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KCNE2_HUMAN
ID   KCNE2_HUMAN             Reviewed;         123 AA.
AC   Q9Y6J6; A5H1P3; D3DSF8; Q52LJ5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Potassium voltage-gated channel subfamily E member 2;
DE   AltName: Full=MinK-related peptide 1;
DE   AltName: Full=Minimum potassium ion channel-related peptide 1;
DE   AltName: Full=Potassium channel subunit beta MiRP1;
GN   Name=KCNE2;
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], VARIANTS LQT6 THR-54 AND THR-57, VARIANTS ALA-8
RP   AND GLU-9, FUNCTION, CHARACTERIZATION OF VARIANTS LQT6 THR-54 AND THR-57,
RP   CHARACTERIZATION OF VARIANT GLU-9, AND INTERACTION WITH KCNH2.
RC   TISSUE=Heart;
RX   PubMed=10219239; DOI=10.1016/s0092-8674(00)80728-x;
RA   Abbott G.W., Sesti F., Splawski I., Buck M.E., Lehmann M.H., Timothy K.W.,
RA   Keating M.T., Goldstein S.A.N.;
RT   "MiRP1 forms IKr potassium channels with HERG and is associated with
RT   cardiac arrhythmia.";
RL   Cell 97:175-187(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Domenech A., Estivill X., de la Luna S.;
RT   "Cloning of human MIRP1 cDNA.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   ASSOCIATION WITH KCNQ2/KCNQ3, AND TISSUE SPECIFICITY.
RX   PubMed=11034315; DOI=10.1016/s0014-5793(00)01918-9;
RA   Tinel N., Diochot S., Lauritzen I., Barhanin J., Lazdunski M., Borsotto M.;
RT   "M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2
RT   subunit.";
RL   FEBS Lett. 480:137-141(2000).
RN   [7]
RP   INTERACTION WITH KCNQ1, 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   [8]
RP   MUTAGENESIS OF LYS-75.
RX   PubMed=11874988; DOI=10.1096/fj.01-0520hyp;
RA   Abbott G.W., Goldstein S.A.N.;
RT   "Disease-associated mutations in KCNE potassium channel subunits (MiRPs)
RT   reveal promiscuous disruption of multiple currents and conservation of
RT   mechanism.";
RL   FASEB J. 16:390-400(2002).
RN   [9]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH KCNQ1.
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   [10]
RP   VARIANT LQT6 MET-65.
RX   PubMed=12185453; DOI=10.1007/s00109-002-0364-0;
RA   Isbrandt D., Friederich P., Solth A., Haverkamp W., Ebneth A.,
RA   Borggrefe M., Funke H., Sauter K., Breithardt G., Pongs O.,
RA   Schulze-Bahr E.;
RT   "Identification and functional characterization of a novel KCNE2 (MiRP1)
RT   mutation that alters HERG channel kinetics.";
RL   J. Mol. Med. 80:524-532(2002).
RN   [11]
RP   VARIANT ATFB4 CYS-27, AND CHARACTERIZATION OF VARIANT ATFB4 CYS-27.
RX   PubMed=15368194; DOI=10.1086/425342;
RA   Yang Y., Xia M., Jin Q., Bendahhou S., Shi J., Chen Y., Liang B., Lin J.,
RA   Liu Y., Liu B., Zhou Q., Zhang D., Wang R., Ma N., Su X., Niu K., Pei Y.,
RA   Xu W., Chen Z., Wan H., Cui J., Barhanin J., Chen Y.;
RT   "Identification of a KCNE2 gain-of-function mutation in patients with
RT   familial atrial fibrillation.";
RL   Am. J. Hum. Genet. 75:899-905(2004).
RN   [12]
RP   VARIANTS LQT6 THR-57; LEU-60 AND TRP-77, AND VARIANT ALA-8.
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   [13]
RP   VARIANTS LQT6 ILE-14; ASN-20; HIS-27; THR-54; THR-57; LEU-65; GLN-77 AND
RP   GLY-94.
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).
CC   -!- FUNCTION: Ancillary protein that assembles as a beta subunit with a
CC       voltage-gated potassium channel complex of pore-forming alpha subunits.
CC       Modulates the gating kinetics and enhances stability of the channel
CC       complex. Assembled with KCNB1 modulates the gating characteristics of
CC       the delayed rectifier voltage-dependent potassium channel KCNB1.
