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Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1)

 KCNQ1_MOUSE             Reviewed;         668 AA.
P97414; O88702; Q3U4H1; Q7TNZ1; Q7TPL7; Q80VR7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
12-SEP-2018, entry version 166.
RecName: Full=Potassium voltage-gated channel subfamily KQT member 1;
AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000305|PubMed:11120752};
AltName: Full=KQT-like 1 {ECO:0000250|UniProtKB:P51787};
AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000250|UniProtKB:P51787};
Name=Kcnq1 {ECO:0000312|MGI:MGI:108083};
Synonyms=Kcna9 {ECO:0000312|MGI:MGI:108083},
Kvlqt1 {ECO:0000303|PubMed:11120752};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), FUNCTION, AND DISRUPTION
PHENOTYPE.
STRAIN=129/SvJ; TISSUE=Heart;
PubMed=15004216; DOI=10.1124/jpet.103.063743;
Knollmann B.C., Casimiro M.C., Katchman A.N., Sirenko S.G.,
Schober T., Rong Q., Pfeifer K., Ebert S.N.;
"Isoproterenol exacerbates a long QT phenotype in Kcnq1-deficient
neonatal mice: possible roles for human-like Kcnq1 isoform 1 and slow
delayed rectifier K+ current.";
J. Pharmacol. Exp. Ther. 310:311-318(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
STRAIN=FVB/N; TISSUE=Colon, and Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-668 (ISOFORM I), FUNCTION, AND
INTERACTION WITH KCNE1.
TISSUE=Heart;
PubMed=8900282; DOI=10.1038/384078a0;
Barhanin J., Lesage F., Guillemare E., Fink M., Lazdunski M.,
Romey G.;
"K(V)LQT1 and IsK (minK) proteins associate to form the I(Ks) cardiac
potassium current.";
Nature 384:78-80(1996).
[5]
PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM II), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=9618174; DOI=10.1093/hmg/7.7.1149;
Paulsen M., Davies K.R., Bowden L.M., Villar A.J., Franck O.,
Fuermann M., Dean W.L., Moore T.F., Rodrigues N., Davies K.E.,
Hu R.-J., Feinberg A.P., Maher E.R., Reik W., Walter J.;
"Syntenic organization of the mouse distal chromosome 7 imprinting
cluster and the Beckwith-Wiedemann syndrome region in chromosome
11p15.5.";
Hum. Mol. Genet. 7:1149-1159(1998).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11120752; DOI=10.1172/JCI10897;
Lee M.P., Ravenel J.D., Hu R.J., Lustig L.R., Tomaselli G.,
Berger R.D., Brandenburg S.A., Litzi T.J., Bunton T.E., Limb C.,
Francis H., Gorelikow M., Gu H., Washington K., Argani P.,
Goldenring J.R., Coffey R.J., Feinberg A.P.;
"Targeted disruption of the Kvlqt1 gene causes deafness and gastric
hyperplasia in mice.";
J. Clin. Invest. 106:1447-1455(2000).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=16314573; DOI=10.1073/pnas.0505860102;
Vallon V., Grahammer F., Volkl H., Sandu C.D., Richter K.,
Rexhepaj R., Gerlach U., Rong Q., Pfeifer K., Lang F.;
"KCNQ1-dependent transport in renal and gastrointestinal epithelia.";
Proc. Natl. Acad. Sci. U.S.A. 102:17864-17869(2005).
[8]
FUNCTION.
PubMed=17597584; DOI=10.1016/j.bbrc.2007.06.038;
Knollmann B.C., Sirenko S., Rong Q., Katchman A.N., Casimiro M.,
Pfeifer K., Ebert S.N.;
"Kcnq1 contributes to an adrenergic-sensitive steady-state K+ current
in mouse heart.";
Biochem. Biophys. Res. Commun. 360:212-218(2007).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19491250; DOI=10.1113/jphysiol.2009.173302;
Song P., Groos S., Riederer B., Feng Z., Krabbenhoeft A., Smolka A.,
Seidler U.;
"KCNQ1 is the luminal K+ recycling channel during stimulation of
gastric acid secretion.";
J. Physiol. (Lond.) 587:3955-3965(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-408, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Potassium channel that plays an important role in a
number of tissues, including heart, inner ear, stomach and colon
(By similarity) (PubMed:16314573, PubMed:11120752,
PubMed:15004216). Associates with KCNE beta subunits that
modulates current kinetics (By similarity) (PubMed:17597584,
PubMed:15004216). Induces a voltage-dependent by rapidly
activating and slowly deactivating potassium-selective outward
current (By similarity) (PubMed:8900282). Promotes also a delayed
voltage activated potassium current showing outward rectification
characteristic (By similarity). During beta-adrenergic receptor
stimulation participates in cardiac repolarization by associating
with KCNE1 to form the I(Ks) cardiac potassium current that
increases the amplitude and slows down the activation kinetics of
outward potassium current I(Ks) (By similarity) (PubMed:15004216,
PubMed:17597584). Muscarinic agonist oxotremorine-M strongly
suppresses KCNQ1/KCNE1 current (By similarity). When associated
with KCNE3, forms the potassium channel that is important for
cyclic AMP-stimulated intestinal secretion of chloride ions (By
similarity). This interaction with KCNE3 is reduced by 17beta-
estradiol, resulting in the reduction of currents (By similarity).
