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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) (Fragment)

 KCNQ1_FELCA             Reviewed;         582 AA.
O97531; M3W6T1;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
20-JAN-2016, sequence version 2.
31-JAN-2018, entry version 100.
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};
Flags: Fragment;
Name=KCNQ1 {ECO:0000250|UniProtKB:P51787};
Synonyms=KVLQT1 {ECO:0000250|UniProtKB:P51787};
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian;
PubMed=17975172; DOI=10.1101/gr.6380007;
Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N.,
Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U.,
Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N.,
Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.;
"Initial sequence and comparative analysis of the cat genome.";
Genome Res. 17:1675-1689(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 104-275.
TISSUE=Heart;
Chen L.-S.K.;
"Expression of minK and KvLQT1 mRNA in cat tissues: a genetic evidence
for the cardiac IKs channel.";
Submitted (JUL-1997) 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: Phosphorylated 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; AANG02067979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG02067981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG02067980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AANG03336046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF013961; AAC98890.1; -; mRNA.
ProteinModelPortal; O97531; -.
STRING; 9685.ENSFCAP00000006446; -.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
HOVERGEN; HBG059014; -.
InParanoid; O97531; -.
OrthoDB; EOG091G02ZT; -.
Proteomes; UP000011712; Unplaced.
Bgee; ENSFCAG00000006943; -.
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:0016021; C:integral component of membrane; IBA:GO_Central.
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:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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 <1 582 Potassium voltage-gated channel subfamily
KQT member 1.
/FTId=PRO_0000054023.
TRANSMEM 33 53 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 54 58 Extracellular. {ECO:0000255}.
TRANSMEM 59 79 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 80 107 Cytoplasmic. {ECO:0000255}.
TRANSMEM 108 128 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 129 136 Extracellular. {ECO:0000255}.
TRANSMEM 137 159 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 160 172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 173 193 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 194 210 Extracellular. {ECO:0000255}.
INTRAMEM 211 231 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 232 238 Extracellular. {ECO:0000255}.
TRANSMEM 239 259 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 260 582 Cytoplasmic. {ECO:0000255}.
REGION 446 483 Interaction with KCNE1 C-terminus.
{ECO:0000250|UniProtKB:P51787}.
REGION 499 527 Interaction with AKAP9.
{ECO:0000250|UniProtKB:P51787}.
REGION 500 531 C-terminal assembly domain.
{ECO:0000250|UniProtKB:P51787}.
COILED 496 532 {ECO:0000250|UniProtKB:P51787}.
MOTIF 223 228 Selectivity filter. {ECO:0000250}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
NON_TER 1 1
SEQUENCE 582 AA; 65419 MW; 69CF20E75842C6C9 CRC64;
RVSIYSARRP LLARTHIQGR VYNFLERPTG WKCFVYHFAV FLIVLVCLIF SVLSTIEQYV
ALATGTLFWM EIVLVVFFGT EYVVRLWSAG CRSKYVGVWG RLRFARKPIS IIDLIVVLAS
MVVLCVGSKG QVFATSAIRG IRFLQILRML HVDRQGGTWR LLGSVVFIHR QELITTLYIG
FLGLIFSSYF VYLAEKDAVN ESGQVEFGSY ADALWWGVVT VTTIGYGDKV PQTWVGKTIA
SCFSVFAISF FALPAGILGS GFALKVQQKQ RQKHFNRQIP AAASLIQTAW RCYAAENPES
STWNIYVRKP TRSHTLLSPS PKPKKSVMVK KKKFKLDKDN GVSPGEKTLT VPHITCEPVS
EKRRPDHFSV DTCDSSVKSP MLLEVSTTHF LRTNSVAEDL DLEGETPLVP ITHVSQLREH
HRATIKVIRR MQYFVAKKKF QQARKPYDVR DVIEQYSQGH LNLMVRIKEL QRRLDQSIGK
PSLFISVSEK SKDRGSNTIG ARLNRVEDKV AQLDQRLVLI TDMLQQLLSL HHGGPPGSRP
PSGGGAQVQP CGPTNPELFL PGNALPTYEQ LTVPRRGPEE GS


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