CC       Associated with KCNH2/HERG is proposed to form the rapidly activating
CC       component of the delayed rectifying potassium current in heart (IKr).
CC       May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type
CC       current. May associate with HCN1 and HCN2 and increase potassium
CC       current. Interacts with KCNQ1; forms a heterooligomer complex leading
CC       to currents with an apparently instantaneous activation, a rapid
CC       deactivation process and a linear current-voltage relationship and
CC       decreases the amplitude of the outward current (PubMed:11101505).
CC       {ECO:0000250|UniProtKB:P63161, ECO:0000269|PubMed:10219239,
CC       ECO:0000269|PubMed:11101505}.
CC   -!- SUBUNIT: Interacts with KCNB1 (By similarity). Associates with
CC       KCNH2/ERG1 (PubMed:10219239). May associate with KCNQ2 and KCNQ3
CC       (PubMed:11034315,). Associates with HCN1 and probably HCN2.
CC       Heteromultimer with KCNC2. Interacts with KCNC2 (By similarity).
CC       Interacts with KCNQ1; forms a heterooligomer complex that targets to
CC       the membrane raft and 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, PubMed:20533308).
CC       {ECO:0000250|UniProtKB:P63161, ECO:0000269|PubMed:10219239,
CC       ECO:0000269|PubMed:11034315, ECO:0000269|PubMed:11101505,
CC       ECO:0000269|PubMed:20533308}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20533308};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P63161}.
CC       Note=Colocalizes with KCNB1 at the plasma membrane.
CC       {ECO:0000250|UniProtKB:P63161}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, skeletal muscle,
CC       pancreas, placenta, kidney, colon and thymus. A small but significant
CC       expression is found in liver, ovary, testis, prostate, small intestine
CC       and leukocytes. Very low expression, nearly undetectable, in lung and
CC       spleen. {ECO:0000269|PubMed:11034315}.
CC   -!- DISEASE: Long QT syndrome 6 (LQT6) [MIM:613693]: 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:10219239, ECO:0000269|PubMed:12185453,
CC       ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:19716085}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Atrial fibrillation, familial, 4 (ATFB4) [MIM:611493]: A
CC       familial form of atrial fibrillation, a common sustained cardiac rhythm
CC       disturbance. Atrial fibrillation is characterized by disorganized
CC       atrial electrical activity and ineffective atrial contraction promoting
CC       blood stasis in the atria and reduces ventricular filling. It can
CC       result in palpitations, syncope, thromboembolic stroke, and congestive
CC       heart failure. {ECO:0000269|PubMed:15368194}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC       {ECO:0000305}.
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DR   EMBL; AF071002; AAD28086.1; -; mRNA.
DR   EMBL; AF302095; AAG13416.1; -; mRNA.
DR   EMBL; DQ784804; ABQ01239.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09791.1; -; Genomic_DNA.
DR   EMBL; BC093892; AAH93892.1; -; mRNA.
DR   EMBL; BC112087; AAI12088.1; -; mRNA.
DR   CCDS; CCDS13635.1; -.
DR   RefSeq; NP_751951.1; NM_172201.1.
DR   PDB; 2M0Q; NMR; -; A=1-123.
DR   PDBsum; 2M0Q; -.
DR   AlphaFoldDB; Q9Y6J6; -.
DR   BMRB; Q9Y6J6; -.
DR   SMR; Q9Y6J6; -.
DR   BioGRID; 115313; 5.
DR   ComplexPortal; CPX-3073; Voltage-gated potassium channel complex variant 2.
DR   CORUM; Q9Y6J6; -.
DR   STRING; 9606.ENSP00000290310; -.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB01069; Promethazine.
DR   GlyGen; Q9Y6J6; 2 sites.
DR   iPTMnet; Q9Y6J6; -.
DR   PhosphoSitePlus; Q9Y6J6; -.
DR   BioMuta; KCNE2; -.
DR   DMDM; 6685661; -.
DR   MassIVE; Q9Y6J6; -.
DR   PaxDb; Q9Y6J6; -.
DR   PeptideAtlas; Q9Y6J6; -.
DR   PRIDE; Q9Y6J6; -.
DR   ProteomicsDB; 86701; -.
DR   Antibodypedia; 22942; 173 antibodies from 27 providers.