During conditions of increased substrate load, maintains the
driving force for proximal tubular and intestinal sodium ions
absorption, gastric acid secretion, and cAMP-induced jejunal
chloride ions secretion (PubMed:16314573). Allows the provision of
potassium ions to the luminal membrane of the secretory
canaliculus in the resting state as well as during stimulated acid
secretion (PubMed:19491250). When associated with KCNE2, forms an
heterooligomer complex leading to currents with an apparently
instantaneous activation, a rapid deactivation process and a
linear current-voltage relationship and decreases the amplitude of
the outward current (By similarity). When associated with KCNE4,
inhibits voltage-gated potassium channel activity (By similarity).
When associated with KCNE5, this complex only conducts current
upon strong and continued depolarization (By similarity). Also
forms a heterotetramer with KCNQ5; has a voltage-gated potassium
channel activity (By similarity). Binds with phosphatidylinositol
4,5-bisphosphate (By similarity). {ECO:0000250|UniProtKB:P51787,
ECO:0000250|UniProtKB:Q9Z0N7, ECO:0000269|PubMed:11120752,
ECO:0000269|PubMed:15004216, ECO:0000269|PubMed:16314573,
ECO:0000269|PubMed:17597584, ECO:0000269|PubMed:19491250,
ECO:0000269|PubMed:8900282}.
-!- SUBUNIT: Tetramer (By similarity). Heterotetramer with KCNE1; form
the native cardiac channel I(Ks) which increases the amplitude and
slows down the activation kinetics of outward potassium current
and targets to the membrane raft (By similarity) (PubMed:8900282).
Interacts (via C-terminus) with CALM; forms a heterotetramer in a
calcium-independent manner. Interacts with AKAP9; targets protein
kinase A (PKA) catalytic and regulatory subunits and protein
phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex, allowing PKA-
mediated phosphorylation and increase of delayed rectifier
potassium channel activity. Interacts with KCNE2; form an
heterooligomer complex that targets to the membrane raft and
leading to currents with an apparently instantaneous activation, a
rapid deactivation process and a linear current-voltage
relationship and decreases the amplitude of the outward current.
Interacts with AP2M1; mediates estrogen-induced internalization
via clathrin-coated vesicles. Interacts with NEDD4L; promotes
internalization and decreases I(Ks) currents. Interacts with USP2;
counteracts the NEDD4L-specific down-regulation of I(Ks) and
restore plasma membrane localization. Heterotetramer with KCNQ5;
has a voltage-gated potassium channel activity. Interacts with
KCNE3; alters membrane raft localization. Interacts with KCNE4;
impairs KCNQ1 localization in lipid rafts and inhibits voltage-
gated potassium channel activity. Interacts with KCNE5; impairs
KCNQ1 localization in lipid rafts and only conducts current upon
strong and continued depolarization (By similarity).
{ECO:0000250|UniProtKB:P51787, ECO:0000269|PubMed:8900282}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:P51787}. Early endosome
{ECO:0000250|UniProtKB:P51787}. Membrane raft
{ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the
plasma membrane. Upon 17beta-oestradiol treatment, colocalizes
with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly
retained at the endoplasmic reticulum and is localized outside of
lipid raft microdomains. During the early stages of epithelial
cell polarization induced by the calcium switch it removed from
plasma membrane to the endoplasmic reticulum where it retained and
it is redistributed to the basolateral cell surface in a PI3K-
dependent manner at a later stage. {ECO:0000250|UniProtKB:P51787}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=I;
IsoId=P97414-1; Sequence=Displayed;
Name=II;
IsoId=P97414-2; Sequence=VSP_011748, VSP_000983;
-!- TISSUE SPECIFICITY: Expressed in heart, kidney and salivary
glands. Detected in the cochlea. Almost undetectable in brain,
skeletal muscle and liver. Widely expressed in embryonic and
neonatal tissues. {ECO:0000269|PubMed:9618174}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position. {ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The coiled-coil domain mediates tetramerization.
{ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The segment S6 is involved in the inhibition of voltage-
gated potassium channel activity by KCNE4.
{ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The C-terminal assembly domain promotes self-interactiona;
allows functional channel. {ECO:0000250|UniProtKB:P51787}.
-!- PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier
potassium channel activity of the KCNQ1-KCNE1 complex through a
macromolecular complex that includes PKA, PP1, and the targeting
protein AKAP9. {ECO:0000250|UniProtKB:P51787}.
-!- PTM: Ubiquitinated by NEDD4L; promotes internalization. The
ubiquitinylated form is internalized through a clathrin-mediated
endocytosis by interacting with AP2M1 and is recycled back to the
cell membrane via RAB4A and RAB11A.
{ECO:0000250|UniProtKB:P51787}.
-!- PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific
down-regulation of I(Ks) and restores the membrane localization.
{ECO:0000250|UniProtKB:P51787}.
-!- DISRUPTION PHENOTYPE: Mice lacking Kcnq1 show an intestinal
absorption impairment which is associated with reduced serum
vitamin B12 concentrations, mild macrocytic anemia, and fecal loss
of sodium and potassium ions (PubMed:16314573). Mice lacking Kcnq1
show microvillar secretory membranes intact, but basal acid
secretion is absent and forskolin-stimulated acid output is
reduced by approximately 90% in gastric mucosa (PubMed:19491250).
Homozygous Kcnq1 mice develop normally and are viable, demonstrate
hyperactivity, circling, and nodding behaviors; exhibit no
electrocardiographic abnormalities but present a complete
deafness, as well as circular movement and repetitive falling;
show severe anatomic disruption of the cochlear and vestibular end
organs; also display threefold enlargement by weight of the
stomach resulting from mucous neck cell hyperplasia
(PubMed:11120752). Mice neonates lacking Kcnq1 display
significantly prolonged QT intervals during baseline ECG
assessments which significantly increased following isoproterenol
challenge; furthermore, the slow delayed rectifier potassium
current (IKs) is absent (PubMed:15004216).
{ECO:0000269|PubMed:11120752, ECO:0000269|PubMed:15004216,
ECO:0000269|PubMed:16314573, ECO:0000269|PubMed:19491250}.
-!- SIMILARITY: Belongs to the potassium channel family. KQT (TC
1.A.1.15) subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB36518.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY331142; AAP93874.1; -; mRNA.
EMBL; AK154244; BAE32460.1; -; mRNA.
EMBL; BC045142; AAH45142.2; -; mRNA.
EMBL; BC055304; AAH55304.1; -; mRNA.
EMBL; U70068; AAB36518.1; ALT_INIT; mRNA.
EMBL; AJ002201; CAA05246.1; -; mRNA.
CCDS; CCDS22039.1; -. [P97414-1]
RefSeq; NP_032460.2; NM_008434.2. [P97414-1]
UniGene; Mm.439769; -.
UniGene; Mm.453036; -.
UniGene; Mm.453037; -.
ProteinModelPortal; P97414; -.
SMR; P97414; -.
ComplexPortal; CPX-3274; KCNQ1-KCNE1 I(Ks) channel complex.
IntAct; P97414; 117.
STRING; 10090.ENSMUSP00000009689; -.
GuidetoPHARMACOLOGY; 560; -.
TCDB; 1.A.1.15.1; the voltage-gated ion channel (vic) superfamily.
iPTMnet; P97414; -.
PhosphoSitePlus; P97414; -.
MaxQB; P97414; -.
PaxDb; P97414; -.
PeptideAtlas; P97414; -.
PRIDE; P97414; -.
Ensembl; ENSMUST00000009689; ENSMUSP00000009689; ENSMUSG00000009545. [P97414-1]
GeneID; 16535; -.
KEGG; mmu:16535; -.
UCSC; uc009kpb.1; mouse. [P97414-1]
CTD; 3784; -.
