; CYS-315; VAL-316; SER-320; ALA-322; RP MET-322; ARG-325; TYR-339; GLU-341; GLY-341; VAL-341; PHE-342; LEU-343; RP ARG-350; SER-351; ARG-354; MET-360; ARG-362; HIS-365; GLN-366; TRP-366; RP HIS-374; GLY-379; LYS-385; PRO-389; THR-391 INS; TRP-397; ARG-398; GLU-446; RP LEU-448; TRP-451; SER-460; LEU-477; TRP-511; GLN-518; ARG-520; SER-522; RP GLY-524; THR-525; VAL-525; TRP-533; GLN-539; TRP-539; ILE-541; LYS-543; RP LEU-546; ARG-547; CYS-555; HIS-555; SER-555; GLU-557; PHE-566; PRO-566; RP TYR-566; THR-567; ARG-568; GLU-569; LEU-571; MET-587; ASP-589; CYS-591; RP HIS-591; GLN-594; PRO-594; GLU-596 DEL; LYS-596; MET-600; ASN-611; HIS-614 RP DEL; SER-626 AND ARG-635. 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 [67] RP VARIANT LQT1 HIS-320, AND CHARACTERIZATION OF VARIANTS LQT1 ALA-320 AND RP HIS-320. RX PubMed=19540844; DOI=10.1016/j.yjmcc.2009.06.009; RA Thomas D., Khalil M., Alter M., Schweizer P.A., Karle C.A., Wimmer A.B., RA Licka M., Katus H.A., Koenen M., Ulmer H.E., Zehelein J.; RT "Biophysical characterization of KCNQ1 P320 mutations linked to long QT RT syndrome 1."; RL J. Mol. Cell. Cardiol. 48:230-237(2010). RN [68] RP VARIANT LQT1 LEU-277, AND CHARACTERIZATION OF VARIANT LQT1 LEU-277. RX PubMed=21241800; DOI=10.1016/j.bbadis.2011.01.008; RA Aidery P., Kisselbach J., Schweizer P.A., Becker R., Katus H.A., Thomas D.; RT "Biophysical properties of mutant KCNQ1 S277L channels linked to hereditary RT long QT syndrome with phenotypic variability."; RL Biochim. Biophys. Acta 1812:488-494(2011). RN [69] RP VARIANT LQT1 GLU-557, AND CHARACTERIZATION OF VARIANT LQT1 GLU-557. RX PubMed=25139741; DOI=10.1093/cvr/cvu191; RA Spaetjens R.L., Bebarova M., Seyen S.R., Lentink V., Jongbloed R.J., RA Arens Y.H., Heijman J., Volders P.G.; RT "Long-QT mutation p.K557E-Kv7.1: dominant-negative suppression of IKs, but RT preserved cAMP-dependent up-regulation."; RL Cardiovasc. Res. 104:216-225(2014). RN [70] RP VARIANTS LQT1 ASN-235; CYS-315 AND ALA-322, AND CHARACTERIZATION OF VARIANT RP LQT1 ASN-235. RX PubMed=24269949; DOI=10.1016/j.hrthm.2013.11.021; RA Bartos D.C., Giudicessi J.R., Tester D.J., Ackerman M.J., Ohno S., RA Horie M., Gollob M.H., Burgess D.E., Delisle B.P.; RT "A KCNQ1 mutation contributes to the concealed type 1 long QT phenotype by RT limiting the Kv7.1 channel conformational changes associated with protein RT kinase A phosphorylation."; RL Heart Rhythm 11:459-468(2014). RN [71] RP VARIANT LQT1 SER-269, AND CHARACTERIZATION OF VARIANT LQT1 SER-269. RX PubMed=24184248; DOI=10.1016/j.jacc.2013.08.1648; RA Wu J., Naiki N., Ding W.G., Ohno S., Kato K., Zang W.J., Delisle B.P., RA Matsuura H., Horie M.; RT "A molecular mechanism for adrenergic-induced long QT syndrome."; RL J. Am. Coll. Cardiol. 63:819-827(2014). RN [72] RP CHARACTERIZATION OF VARIANTS LQT1 LEU-546; CYS-555; HIS-555; GLU-557 AND RP ASP-589, INTERACTION WITH KCNE1 AND AKAP9, SUBCELLULAR LOCATION, AND RP FUNCTION. 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). RN [73] RP VARIANT LQT1 THR-590, AND CHARACTERIZATION OF VARIANT LQT1 THR-590. RX PubMed=24713462; DOI=10.1016/j.yjmcc.2014.03.019; RA Kinoshita K., Komatsu T., Nishide K., Hata Y., Hisajima N., Takahashi H., RA Kimoto K., Aonuma K., Tsushima E., Tabata T., Yoshida T., Mori H., RA Nishida K., Yamaguchi Y., Ichida F., Fukurotani K., Inoue H., Nishida N.; RT "A590T mutation in KCNQ1 C-terminal helix D decreases IKs channel RT trafficking and function but not Yotiao interaction."; RL J. Mol. Cell. Cardiol. 72:273-280(2014). RN [74] RP CHARACTERIZATION OF VARIANTS LQT1 ASN-242; PRO-243; HIS-250; VAL-306; RP ASN-317; ASP-586 AND MET-619, AND CHARACTERIZATION OF VARIANTS JLNS1 RP PHE-248; ILE-311; MET-322 AND ASP-589. RX PubMed=25705178; DOI=10.3389/fncel.2015.00032; RA Mousavi Nik A., Gharaie S., Jeong Kim H.; RT "Cellular mechanisms of mutations in Kv7.1: auditory functions in Jervell RT and Lange-Nielsen syndrome vs. Romano-Ward syndrome."; RL Front. Cell. Neurosci. 9:32-32(2015). RN [75] RP VARIANT LQT1 ASP-173, AND CHARACTERIZATION OF VARIANT LQT1 ASP-173. RX PubMed=34398675; DOI=10.1161/jaha.121.021236; RA Kasak L., Rull K., Yang T., Roden D.M., Laan M.; RT "Recurrent pregnancy loss and concealed Long-QT syndrome."; RL J. Am. Heart Assoc. 10:e021236-e021236(2021). CC -!- FUNCTION: Potassium channel that plays an important role in a number of CC tissues, including heart, inner ear, stomach and colon CC (PubMed:10646604, PubMed:25441029). Associates with KCNE beta subunits CC that modulates current kinetics (PubMed:9312006, PubMed:9108097, CC PubMed:8900283, PubMed:10646604, PubMed:11101505, PubMed:19687231). CC Induces a voltage-dependent current by rapidly activating and slowly CC deactivating potassium-selective outward current (PubMed:9312006, CC PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505, CC PubMed:25441029). Promotes also a delayed voltage activated potassium CC current showing outward rectification characteristic (By similarity). CC During beta-adrenergic receptor stimulation participates in cardiac CC repolarization by associating with KCNE1 to form the I(Ks) cardiac CC potassium current that increases the amplitude and slows down the CC activation kinetics of outward potassium current I(Ks) (By similarity) CC (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, CC PubMed:11101505). Muscarinic agonist oxotremorine-M strongly suppresses CC KCNQ1/KCNE1 current (PubMed:10713961). When associated with KCNE3, CC forms the potassium channel that is important for cyclic AMP-stimulated CC intestinal secretion of chloride ions (PubMed:10646604). This CC interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the CC reduction of currents (By similarity). During conditions of increased CC substrate load, maintains the driving force for proximal tubular and CC intestinal sodium ions absorption, gastric acid secretion, and cAMP- CC induced jejunal chloride ions secretion (By similarity). Allows the CC provision of potassium ions to the luminal membrane of the secretory CC canaliculus in the resting state as well as during stimulated acid CC secretion (By similarity). When associated with KCNE2, forms a CC heterooligomer complex leading to currents with an apparently CC instantaneous activation, a rapid deactivation process and a linear CC current-voltage relationship and decreases the amplitude of the outward CC current (PubMed:11101505). When associated with KCNE4, inhibits CC voltage-gated potassium channel activity (PubMed:19687231). When CC associated with KCNE5, this complex only conducts current upon strong CC and continued depolarization (PubMed:12324418). Also forms a CC heterotetramer with KCNQ5; has a voltage-gated potassium channel CC activity (PubMed:24855057). Binds with phosphatidylinositol 4,5- CC bisphosphate (PubMed:25037568). KCNQ1-KCNE2 channel associates with CC Na(+)-coupled myo-inositol symporter in the apical membrane of choroid CC plexus epithelium and regulates the myo-inositol gradient between blood CC and cerebrospinal fluid with an impact on neuron excitability. CC {ECO:0000250|UniProtKB:P97414, ECO:0000250|UniProtKB:Q9Z0N7, CC ECO:0000269|PubMed:10646604, ECO:0000269|PubMed:10713961, CC ECO:0000269|PubMed:11101505, ECO:0000269|PubMed:12324418, CC ECO:0000269|PubMed:19687231, ECO:0000269|PubMed:24595108, CC ECO:0000269|PubMed:24855057, ECO:0000269|PubMed:25037568, CC ECO:0000269|PubMed:8900283, ECO:0000269|PubMed:9108097, CC ECO:0000269|PubMed:9312006}. CC -!- FUNCTION: [Isoform 2]: Non-functional alone but modulatory when CC coexpressed with the full-length isoform 1. CC {ECO:0000269|PubMed:9305853}. CC -!- SUBUNIT: Tetramer (PubMed:18165683, PubMed:19693805, PubMed:25441029). CC Heterotetramer with KCNE1; targets to the membrane raft CC (PubMed:25037568, PubMed:19693805, PubMed:20533308). Interacts (via C- CC terminus) with CALM; forms a heterooctameric structure (with 4:4 CC KCNQ1:CALM stoichiometry) in a calcium-independent manner CC (PubMed:18165683, PubMed:25441029). Interacts with AKAP9; targets CC protein kinase A (PKA) catalytic and regulatory subunits and protein CC phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex, allowing PKA-mediated CC phosphorylation and increase of delayed rectifier potassium channel CC activity (PubMed:11799244, PubMed:25037568). Interacts with KCNE2; CC forms a heterooligomer complex that targets to the membrane raft and CC leading to currents with an apparently instantaneous activation, a CC rapid deactivation process and a linear current-voltage relationship CC and decreases the amplitude of the outward current (PubMed:11101505, CC PubMed:20533308). Interacts with AP2M1; mediates estrogen-induced CC internalization via clathrin-coated vesicles (PubMed:23529131). CC Interacts with NEDD4L; promotes internalization and decreases I(Ks) CC currents (PubMed:23529131, PubMed:22024150). Interacts with USP2; CC counteracts the NEDD4L-specific down-regulation of I(Ks) and restore CC plasma membrane localization (PubMed:22024150). Heterotetramer with CC KCNQ5; has a voltage-gated potassium channel activity CC (PubMed:24855057). Interacts with KCNE3; alters membrane raft CC localization (PubMed:20533308). Interacts with KCNE4; impairs KCNQ1 CC localization in lipid rafts and inhibits voltage-gated potassium CC channel activity (PubMed:19687231, PubMed:20533308). Interacts with CC KCNE5; impairs KCNQ1 localization in lipid rafts and only conducts CC current upon strong and continued depolarization (PubMed:20533308, CC PubMed:12324418). Interacts with SLC5A3; forms coregulatory channel- CC transporter complexes that modulate Na(+)-coupled myo-inositol influx CC through the transporter. {ECO:0000269|PubMed:11101505, CC ECO:0000269|PubMed:11799244, ECO:0000269|PubMed:12324418, CC ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:19687231, CC ECO:0000269|PubMed:19693805, ECO:0000269|PubMed:20533308, CC ECO:0000269|PubMed:22024150, ECO:0000269|PubMed:23529131, CC ECO:0000269|PubMed:24595108, ECO:0000269|PubMed:24855057, CC ECO:0000269|PubMed:25037568, ECO:0000269|PubMed:25441029}. CC -!