KCNQ1_FELCA
ID KCNQ1_FELCA Reviewed; 582 AA.
AC O97531; M3W6T1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 1 {ECO:0000250|UniProtKB:P51787};
DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000250|UniProtKB:P51787};
DE AltName: Full=KQT-like 1 {ECO:0000250|UniProtKB:P51787};
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000250|UniProtKB:P51787};
DE Flags: Fragment;
GN Name=KCNQ1 {ECO:0000250|UniProtKB:P51787};
GN Synonyms=KVLQT1 {ECO:0000250|UniProtKB:P51787};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian;
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-275.
RC TISSUE=Heart;
RA Chen L.-S.K.;
RT "Expression of minK and KvLQT1 mRNA in cat tissues: a genetic evidence for
RT the cardiac IKs channel.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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 Associates with KCNE beta subunits that modulates current kinetics (By
CC similarity). Induces a voltage-dependent by rapidly activating and
CC slowly deactivating potassium-selective outward current (By
CC similarity). Promotes also a delayed voltage activated potassium
CC current showing outward rectification characteristic (By similarity).
CC During beta-adrenergic receptor stimulation participates in cardiac
CC repolarization by associating with KCNE1 to form the I(Ks) cardiac
CC potassium current that increases the amplitude and slows down the
CC activation kinetics of outward potassium current I(Ks) (By similarity).
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 (By similarity). 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 (By
CC similarity). When associated with KCNE2, forms a heterooligomer complex
CC leading to currents with an apparently instantaneous activation, a
CC rapid deactivation process and a linear current-voltage relationship
CC and decreases the amplitude of the outward current (By similarity).
CC When associated with KCNE4, inhibits voltage-gated potassium channel
CC activity (By similarity). When associated with KCNE5, this complex only
CC conducts current upon strong and continued depolarization (By
CC similarity). Also forms a heterotetramer with KCNQ5 that has a voltage-
CC gated potassium channel activity (By similarity). Binds with
CC phosphatidylinositol 4,5-bisphosphate (By similarity).
CC {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414,
CC ECO:0000250|UniProtKB:Q9Z0N7}.
CC -!- SUBUNIT: Tetramer. Heterotetramer with KCNE1; targets to the membrane
CC raft. Interacts (via C-terminus) with CALM; forms a heterooctameric
CC structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent
CC manner. Interacts with AKAP9; targets protein kinase A (PKA) catalytic
CC and regulatory subunits and protein phosphatase 1 (PP1) to the KCNQ1-
CC KCNE1 complex, allowing PKA-mediated phosphorylation and increase of
CC delayed rectifier potassium channel activity. Interacts with KCNE2;
CC form a heterooligomer complex that targets to the membrane raft and
CC leading to currents with an apparently instantaneous activation, a
CC rapid deactivation process and a linear current-voltage relationship
CC and decreases the amplitude of the outward current. Interacts with
CC AP2M1; mediates estrogen-induced internalization via clathrin-coated
CC vesicles. Interacts with NEDD4L; promotes internalization and decreases
CC I(Ks) currents. Interacts with USP2; counteracts the NEDD4L-specific
CC down-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.
CC {ECO:0000250|UniProtKB:P51787}.
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 -!- 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: Phosphorylated by PKA; increases delayed rectifier potassium
CC channel activity of the KCNQ1-KCNE1 complex through a macromolecular
CC complex that includes PKA, PP1, and the targeting protein AKAP9.
CC {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 -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15)
CC subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}.
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DR EMBL; AANG02067979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG02067981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG02067980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AANG03336046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF013961; AAC98890.1; -; mRNA.
DR AlphaFoldDB; O97531; -.
DR SMR; O97531; -.
DR STRING; 9685.ENSFCAP00000006446; -.
DR eggNOG; KOG1419; Eukaryota.
DR InParanoid; O97531; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0034702; C:ion channel complex; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
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:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IBA:GO_Central.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IBA:GO_Central.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
DR GO; GO:0086009; P:membrane repolarization; ISS:UniProtKB.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IBA:GO_Central.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0060453; P:regulation of gastric acid secretion; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0070293; P:renal absorption; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Calmodulin-binding; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN <1..582
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 1"
FT /id="PRO_0000054023"
FT TRANSMEM 33..53
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..159
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 211..231
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 281..293
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 426..440
FT /note="Interaction with CALM; calcium-dependent"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 446..483
FT /note="Interaction with KCNE1 C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 499..527
FT /note="Interaction with AKAP9"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 500..531
FT /note="C-terminal assembly domain"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 530..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 496..532
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT MOTIF 223..228
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97414"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97414"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ 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