DR   DNASU; 9992; -.
DR   Ensembl; ENST00000290310.4; ENSP00000290310.2; ENSG00000159197.4.
DR   GeneID; 9992; -.
DR   KEGG; hsa:9992; -.
DR   MANE-Select; ENST00000290310.4; ENSP00000290310.2; NM_172201.2; NP_751951.1.
DR   UCSC; uc002ytt.2; human.
DR   CTD; 9992; -.
DR   DisGeNET; 9992; -.
DR   GeneCards; KCNE2; -.
DR   GeneReviews; KCNE2; -.
DR   HGNC; HGNC:6242; KCNE2.
DR   HPA; ENSG00000159197; Tissue enriched (stomach).
DR   MalaCards; KCNE2; -.
DR   MIM; 603796; gene.
DR   MIM; 611493; phenotype.
DR   MIM; 613693; phenotype.
DR   neXtProt; NX_Q9Y6J6; -.
DR   OpenTargets; ENSG00000159197; -.
DR   Orphanet; 334; Familial atrial fibrillation.
DR   Orphanet; 101016; Romano-Ward syndrome.
DR   PharmGKB; PA392; -.
DR   VEuPathDB; HostDB:ENSG00000159197; -.
DR   eggNOG; ENOG502S1GJ; Eukaryota.
DR   GeneTree; ENSGT00940000154497; -.
DR   HOGENOM; CLU_1991831_0_0_1; -.
DR   InParanoid; Q9Y6J6; -.
DR   OMA; DYVILYL; -.
DR   OrthoDB; 1493495at2759; -.
DR   PhylomeDB; Q9Y6J6; -.
DR   TreeFam; TF336058; -.
DR   PathwayCommons; Q9Y6J6; -.
DR   Reactome; R-HSA-5576890; Phase 3 - rapid repolarisation.
DR   Reactome; R-HSA-5576893; Phase 2 - plateau phase.
DR   SignaLink; Q9Y6J6; -.
DR   BioGRID-ORCS; 9992; 29 hits in 1059 CRISPR screens.
DR   ChiTaRS; KCNE2; human.
DR   GeneWiki; KCNE2; -.
DR   GenomeRNAi; 9992; -.
DR   Pharos; Q9Y6J6; Tbio.
DR   PRO; PR:Q9Y6J6; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; Q9Y6J6; protein.
DR   Bgee; ENSG00000159197; Expressed in body of stomach and 109 other tissues.
DR   Genevisible; Q9Y6J6; HS.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; IDA: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:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:BHF-UCL.
DR   GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR   GO; GO:0086011; P:membrane repolarization during 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:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:BHF-UCL.
DR   GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:BHF-UCL.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:BHF-UCL.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL.
DR   GO; GO:1902159; P:regulation of cyclic nucleotide-gated ion channel activity; IEA:Ensembl.
DR   GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR   GO; GO:0043586; P:tongue development; IEA:Ensembl.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR   InterPro; IPR000369; K_chnl_KCNE.
DR   InterPro; IPR005425; K_chnl_volt-dep_bsu_KCNE2.
DR   PANTHER; PTHR15282; PTHR15282; 1.
DR   Pfam; PF02060; ISK_Channel; 1.
DR   PRINTS; PR01605; KCNE2CHANNEL.
