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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_SQUAC             Reviewed;         660 AA.
O73925;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
31-JAN-2018, entry version 94.
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:0000303|PubMed:9929573};
Squalus acanthias (Spiny dogfish).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
Elasmobranchii; Squalimorphii; Squaliformes; Squalidae; Squalus.
NCBI_TaxID=7797;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Rectal gland;
PubMed=9929573; DOI=10.1007/s004240050783;
Waldegger S., Fakler B., Bleich M., Barth P., Hopf A., Schulte U.,
Busch A.E., Aller S.G., Forrest J.N. Jr., Greger R., Lang F.;
"Molecular and functional characterization of s-KCNQ1 potassium
channel from rectal gland of Squalus acanthias.";
Pflugers Arch. 437:298-304(1999).
-!- 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). When associated
with KCNE3, forms the potassium channel that is important for
cyclic AMP-stimulated intestinal secretion of chloride ions (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).
{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
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 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}. Membrane raft
{ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P51787}.
-!- TISSUE SPECIFICITY: Expressed only in rectal gland and heart.
Faintly expressed in intestine. Undetectable in kidney, brain,
testis, liver and gills.
-!- 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}.
-!- 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; AJ223714; CAA11526.1; -; mRNA.
ProteinModelPortal; O73925; -.
HOVERGEN; HBG059014; -.
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: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; Cytoplasmic vesicle;
Endoplasmic reticulum; Ion channel; Ion transport; Membrane;
Potassium; Potassium channel; Potassium transport; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 660 Potassium voltage-gated channel subfamily
KQT member 1.
/FTId=PRO_0000054029.
TOPO_DOM 1 114 Cytoplasmic. {ECO:0000255}.
TRANSMEM 115 135 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 136 148 Extracellular. {ECO:0000255}.
TRANSMEM 149 169 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 170 195 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 282 292 Extracellular. {ECO:0000255}.
INTRAMEM 293 313 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 314 320 Extracellular. {ECO:0000255}.
TRANSMEM 321 341 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 342 660 Cytoplasmic. {ECO:0000255}.
COILED 579 615 {ECO:0000250|UniProtKB:P51787}.
MOTIF 305 310 Selectivity filter. {ECO:0000250}.
SEQUENCE 660 AA; 74687 MW; 73B416E88A08A352 CRC64;
MSSEVKSRWS GSGSQKSGTA RKPTMLEMAE NAASRHYEPV PLPLQRSNSP DSSTDKNPES
RAADSRAEVI INPDIPPKAI ALPLSRYRGR NPFFSKVNIQ GRTYNFLERP TGWKCFIYHF
TVFLIVLVCL IFSVMSTIEQ YHYFANRALV WMEIVLVVFF GTEYIVRLWS AGCRSKYVGF
WGRLRFARKP ISIIDLIVVV ASVIVLCVGS NGQVFATSAI RGIRFLQILR MLHVDRQGGT
WRLLGSVVFI HRQELITTLY IGFLGLIFSS YFVYLAEKDA VDDSGSQQFG SYADALWWGV
VTVTTIGYGD KVPQTWIGRT IASCFSVFAI SFFALPAGIL GSGFALKVQQ KQRQKHFNRQ
IPAAASLIQT SWRCHAAENH ESATWKMYVR QPTKFYVASP SPKTKKSVGK RKKLKTDKDN
GLNSEKSLNV PNITYDHVVD KDDRKFENSN IDGYDSSVKK SLGILDVNSG ALSRANSYAD
DLDFIEGEPV LAPITHVSQL RESHRVTVKV IRRMQYFVAK KKFQQARKPY DVRDVIEQYS
QGHLNLMVRI KELQRRLDQS LGKPTMFLSV SEKSQDRGKN TIGARLNRVE EKFVHMDQKL
NTITDMLHHL VAHQQGHPHP QTQPQAQGTV VQAVASTHSS LPSYEQLTVR RKDQDNQPDL


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