KCNQ1_XENLA
ID KCNQ1_XENLA Reviewed; 652 AA.
AC P70057; B1N659;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 1 {ECO:0000305};
DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha xKvLQT1 {ECO:0000305|PubMed:8900283};
DE AltName: Full=KQT-like 1 {ECO:0000250|UniProtKB:P51787};
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000250|UniProtKB:P51787};
GN Name=kcnq1 {ECO:0000303|PubMed:18453744};
GN Synonyms=kvlqt1 {ECO:0000305|PubMed:8900283};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18453744; DOI=10.1159/000129628;
RA Morokuma J., Blackiston D., Levin M.;
RT "KCNQ1 and KCNE1 K+ channel components are involved in early left-right
RT patterning in Xenopus laevis embryos.";
RL Cell. Physiol. Biochem. 21:357-372(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-401.
RC TISSUE=Oocyte;
RX PubMed=8900283; DOI=10.1038/384080a0;
RA Sanguinetti M.C., Curran M.E., Zou A., Shen J., Spector P.S.,
RA Atkinson D.L., Keating M.T.;
RT "Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks)
RT potassium channel.";
RL Nature 384:80-83(1996).
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 When associated with KCNE3, forms the potassium channel that is
CC important for cyclic AMP-stimulated intestinal secretion of chloride
CC ions (By similarity). When associated with KCNE2, forms a
CC heterooligomer complex leading to currents with an apparently
CC instantaneous activation, a rapid deactivation process and a linear
CC current-voltage relationship and decreases the amplitude of the outward
CC current (By similarity). When associated with KCNE4, inhibits voltage-
CC gated potassium channel activity (By similarity). When associated with
CC KCNE5, this complex only conducts current upon strong and continued
CC depolarization (By similarity). {ECO:0000250|UniProtKB:P51787,
CC ECO:0000250|UniProtKB:P97414, ECO:0000250|UniProtKB:Q9Z0N7}.
CC -!- SUBUNIT: Tetramer. Heterotetramer with KCNE1; targets to the membrane
CC raft. Interacts (via C-terminus) with CALM; forms an heterotetramer in
CC a calcium-independent manner. Interacts with KCNE2; form a
CC heterooligomer complex that targets to the membrane raft and leading to
CC currents with an apparently instantaneous activation, a rapid
CC deactivation process and a linear current-voltage relationship and
CC decreases the amplitude of the outward current. Interacts with KCNE3;
CC alters membrane raft localization. Interacts with KCNE4; impairs KCNQ1
CC localization in lipid rafts and inhibits voltage-gated potassium
CC channel activity. Interacts with KCNE5; impairs KCNQ1 localization in
CC lipid rafts and only conducts current upon strong and continued
CC depolarization. {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}. Membrane raft
CC {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane
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 segment S6 is involved in the inhibition of voltage-gated
CC potassium channel activity by KCNE4. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60042.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF078696; ABN41465.1; -; mRNA.
DR EMBL; U71076; AAC60042.1; ALT_INIT; mRNA.
DR RefSeq; NP_001116347.1; NM_001122875.1.
DR RefSeq; XP_018111889.1; XM_018256400.1.
DR PDB; 5VMS; EM; 3.70 A; A=66-610.
DR PDBsum; 5VMS; -.
DR AlphaFoldDB; P70057; -.
DR SMR; P70057; -.
DR GeneID; 373746; -.
DR KEGG; xla:373746; -.
DR CTD; 373746; -.
DR Xenbase; XB-GENE-5921471; kcnq1.L.
DR OMA; QTGPDEG; -.
DR OrthoDB; 1168835at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 373746; Expressed in heart and 19 other tissues.
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:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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: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: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 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell membrane; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..652
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 1"
FT /id="PRO_0000054028"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..214
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 266..286
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 393..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 278..283
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 74368 MW; 40F4C6BE9340D86A CRC64;
MSSEQPAWTF GLFTPDQNKQ APLEMNENAI NSLYEAIPLP QDGSSNGQRQ EDRQANSFEL
KRETLVATDP PRPTINLDPR VSIYSGRRPL LSRTNIQGRV YNFLERPTGW KCFVYHFTVF
LIVLICLIFS VLSTIQQYNN LATETLFWME IVLVVFFGAE YVVRLWSAGC RSKYVGVWGR
LRFARKPISV IDLIVVVASV IVLCVGSNGQ VFATSAIRGI RFLQILRMLH VDRQGGTWRL
LGSVVFIHRQ ELITTLYIGF LGLIFSSYFV YLAEKDAIDS SGEYQFGSYA DALWWGVVTV
TTIGYGDKVP QTWIGKTIAS CFSVFAISFF ALPAGILGSG FALKVQQKQR QKHFNRQIPA
AASLIQTAWR CYAAENPDSA TWKIYIRKQS RNHHLMSPSP KPKKSAMVKK KKIRTERDEG
STDKMLNIPH ITYDHVADDR KNDGYSVESY ENTVRKPFGF LDPSTGPFIR TSSFTDDLDM
EGDTLLTPIT HISELKEHHR AAIKVIRRMQ YFVAKKKFQQ ARKPYDVRDV IEQYSQGHLN
LMVRIKELQR RLDQSLGKPS LFLSVSDKVK DKGINTIGSR LNRVEDKVTQ MDHKLNLITD
MLHHLLTNQQ GSQSIRTPHR SNSLNSENHP SRNTLPTYEQ LNVPRMTQDN IS