- INTERACTION: CC P51787; P15382: KCNE1; NbExp=4; IntAct=EBI-359667, EBI-7043557; CC P51787-1; P62158: CALM3; NbExp=6; IntAct=EBI-15885881, EBI-397435; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10646604, CC ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:21228319, CC ECO:0000269|PubMed:22024150, ECO:0000269|PubMed:25037568}; Multi-pass CC membrane protein {ECO:0000269|PubMed:18165683}. Cytoplasmic vesicle CC membrane {ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:23529131}. CC Early endosome {ECO:0000269|PubMed:23529131}. Membrane raft CC {ECO:0000269|PubMed:20533308, ECO:0000269|PubMed:24855057}. Endoplasmic CC reticulum {ECO:0000269|PubMed:21228319, ECO:0000269|PubMed:24855057}. CC Basolateral cell membrane {ECO:0000269|PubMed:21228319}. Apical cell CC membrane {ECO:0000250|UniProtKB:P97414}; Multi-pass membrane protein CC {ECO:0000255}. Note=Colocalized with KCNE3 at the plasma membrane CC (PubMed:10646604). Upon 17beta-oestradiol treatment, colocalizes with CC RAB5A at early endosome (PubMed:23529131). Heterotetramer with KCNQ5 is CC highly retained at the endoplasmic reticulum and is localized outside CC of lipid raft microdomains (PubMed:24855057). During the early stages CC of epithelial cell polarization induced by the calcium switch, it is CC removed from the plasma membrane to the endoplasmic reticulum, where it CC is retained, and redistributed to the basolateral cell surface in a CC PI3K-dependent manner at a later stage (PubMed:21228319). Colocalizes CC with SLC5A3 at the apical membrane of choroid plexus epithelium. CC {ECO:0000250|UniProtKB:P97414, ECO:0000269|PubMed:10646604, CC ECO:0000269|PubMed:21228319, ECO:0000269|PubMed:23529131, CC ECO:0000269|PubMed:24855057}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P51787-1; Sequence=Displayed; CC Name=2; Synonyms=TKvLQT1; CC IsoId=P51787-2; Sequence=VSP_000981, VSP_000982; CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart, pancreas, prostate, CC kidney, small intestine and peripheral blood leukocytes. Less abundant CC in placenta, lung, spleen, colon, thymus, testis and ovaries. CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is CC characterized by a series of positively charged amino acids at every CC third position. CC -!- DOMAIN: The coiled-coil domain mediates tetramerization. CC {ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:19693805}. CC -!- DOMAIN: The segment S6 is involved in the inhibition of voltage-gated CC potassium channel activity by KCNE4. {ECO:0000269|PubMed:19687231}. CC -!- DOMAIN: The C-terminal assembly domain promotes self-interactiona; CC allows functional channel. {ECO:0000269|PubMed:10654932}. CC -!- DOMAIN: The C-terminal coiled-coil domain interacts with a single CALM CC molecule via the first two membrane-proximal helical regions, with CALM CC forming a clamp-like structure. Binding of CALM C-terminus to the first CC helical region is calcium-independent but is essential for assembly of CC the structure. Binding of CALM N-terminus to the second helical region CC is calcium-dependent and regulates electrophysiological activity of the CC channel. {ECO:0000269|PubMed:25441029}. CC -!- PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier CC potassium channel activity of the KCNQ1-KCNE1 complex through a CC macromolecular complex that includes PKA, PP1, and the targeting CC protein AKAP9. {ECO:0000269|PubMed:11799244, CC ECO:0000269|PubMed:25037568}. CC -!- PTM: Ubiquitinated by NEDD4L; promotes internalization CC (PubMed:22024150). The ubiquitinylated form is internalized through a CC clathrin-mediated endocytosis by interacting with AP2M1 and is recycled CC back to the cell membrane via RAB4A and RAB11A (PubMed:23529131). CC {ECO:0000269|PubMed:22024150, ECO:0000269|PubMed:23529131}. CC -!- PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific down- CC regulation of I(Ks) and restores the membrane localization. CC {ECO:0000269|PubMed:22024150}. CC -!- DISEASE: Long QT syndrome 1 (LQT1) [MIM:192500]: 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:10024302, ECO:0000269|PubMed:10220144, CC ECO:0000269|PubMed:10220146, ECO:0000269|PubMed:10367071, CC ECO:0000269|PubMed:10409658, ECO:0000269|PubMed:10482963, CC ECO:0000269|PubMed:10728423, ECO:0000269|PubMed:10973849, CC ECO:0000269|PubMed:11799244, ECO:0000269|PubMed:12442276, CC ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944, CC ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:18165683, CC ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:19540844, CC ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:19808498, CC ECO:0000269|PubMed:21241800, ECO:0000269|PubMed:24184248, CC ECO:0000269|PubMed:24269949, ECO:0000269|PubMed:24713462, CC ECO:0000269|PubMed:25037568, ECO:0000269|PubMed:25139741, CC ECO:0000269|PubMed:25705178, ECO:0000269|PubMed:34398675, CC ECO:0000269|PubMed:8528244, ECO:0000269|PubMed:8818942, CC ECO:0000269|PubMed:8872472, ECO:0000269|PubMed:9024139, CC ECO:0000269|PubMed:9272155, ECO:0000269|PubMed:9302275, CC ECO:0000269|PubMed:9312006, ECO:0000269|PubMed:9323054, CC ECO:0000269|PubMed:9386136, ECO:0000269|PubMed:9482580, CC ECO:0000269|PubMed:9570196, ECO:0000269|PubMed:9641694, CC ECO:0000269|PubMed:9693036, ECO:0000269|PubMed:9702906, CC ECO:0000269|PubMed:9799083, ECO:0000269|PubMed:9927399, CC ECO:0000269|Ref.33}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- DISEASE: Jervell and Lange-Nielsen syndrome 1 (JLNS1) [MIM:220400]: 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:10090886, ECO:0000269|PubMed:10728423, CC ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:18441444, CC ECO:0000269|PubMed:25705178, ECO:0000269|PubMed:9781056}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Atrial fibrillation, familial, 3 (ATFB3) [MIM:607554]: An CC autosomal dominant form of atrial fibrillation, a common sustained CC cardiac rhythm disturbance. Atrial fibrillation is characterized by CC disorganized atrial electrical activity and ineffective atrial CC contraction promoting blood stasis in the atria and reduces ventricular CC filling. It can result in palpitations, syncope, thromboembolic stroke, CC and congestive heart failure. {ECO:0000269|PubMed:12522251}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Short QT syndrome 2 (SQT2) [MIM:609621]: An autosomal dominant CC form of short QT syndrome, a heart disorder characterized by idiopathic CC persistently and uniformly short QT interval on ECG in the absence of CC structural heart disease in affected individuals. It can cause syncope CC and sudden death. {ECO:0000269|PubMed:15159330}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial CC disorder of glucose homeostasis caused by a lack of sensitivity to the CC body's own insulin. Affected individuals usually have an obese body CC habitus and manifestations of a metabolic syndrome characterized by CC diabetes, insulin resistance, hypertension and hypertriglyceridemia. CC The disease results in long-term complications that affect the eyes, CC kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:18711366, CC ECO:0000269|PubMed:18711367, ECO:0000269|PubMed:24390345}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. CC -!- MISCELLANEOUS: Mutagenesis experiments were carried out by expressing CC in Xenopus oocytes or COS-7 cells KCNQ1 mutants either individually CC (homomultimers) or in combination with both wild-type KCNQ1 (mut/wt CC homomultimers) and minK (heteromultimers). CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) CC subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC51781.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305}; CC Sequence=BAA34739.