KCNQ1_MOUSE
ID KCNQ1_MOUSE Reviewed; 668 AA.
AC P97414; O88702; Q3U4H1; Q7TNZ1; Q7TPL7; Q80VR7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 1;
DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000305|PubMed:11120752};
DE AltName: Full=KQT-like 1 {ECO:0000250|UniProtKB:P51787};
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000250|UniProtKB:P51787};
GN Name=Kcnq1 {ECO:0000312|MGI:MGI:108083};
GN Synonyms=Kcna9 {ECO:0000312|MGI:MGI:108083},
GN Kvlqt1 {ECO:0000303|PubMed:11120752};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/SvJ; TISSUE=Heart;
RX PubMed=15004216; DOI=10.1124/jpet.103.063743;
RA Knollmann B.C., Casimiro M.C., Katchman A.N., Sirenko S.G., Schober T.,
RA Rong Q., Pfeifer K., Ebert S.N.;
RT "Isoproterenol exacerbates a long QT phenotype in Kcnq1-deficient neonatal
RT mice: possible roles for human-like Kcnq1 isoform 1 and slow delayed
RT rectifier K+ current.";
RL J. Pharmacol. Exp. Ther. 310:311-318(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=FVB/N; TISSUE=Colon, and Olfactory epithelium;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-668 (ISOFORM I), FUNCTION, AND INTERACTION
RP WITH KCNE1.
RC TISSUE=Heart;
RX PubMed=8900282; DOI=10.1038/384078a0;
RA Barhanin J., Lesage F., Guillemare E., Fink M., Lazdunski M., Romey G.;
RT "K(V)LQT1 and IsK (minK) proteins associate to form the I(Ks) cardiac
RT potassium current.";
RL Nature 384:78-80(1996).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM II), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=9618174; DOI=10.1093/hmg/7.7.1149;
RA Paulsen M., Davies K.R., Bowden L.M., Villar A.J., Franck O., Fuermann M.,
RA Dean W.L., Moore T.F., Rodrigues N., Davies K.E., Hu R.-J., Feinberg A.P.,
RA Maher E.R., Reik W., Walter J.;
RT "Syntenic organization of the mouse distal chromosome 7 imprinting cluster
RT and the Beckwith-Wiedemann syndrome region in chromosome 11p15.5.";
RL Hum. Mol. Genet. 7:1149-1159(1998).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11120752; DOI=10.1172/jci10897;
RA Lee M.P., Ravenel J.D., Hu R.J., Lustig L.R., Tomaselli G., Berger R.D.,
RA Brandenburg S.A., Litzi T.J., Bunton T.E., Limb C., Francis H.,
RA Gorelikow M., Gu H., Washington K., Argani P., Goldenring J.R.,
RA Coffey R.J., Feinberg A.P.;
RT "Targeted disruption of the Kvlqt1 gene causes deafness and gastric
RT hyperplasia in mice.";
RL J. Clin. Invest. 106:1447-1455(2000).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16314573; DOI=10.1073/pnas.0505860102;
RA Vallon V., Grahammer F., Volkl H., Sandu C.D., Richter K., Rexhepaj R.,
RA Gerlach U., Rong Q., Pfeifer K., Lang F.;
RT "KCNQ1-dependent transport in renal and gastrointestinal epithelia.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17864-17869(2005).
RN [8]
RP FUNCTION.
RX PubMed=17597584; DOI=10.1016/j.bbrc.2007.06.038;
RA Knollmann B.C., Sirenko S., Rong Q., Katchman A.N., Casimiro M.,
RA Pfeifer K., Ebert S.N.;
RT "Kcnq1 contributes to an adrenergic-sensitive steady-state K+ current in
RT mouse heart.";
RL Biochem. Biophys. Res. Commun. 360:212-218(2007).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19491250; DOI=10.1113/jphysiol.2009.173302;
RA Song P., Groos S., Riederer B., Feng Z., Krabbenhoeft A., Smolka A.,
RA Seidler U.;
RT "KCNQ1 is the luminal K+ recycling channel during stimulation of gastric
RT acid secretion.";
RL J. Physiol. (Lond.) 587:3955-3965(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-408, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Potassium channel that plays an important role in a number of
CC tissues, including heart, inner ear, stomach and colon (By similarity)
CC (PubMed:16314573, PubMed:11120752, PubMed:15004216). Associates with
CC KCNE beta subunits that modulates current kinetics (By similarity)
CC (PubMed:17597584, PubMed:15004216). Induces a voltage-dependent by
CC rapidly activating and slowly deactivating potassium-selective outward
CC current (By similarity) (PubMed:8900282). Promotes also a delayed
CC voltage activated potassium current showing outward rectification
CC characteristic (By similarity). During beta-adrenergic receptor
CC stimulation participates in cardiac repolarization by associating with
CC KCNE1 to form the I(Ks) cardiac potassium current that increases the
CC amplitude and slows down the activation kinetics of outward potassium
CC current I(Ks) (By similarity) (PubMed:15004216, PubMed:17597584).