PE   1: Evidence at protein level;
KW   3D-structure; Atrial fibrillation; Cell membrane; Disease variant;
KW   Glycoprotein; Ion channel; Ion transport; Long QT syndrome; Membrane;
KW   Potassium; Potassium channel; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..123
FT                   /note="Potassium voltage-gated channel subfamily E member
FT                   2"
FT                   /id="PRO_0000144285"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         8
FT                   /note="T -> A (in dbSNP:rs2234916)"
FT                   /evidence="ECO:0000269|PubMed:10219239,
FT                   ECO:0000269|PubMed:16922724"
FT                   /id="VAR_008375"
FT   VARIANT         8
FT                   /note="T -> I (in dbSNP:rs35759083)"
FT                   /id="VAR_037794"
FT   VARIANT         9
FT                   /note="Q -> E (risk factor for drug-induced arrhythmia;
FT                   impedes activation and increases sensitivity to macrolide
FT                   antibiotics; may lower current in KCNQ1/KCNE2 channel;
FT                   dbSNP:rs16991652)"
FT                   /evidence="ECO:0000269|PubMed:10219239"
FT                   /id="VAR_008376"
FT   VARIANT         14
FT                   /note="V -> I (in LQT6; unknown pathological significance;
FT                   dbSNP:rs142153692)"
FT                   /evidence="ECO:0000269|PubMed:19716085"
FT                   /id="VAR_074921"
FT   VARIANT         20
FT                   /note="I -> N (in LQT6; unknown pathological significance;
FT                   dbSNP:rs199473363)"
FT                   /evidence="ECO:0000269|PubMed:19716085"
FT                   /id="VAR_074922"
FT   VARIANT         27
FT                   /note="R -> C (in ATFB4; gain-of-function mutation
FT                   associated with the initiation and/or maintenance of AF;
FT                   dbSNP:rs74315449)"
FT                   /evidence="ECO:0000269|PubMed:15368194"
FT                   /id="VAR_037795"
FT   VARIANT         27
FT                   /note="R -> H (in LQT6; unknown pathological significance;
FT                   dbSNP:rs148968498)"
FT                   /evidence="ECO:0000269|PubMed:19716085"
FT                   /id="VAR_074923"
FT   VARIANT         54
FT                   /note="M -> T (in LQT6; forms I(KR) channels that
FT                   deactivate twice as fast as wild type; dbSNP:rs74315447)"
FT                   /evidence="ECO:0000269|PubMed:10219239,
FT                   ECO:0000269|PubMed:19716085"
FT                   /id="VAR_008377"
FT   VARIANT         57
FT                   /note="I -> T (in LQT6; may affect KCNQ1/KCNE2 channel;
FT                   dbSNP:rs74315448)"
FT                   /evidence="ECO:0000269|PubMed:10219239,
FT                   ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:19716085"
FT                   /id="VAR_008378"
FT   VARIANT         60
FT                   /note="F -> L (in LQT6; unknown pathological significance;
FT                   dbSNP:rs16991654)"
FT                   /evidence="ECO:0000269|PubMed:16922724"
FT                   /id="VAR_029334"
FT   VARIANT         65
FT                   /note="V -> L (in LQT6; unknown pathological significance;
FT                   dbSNP:rs199473364)"
FT                   /evidence="ECO:0000269|PubMed:19716085"
FT                   /id="VAR_074924"
FT   VARIANT         65
FT                   /note="V -> M (in LQT6; dbSNP:rs199473364)"
FT                   /evidence="ECO:0000269|PubMed:12185453"
FT                   /id="VAR_015063"
FT   VARIANT         66
FT                   /note="A -> V (in dbSNP:rs16991656)"
FT                   /id="VAR_022052"
FT   VARIANT         77
FT                   /note="R -> Q (in LQT6; unknown pathological significance;
FT                   dbSNP:rs199473365)"
FT                   /evidence="ECO:0000269|PubMed:19716085"
FT                   /id="VAR_074925"
FT   VARIANT         77
FT                   /note="R -> W (in LQT6; dbSNP:rs141423405)"
FT                   /evidence="ECO:0000269|PubMed:16922724"
FT                   /id="VAR_035386"
FT   VARIANT         94
FT                   /note="E -> G (in LQT6; unknown pathological significance;
FT                   dbSNP:rs74424227)"
FT                   /evidence="ECO:0000269|PubMed:19716085"
FT                   /id="VAR_074926"
FT   MUTAGEN         75
FT                   /note="K->H: Increases tail current in KCNH2/KCNE2
FT                   channel."
FT                   /evidence="ECO:0000269|PubMed:11874988"
FT   HELIX           3..38
FT                   /evidence="ECO:0007829|PDB:2M0Q"
FT   HELIX           46..74
FT                   /evidence="ECO:0007829|PDB:2M0Q"
FT   HELIX           88..114
FT                   /evidence="ECO:0007829|PDB:2M0Q"
SQ   SEQUENCE   123 AA;  14472 MW;  C3016415E1B44890 CRC64;
     MSTLSNFTQT LEDVFRRIFI TYMDNWRQNT TAEQEALQAK VDAENFYYVI LYLMVMIGMF
     SFIIVAILVS TVKSKRREHS NDPYHQYIVE DWQEKYKSQI LNLEESKATI HENIGAAGFK
     MSP
 
 
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