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=KvLQT1 entry; CC URL="https://en.wikipedia.org/wiki/KvLQT1"; 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; AF000571; AAC51776.1; -; mRNA. DR EMBL; AF051426; AAC05705.1; -; mRNA. DR EMBL; AB015163; BAA34738.1; -; Genomic_DNA. DR EMBL; AB015163; BAA34739.1; ALT_FRAME; Genomic_DNA. DR EMBL; AJ006345; CAB44649.1; -; Genomic_DNA. DR EMBL; AJ006345; CAB44650.1; -; Genomic_DNA. DR EMBL; AY114213; AAM94040.1; -; mRNA. DR EMBL; AK290618; BAF83307.1; -; mRNA. DR EMBL; AC013791; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC021424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC124055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC124057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP006463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455303; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455304; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455305; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455306; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF459741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471158; EAX02517.1; -; Genomic_DNA. DR EMBL; BC113545; AAI13546.1; -; mRNA. DR EMBL; U86146; AAB53974.1; -; mRNA. DR EMBL; U89364; AAC51781.1; ALT_SEQ; mRNA. DR CCDS; CCDS7736.1; -. [P51787-1] DR RefSeq; NP_000209.2; NM_000218.2. [P51787-1] DR RefSeq; NP_861463.1; NM_181798.1. [P51787-2] DR PDB; 3BJ4; X-ray; 2.00 A; A/B=574-622. DR PDB; 3HFC; X-ray; 2.45 A; A/B/C=583-611. DR PDB; 3HFE; X-ray; 1.70 A; A/B/C=583-611. DR PDB; 4UMO; X-ray; 3.00 A; A/B=352-539. DR PDB; 4V0C; X-ray; 2.86 A; A/B=352-539. DR PDB; 6MIE; NMR; -; A=100-249. DR PDB; 6UZZ; EM; 3.10 A; A/C/E/G=76-620. DR PDB; 6V00; EM; 3.10 A; A/D/G/J=76-620. DR PDB; 6V01; EM; 3.90 A; A/D/G/J=75-620. DR PDB; 7VUO; X-ray; 2.68 A; A=364-424. DR PDB; 7VVD; X-ray; 3.13 A; A/D=364-424. DR PDB; 7VVH; X-ray; 2.30 A; A=364-424. DR PDB; 7XNI; EM; 3.50 A; A/B/D/G=1-676. DR PDB; 7XNK; EM; 2.60 A; A/C/E/G=1-676. DR PDB; 7XNL; EM; 3.10 A; A/C/E/G=1-676. DR PDB; 7XNN; EM; 2.50 A; B/C/E/G=1-676. DR PDB; 8SIK; EM; 2.90 A; A/C/E/G=75-620. DR PDB; 8SIM; EM; 6.20 A; A/C/E/G=75-620. DR PDB; 8SIN; EM; 6.80 A; A/C/E/G=75-620. DR PDBsum; 3BJ4; -. DR PDBsum; 3HFC; -. DR PDBsum; 3HFE; -. DR PDBsum; 4UMO; -. DR PDBsum; 4V0C; -. DR PDBsum; 6MIE; -. DR PDBsum; 6UZZ; -. DR PDBsum; 6V00; -. DR PDBsum; 6V01; -. DR PDBsum; 7VUO; -. DR PDBsum; 7VVD; -. DR PDBsum; 7VVH; -. DR PDBsum; 7XNI; -. DR PDBsum; 7XNK; -. DR PDBsum; 7XNL; -. DR PDBsum; 7XNN; -. DR PDBsum; 8SIK; -. DR PDBsum; 8SIM; -. DR PDBsum; 8SIN; -. DR AlphaFoldDB; P51787; -. DR BMRB; P51787; -. DR EMDB; EMD-20965; -. DR EMDB; EMD-20966; -. DR EMDB; EMD-20967; -. DR EMDB; EMD-40508; -. DR EMDB; EMD-40509; -. DR EMDB; EMD-40510; -. DR SMR; P51787; -. DR BioGRID; 109985; 18. DR ComplexPortal; CPX-3271; KCNQ1-KCNE1 I(Ks) channel complex. DR ComplexPortal; CPX-902; Kv7.1 channel complex. DR CORUM; P51787; -. DR DIP; DIP-27591N; -. DR DIP; DIP-29941N; -. DR IntAct; P51787; 5. DR MINT; P51787; -. DR STRING; 9606.ENSP00000155840; -. DR BindingDB; P51787; -. DR ChEMBL; CHEMBL1866; -. DR DrugBank; DB04957; Azimilide. DR DrugBank; DB01244; Bepridil. DR DrugBank; DB04855; Dronedarone. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB06089; ICA-105665. DR DrugBank; DB11633; Isavuconazole. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01069; Promethazine. DR DrugCentral; P51787; -. DR GuidetoPHARMACOLOGY; 560; -. DR TCDB; 1.A.1.15.6; the voltage-gated ion channel (vic) superfamily. DR GlyCosmos; P51787; 1 site, No reported glycans. DR GlyGen; P51787; 1 site. DR iPTMnet; P51787; -. DR PhosphoSitePlus; P51787; -. DR BioMuta; KCNQ1; -. DR DMDM; 6166005; -. DR EPD; P51787; -. DR jPOST; P51787; -. DR MassIVE; P51787; -. DR PaxDb; 9606-ENSP00000155840; -. DR PeptideAtlas; P51787; -. DR ProteomicsDB; 56383; -. [P51787-1] DR ProteomicsDB; 56384; -. [P51787-2] DR Antibodypedia; 4357; 529 antibodies from 40 providers. DR DNASU; 3784; -. DR Ensembl; ENST00000155840.12; ENSP00000155840.2; ENSG00000053918.19. [P51787-1] DR Ensembl; ENST00000335475.6; ENSP00000334497.5; ENSG00000053918.19. [P51787-2] DR GeneID; 3784; -. DR KEGG; hsa:3784; -. DR MANE-Select; ENST00000155840.12; ENSP00000155840.2; NM_000218.3; NP_000209.2. DR UCSC; uc001lwn.4; human. [P51787-1] DR AGR; HGNC:6294; -. DR CTD; 3784; -. DR DisGeNET; 3784; -. DR GeneCards; KCNQ1; -. DR GeneReviews; KCNQ1; -. DR HGNC; HGNC:6294; KCNQ1. DR HPA; ENSG00000053918; Tissue enhanced (adrenal gland, stomach). DR MalaCards; KCNQ1; -. DR MIM; 125853; phenotype. DR MIM; 192500; phenotype. DR MIM; 220400; phenotype. DR MIM; 607542; gene. DR MIM; 607554; phenotype. DR MIM; 609621; phenotype. DR neXtProt; NX_P51787; -. DR OpenTargets; ENSG00000053918; -. DR Orphanet; 334; Familial atrial fibrillation. DR Orphanet; 51083; Familial short QT syndrome. DR Orphanet; 90647; Jervell and Lange-Nielsen syndrome. DR Orphanet; 101016; Romano-Ward syndrome. DR PharmGKB; PA223; -. DR VEuPathDB; HostDB:ENSG00000053918; -. DR eggNOG; KOG1419; Eukaryota. DR GeneTree; ENSGT00940000161001; -. DR HOGENOM; CLU_011722_8_3_1; -. DR InParanoid; P51787; -. DR OMA; ETKETHH; -. DR OrthoDB; 2911641at2759; -. DR PhylomeDB; P51787; -. DR TreeFam; TF315186; -. DR PathwayCommons; P51787; -. DR Reactome; R-HSA-1296072; Voltage gated Potassium channels. DR Reactome; R-HSA-5576890; Phase 3 - rapid repolarisation. DR Reactome; R-HSA-5576893; Phase 2 - plateau phase. DR SignaLink; P51787; -. DR SIGNOR; P51787; -. DR BioGRID-ORCS; 3784; 13 hits in 1156 CRISPR screens. DR ChiTaRS; KCNQ1; human. DR EvolutionaryTrace; P51787; -. DR GeneWiki; KvLQT1; -. DR GenomeRNAi; 3784; -. DR Pharos; P51787; Tclin. DR PRO; PR:P51787; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P51787; Protein. DR Bgee; ENSG00000053918; Expressed in left adrenal gland cortex and 98 other cell types or tissues. DR ExpressionAtlas; P51787; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:1990794; C:basolateral part of cell; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0097546; C:ciliary base; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005769; C:early endosome; IDA:BHF-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005770; C:late endosome; IDA:BHF-UCL. DR GO; GO:0098576; C:lumenal side of membrane; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; NAS:ComplexPortal. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0034702; C:monoatomic ion channel complex; IPI:UniProtKB. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0030133; C:transport vesicle; IEA:Ensembl. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL. DR GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL. DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB. DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IDA:BHF-UCL. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:BHF-UCL. DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:BHF-UCL. DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB. DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB. DR GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IMP:BHF-UCL. DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; IMP:BHF-UCL. DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:BHF-UCL. DR GO; GO:0071875; P:adrenergic receptor signaling pathway; IEA:Ensembl. DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; IMP:BHF-UCL. DR GO; GO:0060117; P:auditory receptor cell development; IEA:Ensembl. DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL. DR GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL. DR GO; GO:0071872; P:cellular response to epinephrine stimulus; TAS:BHF-UCL. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:BHF-UCL. DR GO; GO:0090102; P:cochlea development; IEA:Ensembl. DR GO; GO:0035934; P:corticosterone secretion; IEA:Ensembl. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl. DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl. DR GO; GO:0001698; P:gastrin-induced gastric acid secretion; IEA:Ensembl. DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB. DR GO; GO:0030644; P:intracellular chloride ion homeostasis; IEA:Ensembl. DR GO; GO:0015705; P:iodide transport; IEA:Ensembl. DR GO; GO:0086011; P:membrane repolarization during action potential; IDA:BHF-UCL. DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL. DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IMP: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:1903817; P:negative regulation of voltage-gated potassium channel activity; IDA:UniProtKB. DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl. DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:BHF-UCL. DR GO; GO:0010460; P:positive regulation of heart rate; IMP: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:0055075; P:potassium ion homeostasis; IEA:Ensembl. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL. DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IMP:BHF-UCL. DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl. DR GO; GO:0060453; P:regulation of gastric acid secretion; ISS:UniProtKB. DR GO; GO:0008016; P:regulation of heart contraction; IC:BHF-UCL. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL. DR GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL. DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL. DR GO; GO:0070293; P:renal absorption; ISS:UniProtKB. DR GO; GO:0070294; P:renal sodium ion absorption; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0007622; P:rhythmic behavior; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc. DR GO; GO:0035176; P:social behavior; IEA:Ensembl. DR GO; GO:0062094; P:stomach development; IEA:Ensembl. DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 6.10.140.1910; -; 2. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ. DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C. DR InterPro; IPR005827; K_chnl_volt-dep_KCQN1. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR47735:SF6; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 1; 1. DR PANTHER; PTHR47735; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF03520; KCNQ_channel; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01460; KCNQ1CHANNEL. DR PRINTS; PR01459; KCNQCHANNEL. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; P51787; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Atrial fibrillation; KW Calmodulin-binding; Cell membrane; Coiled coil; Cytoplasmic vesicle; KW Deafness; Diabetes mellitus; Disease variant; Endoplasmic reticulum; KW Endosome; Glycoprotein; Ion channel; Ion transport; Long QT syndrome; KW Membrane; Phosphoprotein; Potassium; Potassium channel; KW Potassium transport; Reference proteome; Short QT syndrome; Transmembrane; KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel. FT CHAIN 1..676 FT /note="Potassium voltage-gated channel subfamily KQT member FT 1" FT /id="PRO_0000054022" FT TOPO_DOM 1..121 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 122..142 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000255" FT TOPO_DOM 143..147 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 148..168 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000255" FT TOPO_DOM 169..196 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 197..217 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000255" FT TOPO_DOM 218..225 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 226..248 FT /note="Helical; Voltage-sensor; Name=Segment S4" FT /evidence="ECO:0000255" FT TOPO_DOM 249..261 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 262..282 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000255" FT TOPO_DOM 283..299 FT /note="Extracellular" FT /evidence="ECO:0000255" FT INTRAMEM 300..320 FT /note="Pore-forming; Name=Segment H5" FT /evidence="ECO:0000255" FT TOPO_DOM 321..327 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 328..348 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000255" FT TOPO_DOM 349..676 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 62..84 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..382 FT /note="Interaction with CALM" FT /evidence="ECO:0000269|PubMed:25441029" FT REGION 515..529 FT /note="Interaction with CALM; calcium-dependent" FT /evidence="ECO:0000269|PubMed:25441029" FT REGION 535..572 FT /note="Interaction with KCNE1 C-terminus" FT /evidence="ECO:0000269|PubMed:25037568" FT REGION 588..616 FT /note="Interaction with AKAP9" FT /evidence="ECO:0000269|PubMed:11799244" FT REGION 589..620 FT /note="C-terminal assembly domain" FT /evidence="ECO:0000269|PubMed:10654932" FT REGION 620..676 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 585..621 FT /evidence="ECO:0000269|PubMed:19693805" FT MOTIF 312..317 FT /note="Selectivity filter" FT /evidence="ECO:0000250" FT COMPBIAS 62..80 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 27 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:11799244" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97414" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97414" FT CARBOHYD 289 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..127 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9305853" FT /id="VSP_000981" FT VAR_SEQ 128..129 FT /note="AV -> MD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9305853" FT /id="VSP_000982" FT VARIANT 2 FT /note="A -> V (in LQT1; uncertain significance; FT dbSNP:rs199473442)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074927" FT VARIANT 7 FT /note="P -> S (in LQT1; uncertain significance; FT dbSNP:rs199473443)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074928" FT VARIANT 46 FT /note="A -> T (in LQT1; uncertain significance; hardly any FT effect on channel activity, shows fast activation; FT dbSNP:rs199473671)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:19808498" FT /id="VAR_074929" FT VARIANT 64..70 FT /note="Missing (in LQT1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074930" FT VARIANT 66 FT /note="S -> F (in LQT1; uncertain significance; FT dbSNP:rs199473446)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074931" FT VARIANT 71..73 FT /note="Missing (in LQT1)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_009917" FT VARIANT 73 FT /note="P -> T (in LQT1; uncertain significance; FT dbSNP:rs199472676)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068287" FT VARIANT 111 FT /note="Y -> C (in LQT1; uncertain significance; FT dbSNP:rs199472678)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:19716085" FT /id="VAR_009918" FT VARIANT 115 FT /note="E -> G (in LQT1; dbSNP:rs199472679)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068288" FT VARIANT 117 FT /note="P -> L (in LQT1; uncertain significance; FT dbSNP:rs120074191)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074932" FT VARIANT 122 FT /note="C -> Y (in LQT1; dbSNP:rs199472681)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068289" FT VARIANT 127 FT /note="F -> L (in LQT1; uncertain significance; FT dbSNP:rs199472682)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074933" FT VARIANT 133 FT /note="V -> I (in LQT1; dbSNP:rs199473449)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068290" FT VARIANT 134 FT /note="L -> P (in LQT1; uncertain significance; FT dbSNP:rs199472685)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074934" FT VARIANT 136 FT /note="C -> F (in LQT1; dbSNP:rs199472686)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068291" FT VARIANT 137 FT /note="L -> F (in LQT1; uncertain significance; FT dbSNP:rs199473450)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074935" FT VARIANT 140 FT /note="S -> G (in ATFB3; gain of function; FT dbSNP:rs120074192)" FT /evidence="ECO:0000269|PubMed:12522251" FT /id="VAR_015742" FT VARIANT 144 FT /note="T -> A (in LQT1; uncertain significance; FT dbSNP:rs199473451)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074936" FT VARIANT 146 FT /note="E -> K (in LQT1; uncertain significance; FT dbSNP:rs199472688)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074937" FT VARIANT 153 FT /note="T -> M (in LQT1; uncertain significance; FT dbSNP:rs143709408)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074938" FT VARIANT 157 FT /note="F -> C (in LQT1; dbSNP:rs199472690)" FT /evidence="ECO:0000269|PubMed:10220146" FT /id="VAR_008124" FT VARIANT 160 FT /note="E -> K (in LQT1; dbSNP:rs199473453)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476" FT /id="VAR_009919" FT VARIANT 162 FT /note="V -> M (in LQT1; uncertain significance; FT dbSNP:rs199472692)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074939" FT VARIANT 167..168 FT /note="FG -> W (in LQT1)" FT /id="VAR_001515" FT VARIANT 168 FT /note="G -> R (in LQT1; dbSNP:rs179489)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9386136, ECO:0000269|PubMed:9693036" FT /id="VAR_001516" FT VARIANT 172 FT /note="V -> M (in LQT1; uncertain significance; FT dbSNP:rs199472694)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074940" FT VARIANT 173 FT /note="V -> D (in LQT1; affects channel activity; when FT expressed in heterologous system the mutant significantly FT reduces total IKs steady-state and tail currents with a FT positive shift of the voltage dependence of activation; FT dbSNP:rs199472695)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:34398675" FT /id="VAR_074941" FT VARIANT 174 FT /note="R -> C (in LQT1; dbSNP:rs199472696)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9386136" FT /id="VAR_001517" FT VARIANT 174 FT /note="R -> H (in LQT1; dbSNP:rs199472697)" FT /evidence="ECO:0000269|PubMed:10367071, FT ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:19716085" FT /id="VAR_008939" FT VARIANT 174 FT /note="R -> P (in LQT1; uncertain significance; FT dbSNP:rs199472697)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074942" FT VARIANT 178 FT /note="A -> P (in LQT1; loss of channel activity; FT dbSNP:rs120074177)" FT /evidence="ECO:0000269|PubMed:9323054" FT /id="VAR_001518" FT VARIANT 178 FT /note="A -> T (in LQT1; dbSNP:rs120074177)" FT /evidence="ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9024139" FT /id="VAR_009920" FT VARIANT 179 FT /note="G -> S (in LQT1; uncertain significance; FT dbSNP:rs199473394)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:19716085" FT /id="VAR_009921" FT VARIANT 184 FT /note="Y -> H (in LQT1; uncertain significance; FT dbSNP:rs199473661)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074943" FT VARIANT 184 FT /note="Y -> S (in LQT1; dbSNP:rs199473397)" FT /evidence="ECO:0000269|PubMed:10220144, FT ECO:0000269|PubMed:10973849" FT /id="VAR_008125" FT VARIANT 186 FT /note="G -> R (in LQT1; uncertain significance; FT dbSNP:rs199473398)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074944" FT VARIANT 189 FT /note="G -> R (in LQT1; familial sudden death; FT dbSNP:rs104894252)" FT /evidence="ECO:0000269|PubMed:10220144" FT /id="VAR_001519" FT VARIANT 190 FT /note="R -> L (in LQT1; uncertain significance; FT dbSNP:rs120074178)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074945" FT VARIANT 190 FT /note="R -> Q (in LQT1; loss of channel activity; FT dbSNP:rs120074178)" FT /evidence="ECO:0000269|PubMed:10728423, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001520" FT VARIANT 190 FT /note="R -> W (in LQT1; uncertain significance; FT dbSNP:rs199473662)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074946" FT VARIANT 191 FT /note="L -> P (in LQT1; dbSNP:rs199473401)" FT /evidence="ECO:0000269|PubMed:12442276" FT /id="VAR_074687" FT VARIANT 192 FT /note="R -> P (in LQT1; uncertain significance; FT dbSNP:rs199472698)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074947" FT VARIANT 194 FT /note="A -> P (in LQT1; uncertain significance; FT dbSNP:rs199472699)" FT /evidence="ECO:0000269|PubMed:10973849" FT /id="VAR_009922" FT VARIANT 195 FT /note="R -> W (in LQT1; uncertain significance; FT dbSNP:rs150172393)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074948" FT VARIANT 198 FT /note="I -> V (in LQT1; uncertain significance; FT dbSNP:rs199472700)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074949" FT VARIANT 199 FT /note="S -> A (in LQT1; uncertain significance; FT dbSNP:rs199472701)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074950" FT VARIANT 202 FT /note="D -> H (in LQT1; uncertain significance; FT dbSNP:rs199472702)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074951" FT