MGI; MGI:108083; Kcnq1.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00550000074513; -.
HOGENOM; HOG000220839; -.
HOVERGEN; HBG059014; -.
InParanoid; P97414; -.
KO; K04926; -.
OMA; ERKRWGW; -.
OrthoDB; EOG091G02ZT; -.
TreeFam; TF315186; -.
Reactome; R-MMU-1296072; Voltage gated Potassium channels.
Reactome; R-MMU-5576890; Phase 3 - rapid repolarisation.
Reactome; R-MMU-5576893; Phase 2 - plateau phase.
ChiTaRS; Kcnq1; mouse.
PRO; PR:P97414; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000009545; Expressed in 147 organ(s), highest expression level in stria vascularis of cochlear duct.
ExpressionAtlas; P97414; baseline and differential.
Genevisible; P97414; MM.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0034702; C:ion channel complex; ISS:UniProtKB.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0042383; C:sarcolemma; ISO:MGI.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
GO; GO:0042589; C:zymogen granule membrane; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; ISO:MGI.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0005267; F:potassium channel activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISO:MGI.
GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; ISO:MGI.
GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:MGI.
GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:MGI.
GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
GO; GO:0072358; P:cardiovascular system development; IMP:MGI.
GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
GO; GO:0035690; P:cellular response to drug; ISO:MGI.
GO; GO:0016458; P:gene silencing; IMP:MGI.
GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
GO; GO:0086009; P:membrane repolarization; IMP:UniProtKB.
GO; GO:0086011; P:membrane repolarization during action potential; ISO:MGI.
GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:MGI.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:MGI.
GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:MGI.
GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISO:MGI.
GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; ISO:MGI.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:MGI.
GO; GO:0060454; P:positive regulation of gastric acid secretion; ISO:MGI.
GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
GO; GO:0071435; P:potassium ion export; ISO:MGI.
GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
GO; GO:0006813; P:potassium ion transport; ISO:MGI.
GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:MGI.
GO; GO:0060453; P:regulation of gastric acid secretion; IMP:UniProtKB.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:MGI.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
GO; GO:0070293; P:renal absorption; IMP:UniProtKB.
GO; GO:0072347; P:response to anesthetic; ISO:MGI.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
InterPro; IPR005827; K_chnl_volt-dep_KCQN1.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR11537; PTHR11537; 1.
PANTHER; PTHR11537:SF109; PTHR11537:SF109; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF03520; KCNQ_channel; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01460; KCNQ1CHANNEL.
PRINTS; PR01459; KCNQCHANNEL.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Cell membrane; Coiled coil;
Complete proteome; Cytoplasmic vesicle; Endoplasmic reticulum;
Endosome; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Potassium; Potassium channel; Potassium transport;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; Voltage-gated channel.
CHAIN 1 668 Potassium voltage-gated channel subfamily
KQT member 1.
/FTId=PRO_0000054024.
TOPO_DOM 1 120 Cytoplasmic. {ECO:0000255}.
TRANSMEM 121 141 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 142 146 Extracellular. {ECO:0000255}.
TRANSMEM 147 167 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 168 195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 196 216 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 217 224 Extracellular. {ECO:0000255}.
TRANSMEM 225 247 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 248 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 282 298 Extracellular. {ECO:0000255}.
INTRAMEM 299 319 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 320 330 Extracellular. {ECO:0000255}.
TRANSMEM 331 351 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 352 668 Cytoplasmic. {ECO:0000255}.
REGION 534 571 Interaction with KCNE1 C-terminus.
{ECO:0000250|UniProtKB:P51787}.
REGION 587 615 Interaction with AKAP9.
{ECO:0000250|UniProtKB:P51787}.
REGION 588 619 C-terminal assembly domain.
{ECO:0000250|UniProtKB:P51787}.
COILED 584 620 {ECO:0000250|UniProtKB:P51787}.
MOTIF 311 316 Selectivity filter. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P51787}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 111 Missing (in isoform II). {ECO:0000305}.
/FTId=VSP_011748.
VAR_SEQ 112 128 FLERPTGWKCFVYHFTV -> MHQLPTSILIPKNMPGG
(in isoform II). {ECO:0000305}.
/FTId=VSP_000983.
CONFLICT 473 473 V -> L (in Ref. 1; AAP93874 and 4;
AAB36518). {ECO:0000305}.
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


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