KCNQ1_SQUAC
ID KCNQ1_SQUAC Reviewed; 660 AA.
AC O73925;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
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};
GN Name=KCNQ1 {ECO:0000303|PubMed:9929573};
OS Squalus acanthias (Spiny dogfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Squalomorphii; Squaliformes; Squalidae; Squalus.
OX NCBI_TaxID=7797;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Rectal gland;
RX PubMed=9929573; DOI=10.1007/s004240050783;
RA Waldegger S., Fakler B., Bleich M., Barth P., Hopf A., Schulte U.,
RA Busch A.E., Aller S.G., Forrest J.N. Jr., Greger R., Lang F.;
RT "Molecular and functional characterization of s-KCNQ1 potassium channel
RT from rectal gland of Squalus acanthias.";
RL Pflugers Arch. 437:298-304(1999).
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 -!- TISSUE SPECIFICITY: Expressed only in rectal gland and heart. Faintly
CC expressed in intestine. Undetectable in kidney, brain, testis, liver
CC and gills.
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 -!- 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; AJ223714; CAA11526.1; -; mRNA.
DR AlphaFoldDB; O73925; -.
DR SMR; O73925; -.
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 2: Evidence at transcript level;
KW Calmodulin-binding; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..660
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 1"
FT /id="PRO_0000054029"
FT TOPO_DOM 1..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..247
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 293..313
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 579..615
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT MOTIF 305..310
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