CC Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1
CC current (By similarity). When associated with KCNE3, forms the
CC potassium channel that is important for cyclic AMP-stimulated
CC intestinal secretion of chloride ions (By similarity). This interaction
CC with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction
CC of currents (By similarity). During conditions of increased substrate
CC load, maintains the driving force for proximal tubular and intestinal
CC sodium ions absorption, gastric acid secretion, and cAMP-induced
CC jejunal chloride ions secretion (PubMed:16314573). Allows the provision
CC of potassium ions to the luminal membrane of the secretory canaliculus
CC in the resting state as well as during stimulated acid secretion
CC (PubMed:19491250). When associated with KCNE2, forms an heterooligomer
CC complex leading to currents with an apparently instantaneous
CC activation, a rapid deactivation process and a linear current-voltage
CC relationship and decreases the amplitude of the outward current (By
CC similarity). When associated with KCNE4, inhibits voltage-gated
CC potassium channel activity (By similarity). When associated with KCNE5,
CC this complex only conducts current upon strong and continued
CC depolarization (By similarity). Also forms a heterotetramer with KCNQ5;
CC has a voltage-gated potassium channel activity (By similarity). Binds
CC with phosphatidylinositol 4,5-bisphosphate (By similarity).
CC {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:Q9Z0N7,
CC ECO:0000269|PubMed:11120752, ECO:0000269|PubMed:15004216,
CC ECO:0000269|PubMed:16314573, ECO:0000269|PubMed:17597584,
CC ECO:0000269|PubMed:19491250, ECO:0000269|PubMed:8900282}.
CC -!- SUBUNIT: Tetramer (By similarity). Heterotetramer with KCNE1; form the
CC native cardiac channel I(Ks) which increases the amplitude and slows
CC down the activation kinetics of outward potassium current and targets
CC to the membrane raft (By similarity) (PubMed:8900282). Interacts (via
CC C-terminus) with CALM; forms a heterooctameric structure (with 4:4
CC KCNQ1:CALM stoichiometry) in a calcium-independent manner. Interacts
CC with AKAP9; targets protein kinase A (PKA) catalytic and regulatory
CC subunits and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex,
CC allowing PKA-mediated phosphorylation and increase of delayed rectifier
CC potassium channel activity. Interacts with KCNE2; form an
CC heterooligomer complex that targets to the membrane raft and leading to
CC 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. Interacts with AP2M1;
CC mediates estrogen-induced internalization via clathrin-coated vesicles.
CC Interacts with NEDD4L; promotes internalization and decreases I(Ks)
CC currents. Interacts with USP2; counteracts the NEDD4L-specific down-
CC regulation of I(Ks) and restore plasma membrane localization.
CC Heterotetramer with KCNQ5; has a voltage-gated potassium channel
CC activity. Interacts with KCNE3; alters membrane raft localization.
CC Interacts with KCNE4; impairs KCNQ1 localization in lipid rafts and
CC inhibits voltage-gated potassium channel activity. Interacts with
CC KCNE5; impairs KCNQ1 localization in lipid rafts and only conducts
CC current upon strong and continued depolarization (By similarity).
CC {ECO:0000250|UniProtKB:P51787, ECO:0000269|PubMed:8900282}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome
CC {ECO:0000250|UniProtKB:P51787}. Membrane raft
CC {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the
CC plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with
CC RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained
CC at the endoplasmic reticulum and is localized outside of lipid raft
CC microdomains. During the early stages of epithelial cell polarization
CC induced by the calcium switch it removed from plasma membrane to the
CC endoplasmic reticulum where it retained and it is redistributed to the
CC basolateral cell surface in a PI3K-dependent manner at a later stage.
CC {ECO:0000250|UniProtKB:P51787}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=I;
CC IsoId=P97414-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P97414-2; Sequence=VSP_011748, VSP_000983;
CC -!- TISSUE SPECIFICITY: Expressed in heart, kidney and salivary glands.
CC Detected in the cochlea. Almost undetectable in brain, skeletal muscle
CC and liver. Widely expressed in embryonic and neonatal tissues.
CC {ECO:0000269|PubMed:9618174}.
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. {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The coiled-coil domain mediates tetramerization.
CC {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The segment S6 is involved in the inhibition of voltage-gated
CC potassium channel activity by KCNE4. {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The C-terminal assembly domain promotes self-interactiona;
CC allows functional channel. {ECO:0000250|UniProtKB:P51787}.
