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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_CAVPO             Reviewed;         671 AA.
O70344; H0V4C0; Q9QYG3;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
20-JAN-2016, sequence version 3.
31-JAN-2018, entry version 108.
RecName: Full=Potassium voltage-gated channel subfamily KQT member 1 {ECO:0000250|UniProtKB:P51787};
AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000250|UniProtKB:P51787};
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:0000250|UniProtKB:P51787};
Synonyms=KVLQT1 {ECO:0000250|UniProtKB:P51787};
Cavia porcellus (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10141;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=2N;
PubMed=21993624; DOI=10.1038/nature10530;
Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
Pedersen J.S., Lander E.S., Kellis M.;
"A high-resolution map of human evolutionary constraint using 29
mammals.";
Nature 478:476-482(2011).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 155-253.
TISSUE=Heart;
Shi H., Wang Z.;
"Guinea pig cardiac KvLQT1 potassium channel mRNA.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 201-323.
TISSUE=Heart;
Ohya S., Imaizumi Y., Watanabe M.;
"Guinea-pig potassium channel (KvLQT1).";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Potassium channel that plays an important role in a
number of tissues, including heart, inner ear, stomach and colon
(By similarity). Associates with KCNE beta subunits that modulates
current kinetics (By similarity). Induces a voltage-dependent by
rapidly activating and slowly deactivating potassium-selective
outward current (By similarity). 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). 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 (By similarity).
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 (By similarity). When associated with
KCNE2, forms a 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 that has a
voltage-gated potassium channel activity (By similarity). Binds
with phosphatidylinositol 4,5-bisphosphate (By similarity).
{ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414,
ECO:0000250|UniProtKB:Q9Z0N7}.
-!- SUBUNIT: Tetramer. Heterotetramer with KCNE1; targets to the
membrane raft. Interacts (via C-terminus) with CALM; forms an
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 a 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.
{ECO:0000250|UniProtKB:P51787}.
-!- 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the potassium channel family. KQT (TC
1.A.1.15) subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AAKN02038603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAKN02038605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAKN02038604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF049341; AAC05498.1; -; mRNA.
EMBL; AB032574; BAA88579.1; -; mRNA.
ProteinModelPortal; O70344; -.
STRING; 10141.ENSCPOP00000004457; -.
BindingDB; O70344; -.
ChEMBL; CHEMBL5135; -.
Ensembl; ENSCPOT00000022911; ENSCPOP00000015076; ENSCPOG00000004952.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00550000074513; -.
InParanoid; O70344; -.
OMA; ERKRWGW; -.
OrthoDB; EOG091G02ZT; -.
TreeFam; TF315186; -.
Proteomes; UP000005447; Unassembled WGS sequence.
Bgee; ENSCPOG00000004952; -.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0034702; C:ion channel complex; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
GO; GO:0086009; P:membrane repolarization; ISS:UniProtKB.
GO; GO:0060453; P:regulation of gastric acid secretion; ISS:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0070293; P:renal absorption; ISS:UniProtKB.
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.
2: Evidence at transcript level;
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 1 671 Potassium voltage-gated channel subfamily
KQT member 1.
/FTId=PRO_0000054021.
TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.
TRANSMEM 123 143 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 144 148 Extracellular. {ECO:0000255}.
TRANSMEM 149 169 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 170 196 Cytoplasmic. {ECO:0000255}.
TRANSMEM 197 218 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 219 226 Extracellular. {ECO:0000255}.
TRANSMEM 227 249 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 250 262 Cytoplasmic. {ECO:0000255}.
TRANSMEM 263 283 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 284 300 Extracellular. {ECO:0000255}.
INTRAMEM 301 321 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 322 328 Extracellular. {ECO:0000255}.
TRANSMEM 329 349 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 350 671 Cytoplasmic. {ECO:0000255}.
REGION 536 573 Interaction with KCNE1 C-terminus.
{ECO:0000250|UniProtKB:P51787}.
REGION 589 617 Interaction with AKAP9.
{ECO:0000250|UniProtKB:P51787}.
REGION 590 621 C-terminal assembly domain.
{ECO:0000250|UniProtKB:P51787}.
COILED 586 621 {ECO:0000250|UniProtKB:P51787}.
MOTIF 313 318 Selectivity filter. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P51787}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 236 236 I -> S (in Ref. 2; AAC05498).
{ECO:0000305}.
SEQUENCE 671 AA; 74411 MW; 68B5ABCE83313557 CRC64;
MAAASSPPRT ERKRGGWGRL LGSRRGSASL AKKCPFSLEL AEGGPAGGTL YAPVAPPGAL
SPGSPAPPAS PAAPPAGLEL GPRPPVSLDP RVSIYSARRP LLARTHIQGR VYNFLERPTG
WKCFVYHFAV FLIVLACLIF SVLSTIEQYA ALATGTLFWM EIVLVVFFGT EYVVRLWSAG
CRSKYVGIWG RLRFARKPIS IIDLIVVVAS MVVLCVGSKG QVFATSAIRG IRFLQILRML
HVDRQGGTWR LLGSVVFIHR QELITTLYIG FLGLIFSSYF VYLAEKDAVN ESGRVEFGSY
ADALWWGVVT VTTIGYGDKV PQTWVGKTIA SCFSVFAISF FALPAGILGS GFALKVQQKQ
RQKHFNRQIP AAASLIQTAW RCYAAENPDS STWKIYVRKP ARSHTLLSPS PKPKKSAMVR
KKKFKPDKDN GVSPGEKMLT VPHITCDPPE ERRPDHFSVD GYDSSVRKSP TLLEVSPTHF
MRTNSFAEDL DLEGETLLTP ITHVSQLREH HRATIKVIRR MQYFVAKKKF QQARKPYDVR
DVIEQYSQGH LNLMVRIKEL QRRLDQSIGK PSLFIPISEK SKDRGSNTIG ARLNRVEDKV
TQLDQRLVVI TDMLHQLLSL HQGGPHSGGG PQMVQPCSED GSIHPELFLP SNSLPTYEQL
TVPQRGPDEA S


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