VARIANT 204 FT /note="I -> F (in LQT1; dbSNP:rs199472703)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068292" FT VARIANT 204 FT /note="I -> M (in LQT1; dbSNP:rs199473455)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074952" FT VARIANT 209 FT /note="S -> F (in LQT1; uncertain significance; FT dbSNP:rs199472704)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074953" FT VARIANT 215 FT /note="V -> M (in LQT1; dbSNP:rs17215479)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074954" FT VARIANT 216 FT /note="G -> R (in LQT1)" FT /evidence="ECO:0000269|PubMed:9272155" FT /id="VAR_001521" FT VARIANT 224 FT /note="T -> M (in LQT1; uncertain significance; FT dbSNP:rs199472706)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074955" FT VARIANT 225 FT /note="S -> L (in LQT1; dbSNP:rs199473456)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9927399" FT /id="VAR_009923" FT VARIANT 231 FT /note="R -> C (in LQT1; dbSNP:rs199473457)" FT /evidence="ECO:0000269|PubMed:16922724, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074956" FT VARIANT 231 FT /note="R -> H (in LQT1; dbSNP:rs199472709)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074957" FT VARIANT 235 FT /note="I -> N (in LQT1; decreases delayed rectifier FT potassium current Iks; prevents the up-regulation of Iks FT through PKA activation; dbSNP:rs199472710)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:24269949" FT /id="VAR_068293" FT VARIANT 239 FT /note="L -> P (in LQT1; uncertain significance; FT dbSNP:rs199473458)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074958" FT VARIANT 241 FT /note="V -> G (in LQT1; uncertain significance; FT dbSNP:rs199472711)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074959" FT VARIANT 242 FT /note="D -> N (in LQT1; decreases outward potassium FT current; decreases plasma membrane localization; FT dbSNP:rs199472712)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:25705178, FT ECO:0000269|PubMed:9799083" FT /id="VAR_008940" FT VARIANT 243 FT /note="R -> C (in LQT1; slower rate of activation and FT voltage dependence of activation-inactivation shifted to FT more positive potentials (homomultimers); channels FT non-functional (heteromultimers); dbSNP:rs199472713)" FT /evidence="ECO:0000269|PubMed:10409658, FT ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_010933" FT VARIANT 243 FT /note="R -> H (in JLNS1; minor changes of wt current FT (homomultimers); positive voltage shift of the channel FT activation (heteromultimers); dbSNP:rs120074196)" FT /evidence="ECO:0000269|PubMed:10090886, FT ECO:0000269|PubMed:10728423" FT /id="VAR_008941" FT VARIANT 243 FT /note="R -> P (in LQT1; complete loss of outward potassium FT current; enhances outward potassium current when FT co-transfected with wild type; decreases plasma membrane FT localization; dbSNP:rs120074196)" FT /evidence="ECO:0000269|PubMed:16922724, FT ECO:0000269|PubMed:25705178" FT /id="VAR_074688" FT VARIANT 248 FT /note="W -> F (in JLNS1; does not affect plasma membrane FT localization; complete loss of outward currents; enhances FT outward currents when coexpressed with wild type at FT equimolar ratio; requires 2 nucleotide substitutions; FT dbSNP:rs397508123)" FT /evidence="ECO:0000269|PubMed:18441444, FT ECO:0000269|PubMed:25705178" FT /id="VAR_074689" FT VARIANT 248 FT /note="W -> R (in LQT1; slower rate of activation and FT voltage dependence of activation-inactivation shifted to FT more positive potentials (homomultimers); channels FT non-functional (heteromultimers); dbSNP:rs199473459)" FT /evidence="ECO:0000269|PubMed:10409658, FT ECO:0000269|PubMed:10973849" FT /id="VAR_008942" FT VARIANT 250 FT /note="L -> H (in LQT1; complete loss of outward potassium FT current; enhances outward potassium current when FT co-transfected with wild type; decreases plasma membrane FT localization; dbSNP:rs199472715)" FT /evidence="ECO:0000269|PubMed:25705178, FT ECO:0000269|PubMed:9799083" FT /id="VAR_008943" FT VARIANT 250 FT /note="L -> P (in LQT1; uncertain significance; FT dbSNP:rs199472715)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074960" FT VARIANT 254..256 FT /note="Missing (in LQT1)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068294" FT VARIANT 254 FT /note="V -> L (in LQT1; uncertain significance; FT dbSNP:rs120074179)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074961" FT VARIANT 254 FT /note="V -> M (in LQT1; associated in cis with M-417 in a FT patient; dbSNP:rs120074179)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9386136, ECO:0000269|Ref.33" FT /id="VAR_001522" FT VARIANT 258 FT /note="H -> N (in LQT1; uncertain significance; FT dbSNP:rs199472717)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074962" FT VARIANT 258 FT /note="H -> R (in LQT1; uncertain significance; FT dbSNP:rs199472718)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074963" FT VARIANT 259 FT /note="R -> C (in LQT1; dbSNP:rs199472719)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:19716085" FT /id="VAR_068295" FT VARIANT 259 FT /note="R -> H (in LQT1; uncertain significance; FT dbSNP:rs199472720)" FT /evidence="ECO:0000269|PubMed:16922724" FT /id="VAR_074964" FT VARIANT 259 FT /note="R -> L (in LQT1; dbSNP:rs199472720)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068296" FT VARIANT 261 FT /note="E -> D (in JLNS1; dbSNP:rs199472721)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_008944" FT VARIANT 261 FT /note="E -> K (in LQT1; loss of channel activity and no FT interaction with wt KVLQT1 or MINK subunits; FT dbSNP:rs199472722)" FT /evidence="ECO:0000269|PubMed:10409658, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001523" FT VARIANT 262 FT /note="L -> V (in LQT1; dbSNP:rs199472723)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074965" FT VARIANT 265 FT /note="T -> I (in LQT1; uncertain significance; no effect FT on channel activity; dbSNP:rs199472724)" FT /evidence="ECO:0000269|PubMed:19808498" FT /id="VAR_080331" FT VARIANT 266 FT /note="L -> P (in LQT1; dbSNP:rs199473460)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085" FT /id="VAR_009924" FT VARIANT 268 FT /note="I -> S (in LQT1; uncertain significance; FT dbSNP:rs199472725)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074966" FT VARIANT 269 FT /note="G -> D (in LQT1; dbSNP:rs120074194)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001524" FT VARIANT 269 FT /note="G -> S (in LQT1; decreases IKs amplitude; FT accelerates the IKs deactivation; effect on plasma membrane FT localization; reduces up-regulation of Iks through PKA FT activation; dbSNP:rs120074193)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:24184248" FT /id="VAR_009925" FT VARIANT 272 FT /note="G -> D (in LQT1; dbSNP:rs199472726)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074967" FT VARIANT 273 FT /note="L -> F (in LQT1; functional channel with reduced FT macroscopic conductance (homomultimers); alteration of FT normal KVLQT1 function (mut/wt homomultimers); FT dbSNP:rs120074180)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16922724, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9323054" FT /id="VAR_001525" FT VARIANT 273 FT /note="L -> R (in LQT1; dbSNP:rs199472727)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068297" FT VARIANT 274 FT /note="I -> V (in LQT1; uncertain significance; FT dbSNP:rs199472728)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074968" FT VARIANT 275 FT /note="F -> S (in LQT1; dbSNP:rs199472729)" FT /evidence="ECO:0000269|PubMed:12442276" FT /id="VAR_074690" FT VARIANT 276 FT /note="Missing (in LQT1)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068298" FT VARIANT 277 FT /note="S -> L (in LQT1; loss of function mutation acting in FT a dominant-negative manner; dbSNP:rs199472730)" FT /evidence="ECO:0000269|PubMed:12442276, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:21241800" FT /id="VAR_065777" FT VARIANT 277 FT /note="S -> P (in LQT1; uncertain significance; FT dbSNP:rs199473461)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074969" FT VARIANT 277 FT /note="S -> W (in LQT1; uncertain significance; FT dbSNP:rs199472730)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074970" FT VARIANT 278 FT /note="Y -> H (in LQT1; dbSNP:rs199472731)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068299" FT VARIANT 280 FT /note="V -> E (in LQT1; dbSNP:rs199473462)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074971" FT VARIANT 281 FT /note="Y -> C (in LQT1; dbSNP:rs199472732)" FT /evidence="ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9927399" FT /id="VAR_008945" FT VARIANT 282 FT /note="L -> P (in LQT1; uncertain significance; FT dbSNP:rs199472733)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074972" FT VARIANT 283 FT /note="A -> G (in LQT1; uncertain significance; FT dbSNP:rs199473463)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074973" FT VARIANT 287 FT /note="A -> E (in LQT1; uncertain significance; FT dbSNP:rs199472735)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074974" FT VARIANT 290 FT /note="E -> K (in LQT1; dbSNP:rs199473464)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068300" FT VARIANT 292 FT /note="G -> D (in LQT1; dbSNP:rs199472736)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068301" FT VARIANT 293 FT /note="R -> C (in LQT1; dbSNP:rs199472737)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068302" FT VARIANT 296 FT /note="F -> S (in LQT1; loss of channel activity; FT dbSNP:rs199472738)" FT /evidence="ECO:0000269|PubMed:19808498" FT /id="VAR_080332" FT VARIANT 300 FT /note="A -> T (in LQT1; dbSNP:rs120074187)" FT /evidence="ECO:0000269|PubMed:9641694" FT /id="VAR_001526" FT VARIANT 302 FT /note="A -> E (in LQT1; uncertain significance; FT dbSNP:rs193922365)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074975" FT VARIANT 302 FT /note="A -> T (in LQT1; uncertain significance; FT dbSNP:rs199472739)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074976" FT VARIANT 302 FT /note="A -> V (in LQT1; loss of channel activity; FT dbSNP:rs193922365)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:19808498" FT /id="VAR_068303" FT VARIANT 303 FT /note="L -> P (in LQT1; uncertain significance; FT dbSNP:rs199472740)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074977" FT VARIANT 304 FT /note="W -> R (in LQT1; dbSNP:rs199473466)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068304" FT VARIANT 305 FT /note="W -> R (in LQT1; uncertain significance; FT dbSNP:rs199472741)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074978" FT VARIANT 305 FT /note="W -> S (in JLNS1; dbSNP:rs120074186)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9781056" FT /id="VAR_001527" FT VARIANT 306 FT /note="G -> R (in LQT1; uncertain significance; FT dbSNP:rs120074181)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_001528" FT VARIANT 306 FT /note="G -> V (in LQT1; complete loss of outward potassium FT current; enhances outward potassium current when FT co-transfected with wild type; decreases plasma membrane FT localization; dbSNP:rs199472742)" FT /evidence="ECO:0000269|PubMed:12442276, FT ECO:0000269|PubMed:25705178" FT /id="VAR_074691" FT VARIANT 307 FT /note="V -> L (in SQT2; gain of function; FT dbSNP:rs120074195)" FT /evidence="ECO:0000269|PubMed:15159330" FT /id="VAR_023841" FT VARIANT 308 FT /note="V -> D (in LQT1; uncertain significance; FT dbSNP:rs199473467)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074979" FT VARIANT 309 FT /note="T -> R (in LQT1; dbSNP:rs199472743)" FT /evidence="ECO:0000269|PubMed:9386136" FT /id="VAR_001529" FT VARIANT 310 FT /note="V -> I (in LQT1; dbSNP:rs199472745)" FT /evidence="ECO:0000269|PubMed:10973849" FT /id="VAR_009926" FT VARIANT 311 FT /note="T -> I (in LQT1 and JLNS1; impairs outward potassium FT current; affects plasma membrane localization; FT dbSNP:rs199472746)" FT /evidence="ECO:0000269|PubMed:25705178, FT ECO:0000269|PubMed:9482580" FT /id="VAR_009927" FT VARIANT 312 FT /note="T -> I (in LQT1; loss of channel activity; FT dbSNP:rs120074182)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9323054" FT /id="VAR_001530" FT VARIANT 313 FT /note="I -> M (in LQT1; dbSNP:rs199472747)" FT /evidence="ECO:0000269|PubMed:9024139" FT /id="VAR_001531" FT VARIANT 314 FT /note="G -> C (in LQT1; uncertain significance; FT dbSNP:rs120074184)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074980" FT VARIANT 314 FT /note="G -> D (in LQT1; dbSNP:rs199472748)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068305" FT VARIANT 314 FT /note="G -> R (in LQT1; dbSNP:rs120074184)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068306" FT VARIANT 314 FT /note="G -> S (in LQT1; dbSNP:rs120074184)" FT /evidence="ECO:0000269|PubMed:10220144, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16922724, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:8872472, FT ECO:0000269|PubMed:9386136, ECO:0000269|PubMed:9693036, FT ECO:0000269|PubMed:9799083" FT /id="VAR_001532" FT VARIANT 315 FT /note="Y -> C (in LQT1; dbSNP:rs74462309)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:24269949, FT ECO:0000269|PubMed:9693036, ECO:0000269|PubMed:9927399" FT /id="VAR_008946" FT VARIANT 315 FT /note="Y -> S (in LQT1; dbSNP:rs74462309)" FT /evidence="ECO:0000269|PubMed:10220144, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001533" FT VARIANT 316 FT /note="G -> E (in LQT1; loss of channel activity; FT dbSNP:rs199472749)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:19808498" FT /id="VAR_074981" FT VARIANT 316 FT /note="G -> R (in LQT1; dbSNP:rs104894255)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068307" FT VARIANT 316 FT /note="G -> V (in LQT1; uncertain significance; FT dbSNP:rs199472749)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074982" FT VARIANT 317 FT /note="D -> N (in LQT1; complete loss of outward potassium FT current when expressed alone and even in the presence of FT the wild type at variable ratios; decreases plasma membrane FT localization; dbSNP:rs199472751)" FT /evidence="ECO:0000269|PubMed:25705178, FT ECO:0000269|PubMed:9302275, ECO:0000269|PubMed:9482580" FT /id="VAR_001534" FT VARIANT 318 FT /note="K -> N (in LQT1; dbSNP:rs199472752)" FT /evidence="ECO:0000269|PubMed:9693036" FT /id="VAR_008947" FT VARIANT 320 FT /note="P -> A (in LQT1; loss of function mutation acting in FT a dominant-negative manner; dbSNP:rs199472753)" FT /evidence="ECO:0000269|PubMed:19540844, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001535" FT VARIANT 320 FT /note="P -> H (in LQT1; loss of function mutation acting in FT a dominant-negative manner; dbSNP:rs199473470)" FT /evidence="ECO:0000269|PubMed:19540844" FT /id="VAR_065778" FT VARIANT 320 FT /note="P -> S (in LQT1; uncertain significance; FT dbSNP:rs199472753)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074983" FT VARIANT 322 FT /note="T -> A (in LQT1; dbSNP:rs199472754)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:24269949" FT /id="VAR_068308" FT VARIANT 322 FT /note="T -> M (in JLNS1 and LQT1; impairs outward potassium FT current; affects plasma membrane localization; FT dbSNP:rs199472755)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:25705178" FT /id="VAR_074692" FT VARIANT 325 FT /note="G -> R (in LQT1; dbSNP:rs199472756)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9024139, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001536" FT VARIANT 339 FT /note="F -> S (in LQT1; loss of channel activity; FT dbSNP:rs199472759)" FT /evidence="ECO:0000269|PubMed:19808498" FT /id="VAR_080333" FT VARIANT 339 FT /note="F -> Y (in LQT1; uncertain significance; FT dbSNP:rs199472759)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074984" FT VARIANT 339 FT /note="Missing (in LQT1)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:9702906" FT /id="VAR_001537" FT VARIANT 341 FT /note="A -> E (in LQT1; dbSNP:rs12720459)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:19716085" FT /id="VAR_001538" FT VARIANT 341 FT /note="A -> G (in LQT1; uncertain significance; FT dbSNP:rs12720459)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074985" FT VARIANT 341 FT /note="A -> V (in LQT1; dbSNP:rs12720459)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16922724, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:8818942, FT ECO:0000269|PubMed:8872472, ECO:0000269|PubMed:9386136, FT ECO:0000269|PubMed:9570196" FT /id="VAR_001539" FT VARIANT 342 FT /note="L -> F (in LQT1; dbSNP:rs199472760)" FT /evidence="ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9386136" FT /id="VAR_001540" FT VARIANT 343 FT /note="P -> L (in LQT1; dbSNP:rs199472761)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074986" FT VARIANT 343 FT /note="P -> R (in LQT1; uncertain significance; FT dbSNP:rs199472761)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074987" FT VARIANT 343 FT /note="P -> S (in LQT1; dbSNP:rs199472762)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068309" FT VARIANT 344 FT /note="A -> E (in LQT1; dbSNP:rs199472763)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068310" FT VARIANT 344 FT /note="A -> V (in LQT1; dbSNP:rs199472763)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:9386136" FT /id="VAR_001541" FT VARIANT 345 FT /note="G -> E (in LQT1; dbSNP:rs120074183)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_001542" FT VARIANT 345 FT /note="G -> R (in LQT1; familial sudden death; FT dbSNP:rs199473471)" FT /evidence="ECO:0000269|PubMed:10220144" FT /id="VAR_008126" FT VARIANT 349 FT /note="S -> P (in LQT1; uncertain significance; FT dbSNP:rs199472764)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074988" FT VARIANT 349 FT /note="S -> W (in LQT1; dbSNP:rs199472765)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476" FT /id="VAR_009928" FT VARIANT 350 FT /note="G -> R (in LQT1; dbSNP:rs199472824)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074989" FT VARIANT 351 FT /note="F -> S (in LQT1; dbSNP:rs199473402)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_074990" FT VARIANT 353 FT /note="L -> P (in LQT1; dbSNP:rs199473403)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:9693036" FT /id="VAR_009180" FT VARIANT 354 FT /note="K -> R (in LQT1; uncertain significance; FT dbSNP:rs199473404)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074991" FT VARIANT 360 FT /note="R -> G (in LQT1; loss of channel activity; FT dbSNP:rs199473406)" FT /evidence="ECO:0000269|PubMed:19808498" FT /id="VAR_080334" FT VARIANT 360 FT /note="R -> M (in LQT1; uncertain significance; FT dbSNP:rs199473407)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074992" FT VARIANT 360 FT /note="R -> T (in LQT1; uncertain significance; FT dbSNP:rs199473407)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074993" FT VARIANT 362 FT /note="K -> R (in LQT1; dbSNP:rs12720458)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_048025" FT VARIANT 365 FT /note="N -> H (in LQT1; uncertain significance; FT dbSNP:rs199473409)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074994" FT VARIANT 366 FT /note="R -> P (in LQT1; dbSNP:rs199473410)" FT /evidence="ECO:0000269|PubMed:9024139" FT /id="VAR_001543" FT VARIANT 366 FT /note="R -> Q (in LQT1; dbSNP:rs199473410)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:19716085" FT /id="VAR_009929" FT VARIANT 366 FT /note="R -> W (in LQT1; dbSNP:rs199473411)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:9693036" FT /id="VAR_008948" FT VARIANT 371 FT /note="A -> T (in LQT1; dbSNP:rs199473412)" FT /evidence="ECO:0000269|PubMed:9386136" FT /id="VAR_001544" FT VARIANT 372 FT /note="A -> D (in LQT1; uncertain significance; FT dbSNP:rs199473472)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_074995" FT VARIANT 373 FT /note="S -> P (in LQT1; dbSNP:rs199472766)" FT /evidence="ECO:0000269|PubMed:10220144" FT /id="VAR_008127" FT VARIANT 374 FT /note="L -> H (in LQT1; uncertain significance; FT dbSNP:rs199472767)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068311" FT VARIANT 379 FT /note="W -> G (in LQT1; uncertain significance; FT dbSNP:rs199472768)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074996" FT VARIANT 380 FT /note="R -> S (in LQT1; dbSNP:rs199472771)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068312" FT VARIANT 385 FT /note="E -> K (in LQT1; uncertain significance; FT dbSNP:rs199473473)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074997" FT VARIANT 389 FT /note="S -> P (in LQT1; uncertain significance; FT dbSNP:rs199472772)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074998" FT VARIANT 389 FT /note="S -> Y (in LQT1; dbSNP:rs199472773)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068313" FT VARIANT 391 FT /note="T -> I (in LQT1; dbSNP:rs199473474)" FT /evidence="ECO:0000269|PubMed:10973849" FT /id="VAR_009930" FT VARIANT 391 FT /note="T -> TT (in LQT1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_074999" FT VARIANT 392 FT /note="W -> R (in LQT1; dbSNP:rs199472774)" FT /evidence="ECO:0000269|PubMed:10220144" FT /id="VAR_008128" FT VARIANT 393 FT /note="K -> M (in LQT1; uncertain significance; FT dbSNP:rs199472775)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075000" FT VARIANT 393 FT /note="K -> N (in dbSNP:rs12720457)" FT /id="VAR_048026" FT VARIANT 397 FT /note="R -> W (in LQT1; uncertain significance; FT dbSNP:rs199472776)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075001" FT VARIANT 398 FT /note="K -> R (in LQT1; uncertain significance; FT dbSNP:rs199472777)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075002" FT VARIANT 417 FT /note="V -> M (in LQT1; associated in cis with M-254 in a FT patient; dbSNP:rs267607197)" FT /evidence="ECO:0000269|Ref.33" FT /id="VAR_010934" FT VARIANT 446 FT /note="D -> E (in LQT1; uncertain significance; FT dbSNP:rs199472780)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075003" FT VARIANT 448 FT /note="P -> L (in LQT1; uncertain significance; FT dbSNP:rs12720449)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075004" FT VARIANT 448 FT /note="P -> R (in LQT1; benign; dbSNP:rs12720449)" FT /evidence="ECO:0000269|PubMed:10973849" FT /id="VAR_009931" FT VARIANT 451 FT /note="R -> W (in LQT1; uncertain significance; FT dbSNP:rs199472782)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075005" FT VARIANT 452 FT /note="R -> W (in LQT1; uncertain significance; FT dbSNP:rs140452381)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068314" FT VARIANT 455 FT /note="H -> Y (in LQT1; loss of channel activity; FT dbSNP:rs199473476)" FT /evidence="ECO:0000269|PubMed:19808498" FT /id="VAR_080335" FT VARIANT 460 FT /note="G -> S (in LQT1; uncertain significance; FT dbSNP:rs199472783)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075006" FT VARIANT 477 FT /note="P -> L (in LQT1; uncertain significance; FT dbSNP:rs199472784)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075007" FT VARIANT 511 FT /note="R -> W (in LQT1; uncertain significance; FT dbSNP:rs199472785)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075008" FT VARIANT 518 FT /note="R -> G (in LQT1; uncertain significance; FT dbSNP:rs17215500)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075009" FT VARIANT 518 FT /note="R -> P (in LQT1; uncertain significance; FT dbSNP:rs145974930)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075010" FT VARIANT 518 FT /note="R -> Q (in LQT1; uncertain significance; FT dbSNP:rs145974930)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075011" FT VARIANT 520 FT /note="M -> R (in LQT1; uncertain significance; FT dbSNP:rs199473479)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075012" FT VARIANT 522 FT /note="Y -> S (in LQT1; uncertain significance; FT dbSNP:rs199472789)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075013" FT VARIANT 524 FT /note="V -> G (in LQT1; dbSNP:rs199472790)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068315" FT VARIANT 525 FT /note="A -> T (in LQT1; dbSNP:rs120074188)" FT /evidence="ECO:0000269|PubMed:10482963, FT ECO:0000269|PubMed:19716085" FT /id="VAR_009181" FT VARIANT 525 FT /note="A -> V (in LQT1; uncertain significance; FT dbSNP:rs199472791)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075014" FT VARIANT 526 FT /note="K -> E (in LQT1; dbSNP:rs199472792)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068316" FT VARIANT 533 FT /note="R -> W (in LQT1; minor changes of wt current FT (homomultimers); positive voltage shift of the channel FT activation (heteromultimers); dbSNP:rs199472793)" FT /evidence="ECO:0000269|PubMed:10728423, FT ECO:0000269|PubMed:19716085" FT /id="VAR_008949" FT VARIANT 539 FT /note="R -> Q (in LQT1; uncertain significance; FT dbSNP:rs199472794)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075015" FT VARIANT 539 FT /note="R -> W (in LQT1; minor changes of wt current FT (homomultimers); positive voltage shift of the channel FT activation (heteromultimers); dbSNP:rs199472795)" FT /evidence="ECO:0000269|PubMed:10728423, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085" FT /id="VAR_008950" FT VARIANT 541 FT /note="V -> I (in LQT1; uncertain significance; FT dbSNP:rs199472796)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075016" FT VARIANT 543 FT /note="E -> K (in LQT1; uncertain significance; FT dbSNP:rs199472797)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075017" FT VARIANT 546 FT /note="S -> L (in LQT1; decreases interaction with KCNE1 FT C-terminus; does not affect plasma membrane localization; FT reduces IKS current density; impairs binding with FT phosphatidylinositol 4,5-bisphosphate; loss of channel FT activity; dbSNP:rs199473480)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:19808498, FT ECO:0000269|PubMed:25037568" FT /id="VAR_068317" FT VARIANT 547 FT /note="Q -> R (in LQT1; uncertain significance; FT dbSNP:rs199472798)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075018" FT VARIANT 548 FT /note="G -> D (in LQT1; uncertain significance; FT dbSNP:rs199472799)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075019" FT VARIANT 554 FT /note="V -> A (in LQT1; uncertain significance; FT dbSNP:rs199473481)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075020" FT VARIANT 555 FT /note="R -> C (in LQT1; decreases interaction with KCNE1 FT C-terminus; does not affect plasma membrane localization; FT reduces IKS current density; shifts activation of the FT voltage dependence; deactivates more rapidly; impairs FT binding with phosphatidylinositol 4,5-bisphosphate; FT dbSNP:rs120074185)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:25037568, FT ECO:0000269|PubMed:9312006, ECO:0000269|PubMed:9386136" FT /id="VAR_001545" FT VARIANT 555 FT /note="R -> H (in LQT1; decreases interaction with KCNE1 FT C-terminus; does not affect plasma membrane localization; FT reduces IKS current density; impairs binding with FT Phosphatidylinositol 4,5-bisphosphate; dbSNP:rs199472800)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:25037568" FT /id="VAR_068318" FT VARIANT 555 FT /note="R -> S (in LQT1; uncertain significance; FT dbSNP:rs120074185)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075021" FT VARIANT 557 FT /note="K -> E (in LQT1; no effect on cell membrane FT localization; slows activation kinetics; accelerates FT deactivation kinetics; rightshifts the voltage-dependent FT activation; does not affect cAMP-dependent up-regulation; FT decreases interaction with KCNE1 C-terminus; does not FT affect plasma membrane localization; does not affect FT phosphorylation at S-27 during cAMP-dependent stimulation; FT reduces IKS current density; impairs binding with FT Phosphatidylinositol 4,5-bisphosphate; dbSNP:rs199472801)" FT /evidence="ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:25037568, ECO:0000269|PubMed:25139741" FT /id="VAR_074693" FT VARIANT 566 FT /note="S -> F (in LQT1; dbSNP:rs199472804)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:19716085" FT /id="VAR_009932" FT VARIANT 566 FT /note="S -> P (in LQT1; uncertain significance; FT dbSNP:rs199472803)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075022" FT VARIANT 566 FT /note="S -> Y (in LQT1; dbSNP:rs199472804)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068319" FT VARIANT 567 FT /note="I -> S (in LQT1; dbSNP:rs199472805)" FT /evidence="ECO:0000269|PubMed:15840476" FT /id="VAR_068320" FT VARIANT 567 FT /note="I -> T (in LQT1; dbSNP:rs199472805)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:19716085" FT /id="VAR_075023" FT VARIANT 568 FT /note="G -> R (in LQT1; dbSNP:rs199472807)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:19716085" FT /id="VAR_068321" FT VARIANT 569 FT /note="K -> E (in LQT1; uncertain significance; FT dbSNP:rs199472808)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075024" FT VARIANT 571 FT /note="S -> L (in LQT1; uncertain significance; FT dbSNP:rs199472809)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075025" FT VARIANT 573 FT /note="F -> L (in LQT1; uncertain significance; FT dbSNP:rs199472810)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075026" FT VARIANT 583 FT /note="R -> C (in LQT1; dbSNP:rs17221854)" FT /evidence="ECO:0000269|PubMed:10973849" FT /id="VAR_009933" FT VARIANT 583 FT /note="R -> H (in LQT1; uncertain significance; FT dbSNP:rs199473482)" FT /evidence="ECO:0000269|PubMed:16414944" FT /id="VAR_075027" FT VARIANT 586 FT /note="N -> D (in LQT1; decreases outward potassium FT current; decreases plasma membrane localization; FT dbSNP:rs199472812)" FT /evidence="ECO:0000269|PubMed:16414944, FT ECO:0000269|PubMed:25705178" FT /id="VAR_074694" FT VARIANT 587 FT /note="T -> M (in LQT1; dbSNP:rs120074189)" FT /evidence="ECO:0000269|PubMed:10024302, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085, FT ECO:0000269|PubMed:9799083" FT /id="VAR_008951" FT VARIANT 589 FT /note="G -> D (in LQT1 and JLNS1; affects plasma membrane FT localization; strongly reduces potassium current; impairs FT binding to AKAP9 and the targeting protein kinase A (PKA) FT catalytic subunit and protein phosphatase 1 (PP1); FT dbSNP:rs120074190)" FT /evidence="ECO:0000269|PubMed:11799244, FT ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:25037568, FT ECO:0000269|PubMed:25705178" FT /id="VAR_008952" FT VARIANT 590 FT /note="A -> T (in LQT1; reduces IKs density and causes a FT right-shift of the current?voltage relation of channel FT activation; reduces cell surface expression; no effect on FT interaction with AKAP9; does not affect the cAMP-dependent FT IKs up-regulation; dbSNP:rs199472813)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:24713462" FT /id="VAR_068322" FT VARIANT 591 FT /note="R -> C (in LQT1; uncertain significance; FT dbSNP:rs199473483)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075028" FT VARIANT 591 FT /note="R -> H (in LQT1; dbSNP:rs199472814)" FT /evidence="ECO:0000269|PubMed:10024302, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085" FT /id="VAR_008953" FT VARIANT 594 FT /note="R -> P (in LQT1; uncertain significance; FT dbSNP:rs199472815)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075029" FT VARIANT 594 FT /note="R -> Q (in LQT1; dbSNP:rs199472815)" FT /evidence="ECO:0000269|PubMed:10973849, FT ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:19716085" FT /id="VAR_009934" FT VARIANT 596 FT /note="E -> K (in LQT1; uncertain significance; FT dbSNP:rs199472816)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075030" FT VARIANT 596 FT /note="Missing (in LQT1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075031" FT VARIANT 600 FT /note="T -> M (in LQT1; uncertain significance; FT dbSNP:rs34516117)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075032" FT VARIANT 611 FT /note="D -> N (in LQT1; uncertain significance; FT dbSNP:rs147445322)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075033" FT VARIANT 614 FT /note="Missing (in LQT1; uncertain significance; FT dbSNP:rs397508101)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075034" FT VARIANT 619 FT /note="L -> M (in LQT1; decreases outward potassium FT current; decreases plasma membrane localization; FT dbSNP:rs199472819)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:25705178" FT /id="VAR_068323" FT VARIANT 626 FT /note="G -> S (in LQT1; dbSNP:rs199472821)" FT /evidence="ECO:0000269|PubMed:15840476, FT ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:19716085" FT /id="VAR_068324" FT VARIANT 635 FT /note="G -> R (in LQT1; uncertain significance; FT dbSNP:rs199473484)" FT /evidence="ECO:0000269|PubMed:19716085" FT /id="VAR_075035" FT VARIANT 643 FT /note="G -> S (in dbSNP:rs1800172)" FT /evidence="ECO:0000269|PubMed:9799083" FT /id="VAR_008954" FT MUTAGEN 27 FT /note="S->A: No phosphorylation by PKA. Decreases delayed FT rectifier potassium channel activity." FT /evidence="ECO:0000269|PubMed:11799244" FT MUTAGEN 231 FT /note="R->A: Strongly inhibits SLC5A3 transporter FT activity." FT /evidence="ECO:0000269|PubMed:24595108" FT MUTAGEN 324 FT /note="V->L: Has a voltage-gated potassium channel FT activity. Inhibition of voltage-gated potassium channel FT activity by KCNE4." FT /evidence="ECO:0000269|PubMed:19687231" FT MUTAGEN 326 FT /note="K->R: Has a voltage-gated potassium channel FT activity. Disrupts KCNE4-mediated voltage-gated potassium FT channel activity inhibition." FT /evidence="ECO:0000269|PubMed:19687231" FT MUTAGEN 327 FT /note="T->V: Has a voltage-gated potassium channel FT activity. Disrupts KCNE4-mediated voltage-gated potassium FT channel activity inhibition." FT /evidence="ECO:0000269|PubMed:19687231" FT MUTAGEN 328 FT /note="I->L: Has a voltage-gated potassium channel FT activity. Inhibition of voltage-gated potassium channel FT activity by KCNE4." FT /evidence="ECO:0000269|PubMed:19687231" FT MUTAGEN 338 FT /note="S->C: Inhibits voltage-gated potassium channel FT activity." FT /evidence="ECO:0000269|PubMed:19687231" FT MUTAGEN 340 FT /note="F->C: Inhibits voltage-gated potassium channel FT activity." FT /evidence="ECO:0000269|PubMed:19687231" FT MUTAGEN 375 FT /note="I->D: Reduced protein expression, probably due to FT misfolding and proteasomal degradation. No detectable FT electrophysiological activity. Reduced electrophysiological FT activity in the presence of KCNE1." FT /evidence="ECO:0000269|PubMed:25441029" FT MUTAGEN 516 FT /note="V->D: Reduced protein expression, probably due to FT misfolding and proteasomal degradation. Significantly FT reduced electrophysiological activity. Reduced FT electrophysiological activity in the presence of KCNE1." FT /evidence="ECO:0000269|PubMed:25441029" FT MUTAGEN 589 FT /note="G->M: No effect." FT /evidence="ECO:0000269|PubMed:18165683" FT MUTAGEN 590 FT /note="A->W: Reduced cell surface expression and strongly FT reduced potassium current." FT /evidence="ECO:0000269|PubMed:18165683" FT MUTAGEN 593 FT /note="N->G: Reduced cell surface expression and moderately FT reduced potassium current." FT /evidence="ECO:0000269|PubMed:18165683" FT MUTAGEN 602 FT /note="L->A: Does not interact with AKAP9 and the targeting FT protein kinase A (PKA) catalytic subunit and protein FT phosphatase 1 (PP1); when associated with I-609." FT /evidence="ECO:0000269|PubMed:11799244" FT MUTAGEN 609 FT /note="I->A: Does not interact with AKAP9 and the kinase A FT (PKA) catalytic subunit and protein phosphatase 1 (PP1); FT when associated with L-602." FT /evidence="ECO:0000269|PubMed:11799244" FT CONFLICT 64..65 FT /note="PA -> HV (in Ref. 4; CAB44649)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="Missing (in Ref. 2; AAC05705)" FT /evidence="ECO:0000305" FT CONFLICT 607..608 FT /note="AL -> VI (in Ref. 5; AAM94040)" FT /evidence="ECO:0000305" FT CONFLICT 619..644 FT /note="LHGGSTPGSGGPPREGGAHITQPCGS -> MQQGGPTCNSRSQVVASNE FT (in Ref. 5; AAM94040)" FT /evidence="ECO:0000305" FT CONFLICT 648..649 FT /note="VD -> IN (in Ref. 5; AAM94040)" FT /evidence="ECO:0000305" FT CONFLICT 658 FT /note="T -> S (in Ref. 5; AAM94040)" FT /evidence="ECO:0000305" FT CONFLICT 669..670 FT /note="RR -> QT (in Ref. 5; AAM94040)" FT /evidence="ECO:0000305" FT HELIX 106..114 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 121..141 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:6V00" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 151..176 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:6UZZ" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 186..194 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 197..215 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 224..236 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:7XNN" FT STRAND 241..244 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 246..284 FT /evidence="ECO:0007829|PDB:7XNN" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:6V00" FT HELIX 299..310 FT /evidence="ECO:0007829|PDB:7XNN" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 323..335 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 337..340 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 342..382 FT /evidence="ECO:0007829|PDB:7XNN" FT STRAND 386..389 FT /evidence="ECO:0007829|PDB:4UMO" FT TURN 391..394 FT /evidence="ECO:0007829|PDB:7XNK" FT HELIX 507..531 FT /evidence="ECO:0007829|PDB:7XNN" FT HELIX 538..554 FT /evidence="ECO:0007829|PDB:7XNN" FT TURN 564..566 FT /evidence="ECO:0007829|PDB:6V00" FT HELIX 588..609 FT /evidence="ECO:0007829|PDB:3HFE" SQ SEQUENCE 676 AA; 74699 MW; ADFCA9E2B9763B21 CRC64; MAAASSPPRA ERKRWGWGRL PGARRGSAGL AKKCPFSLEL AEGGPAGGAL YAPIAPGAPG PAPPASPAAP AAPPVASDLG PRPPVSLDPR VSIYSTRRPV LARTHVQGRV YNFLERPTGW KCFVYHFAVF LIVLVCLIFS VLSTIEQYAA LATGTLFWME IVLVVFFGTE YVVRLWSAGC RSKYVGLWGR LRFARKPISI IDLIVVVASM VVLCVGSKGQ VFATSAIRGI RFLQILRMLH VDRQGGTWRL LGSVVFIHRQ ELITTLYIGF LGLIFSSYFV YLAEKDAVNE SGRVEFGSYA DALWWGVVTV TTIGYGDKVP QTWVGKTIAS CFSVFAISFF ALPAGILGSG FALKVQQKQR QKHFNRQIPA AASLIQTAWR CYAAENPDSS TWKIYIRKAP RSHTLLSPSP KPKKSVVVKK KKFKLDKDNG VTPGEKMLTV PHITCDPPEE RRLDHFSVDG YDSSVRKSPT LLEVSMPHFM RTNSFAEDLD LEGETLLTPI THISQLREHH RATIKVIRRM QYFVAKKKFQ QARKPYDVRD VIEQYSQGHL NLMVRIKELQ RRLDQSIGKP SLFISVSEKS KDRGSNTIGA RLNRVEDKVT QLDQRLALIT DMLHQLLSLH GGSTPGSGGP PREGGAHITQ PCGSGGSVDP ELFLPSNTLP TYEQLTVPRR GPDEGS //