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:0000250|UniProtKB:P51787}.
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:0000250|UniProtKB:P51787}.
CC -!- PTM: Ubiquitinated by NEDD4L; promotes internalization. The
CC ubiquitinylated form is internalized through a clathrin-mediated
CC endocytosis by interacting with AP2M1 and is recycled back to the cell
CC membrane via RAB4A and RAB11A. {ECO:0000250|UniProtKB:P51787}.
CC -!- PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific down-
CC regulation of I(Ks) and restores the membrane localization.
CC {ECO:0000250|UniProtKB:P51787}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Kcnq1 show an intestinal absorption
CC impairment which is associated with reduced serum vitamin B12
CC concentrations, mild macrocytic anemia, and fecal loss of sodium and
CC potassium ions (PubMed:16314573). Mice lacking Kcnq1 show microvillar
CC secretory membranes intact, but basal acid secretion is absent and
CC forskolin-stimulated acid output is reduced by approximately 90% in
CC gastric mucosa (PubMed:19491250). Homozygous Kcnq1 mice develop
CC normally and are viable, demonstrate hyperactivity, circling, and
CC nodding behaviors; exhibit no electrocardiographic abnormalities but
CC present a complete deafness, as well as circular movement and
CC repetitive falling; show severe anatomic disruption of the cochlear and
CC vestibular end organs; also display threefold enlargement by weight of
CC the stomach resulting from mucous neck cell hyperplasia
CC (PubMed:11120752). Mice neonates lacking Kcnq1 display significantly
CC prolonged QT intervals during baseline ECG assessments which
CC significantly increased following isoproterenol challenge; furthermore,
CC the slow delayed rectifier potassium current (IKs) is absent
CC (PubMed:15004216). {ECO:0000269|PubMed:11120752,
CC ECO:0000269|PubMed:15004216, ECO:0000269|PubMed:16314573,
CC ECO:0000269|PubMed:19491250}.
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=AAB36518.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY331142; AAP93874.1; -; mRNA.
DR EMBL; AK154244; BAE32460.1; -; mRNA.
DR EMBL; BC045142; AAH45142.2; -; mRNA.
DR EMBL; BC055304; AAH55304.1; -; mRNA.
DR EMBL; U70068; AAB36518.1; ALT_INIT; mRNA.
DR EMBL; AJ002201; CAA05246.1; -; mRNA.
DR CCDS; CCDS22039.1; -. [P97414-1]
DR RefSeq; NP_032460.2; NM_008434.2. [P97414-1]
DR AlphaFoldDB; P97414; -.
DR BMRB; P97414; -.
DR SMR; P97414; -.
DR ComplexPortal; CPX-3274; KCNQ1-KCNE1 I(Ks) channel complex.
DR ComplexPortal; CPX-5826; Kv7.1 channel complex.
DR IntAct; P97414; 117.
DR STRING; 10090.ENSMUSP00000009689; -.
DR DrugCentral; P97414; -.
DR GuidetoPHARMACOLOGY; 560; -.
DR TCDB; 1.A.1.15.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P97414; 1 site.
DR iPTMnet; P97414; -.
DR PhosphoSitePlus; P97414; -.
DR MaxQB; P97414; -.
DR PaxDb; P97414; -.
DR PeptideAtlas; P97414; -.
DR PRIDE; P97414; -.
DR ProteomicsDB; 268965; -. [P97414-1]
DR ProteomicsDB; 268966; -. [P97414-2]
DR Antibodypedia; 4357; 495 antibodies from 40 providers.
DR DNASU; 16535; -.
DR Ensembl; ENSMUST00000009689; ENSMUSP00000009689; ENSMUSG00000009545. [P97414-1]
DR GeneID; 16535; -.
DR KEGG; mmu:16535; -.
DR UCSC; uc009kpb.1; mouse. [P97414-1]
DR CTD; 3784; -.
DR MGI; MGI:108083; Kcnq1.
DR VEuPathDB; HostDB:ENSMUSG00000009545; -.
DR eggNOG; KOG1419; Eukaryota.
DR GeneTree; ENSGT00940000161001; -.
DR InParanoid; P97414; -.
DR OMA; QTGPDEG; -.
DR OrthoDB; 1168835at2759; -.
DR PhylomeDB; P97414; -.
DR TreeFam; TF315186; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR Reactome; R-MMU-5576890; Phase 3 - rapid repolarisation.
DR Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR BioGRID-ORCS; 16535; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnq1; mouse.
DR PRO; PR:P97414; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P97414; protein.
DR Bgee; ENSMUSG00000009545; Expressed in epithelium of stomach and 116 other tissues.
DR ExpressionAtlas; P97414; baseline and differential.
DR Genevisible; P97414; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:1990794; C:basolateral part of cell; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0034702; C:ion channel complex; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IMP:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034705; C:potassium channel complex; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; IDA:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:MGI.
DR GO; GO:0042589; C:zymogen granule membrane; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:MGI.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0060117; P:auditory receptor cell development; IMP:MGI.
DR GO; GO:0061337; P:cardiac conduction; IMP:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IDA:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0055064; P:chloride ion homeostasis; IMP:MGI.
DR GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:MGI.
DR GO; GO:0035934; P:corticosterone secretion; IMP:MGI.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0001696; P:gastric acid secretion; IMP:MGI.
DR GO; GO:0001698; P:gastrin-induced gastric acid secretion; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
DR GO; GO:0015705; P:iodide transport; IMP:MGI.
DR GO; GO:0086009; P:membrane repolarization; IMP:UniProtKB.
DR GO; GO:0086011; P:membrane repolarization during action potential; IMP:MGI.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IDA:MGI.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; ISO:MGI.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0060453; P:regulation of gastric acid secretion; IMP:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR GO; GO:0032409; P:regulation of transporter activity; IMP:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:MGI.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; IMP:MGI.
DR GO; GO:0070293; P:renal absorption; IMP:UniProtKB.
DR GO; GO:0070294; P:renal sodium ion absorption; IMP:MGI.
DR GO; GO:0072347; P:response to anesthetic; ISO:MGI.
DR GO; GO:0071871; P:response to epinephrine; IMP:MGI.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR GO; GO:0035094; P:response to nicotine; IMP:MGI.
DR GO; GO:0007622; P:rhythmic behavior; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR GO; GO:0062094; P:stomach development; IMP:MGI.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
DR Gene3D; 1.20.120.350; -; 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; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR PANTHER; PTHR11537:SF266; PTHR11537:SF266; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 1.
DR PRINTS; PR01460; KCNQ1CHANNEL.
DR PRINTS; PR01459; KCNQCHANNEL.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell membrane; Coiled coil;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..668
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 1"
FT /id="PRO_0000054024"
FT TOPO_DOM 1..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..247
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 299..319
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 369..381
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 514..528
FT /note="Interaction with CALM; calcium-dependent"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 534..571
FT /note="Interaction with KCNE1 C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 587..615
FT /note="Interaction with AKAP9"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 588..619
FT /note="C-terminal assembly domain"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT COILED 584..620
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT MOTIF 311..316
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_011748"
FT VAR_SEQ 112..128
FT /note="FLERPTGWKCFVYHFTV -> MHQLPTSILIPKNMPGG (in isoform
FT II)"
FT /evidence="ECO:0000305"
FT /id="VSP_000983"
FT CONFLICT 473
FT /note="V -> L (in Ref. 1; AAP93874 and 4; AAB36518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 74514 MW; 8CE35CBA3102B85B CRC64;
MDTASSPPSA ERKRAGWSRL LGARRGSAVV KKCPFSLELA EGGPEGSTVY APIAPTGAPG
LAPPMSTPVS PAPAPADLGP RPRVSLDPRV SIYSARRPLL ARTHIQGRVY NFLERPTGWK
CFVYHFTVFL IVLVCLIFSV LSTIEQYAAL ATGTLFWMEI VLVVFFGTEY VVRLWSAGCR
SKYVGIWGRL RFARKPISII DLIVVVASMV VLCVGSKGQV FATSAIRGIR FLQILRMLHV
DRQGGTWRLL GSVVFIHRQE LITTLYIGFL GLIFSSYFVY LAEKDAVNES GRIEFGSYAD
ALWWGVVTVT TIGYGDKVPQ TWVGKTIASC FSVFAISFFA LPAGILGSGF ALKVQQKQRQ
KHFNRQIPAA ASLIQTAWRC YAAENPDSAT WKIYVRKPAR SHTLLSPSPK PKKSVMVKKK
KFKLDKDNGM SPGEKMFNVP HITYDPPEDR RPDHFSIDGY DSSVRKSPTL LEVSTPHFLR
TNSFAEDLDL EGETLLTPIT HVSQLRDHHR ATIKVIRRMQ YFVAKKKFQQ ARKPYDVRDV
IEQYSQGHLN LMVRIKELQR RLDQSIGKPS LFIPISEKSK DRGSNTIGAR LNRVEDKVTQ
LDQRLVIITD MLHQLLSMQQ GGPTCNSRSQ VVASNEGGSI NPELFLPSNS LPTYEQLTVP
QTGPDEGS
