KCNQ3_BOVIN
ID KCNQ3_BOVIN Reviewed; 866 AA.
AC P58126;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 3 {ECO:0000305};
DE AltName: Full=KQT-like 3;
DE AltName: Full=Potassium channel subunit alpha KvLQT3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.3;
GN Name=KCNQ3 {ECO:0000250|UniProtKB:O43525};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L.;
RT "Ion channels in ocular epithelia.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel
CC with essentially identical properties to the channel underlying the
CC native M-current, a slowly activating and deactivating potassium
CC conductance which plays a critical role in determining the subthreshold
CC electrical excitability of neurons as well as the responsiveness to
CC synaptic inputs. Therefore, it is important in the regulation of
CC neuronal excitability. {ECO:0000250|UniProtKB:O43525}.
CC -!- SUBUNIT: Heterotetramer with KCNQ2; form the heterotetrameric M
CC potassium channel. Interacts with calmodulin; the interaction is
CC calcium-independent, constitutive and participates in the proper
CC assembly of a functional heterotetrameric M channel. Heteromultimer
CC with KCNQ5. May associate with KCNE2. Interacts with IQCJ-SCHIP1 (By
CC similarity). {ECO:0000250|UniProtKB:O43525,
CC ECO:0000250|UniProtKB:Q8K3F6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43525};
CC Multi-pass membrane protein {ECO:0000255}.
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}.
CC -!- PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to
CC protein degradation. Degradation induced by NEDD4L is inhibited by
CC USP36. {ECO:0000250|UniProtKB:O43525}.
CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15)
CC subfamily. Kv7.3/KCNQ3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF325548; AAK11221.1; -; mRNA.
DR RefSeq; NP_776799.1; NM_174374.2.
DR AlphaFoldDB; P58126; -.
DR SMR; P58126; -.
DR STRING; 9913.ENSBTAP00000027546; -.
DR PaxDb; P58126; -.
DR PRIDE; P58126; -.
DR Ensembl; ENSBTAT00000027546; ENSBTAP00000027546; ENSBTAG00000020667.
DR GeneID; 281884; -.
DR KEGG; bta:281884; -.
DR CTD; 3786; -.
DR VEuPathDB; HostDB:ENSBTAG00000020667; -.
DR VGNC; VGNC:30488; KCNQ3.
DR eggNOG; KOG1419; Eukaryota.
DR GeneTree; ENSGT00940000159760; -.
DR HOGENOM; CLU_011722_8_2_1; -.
DR InParanoid; P58126; -.
DR OMA; QDRDDYM; -.
DR OrthoDB; 1168835at2759; -.
DR TreeFam; TF315186; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000020667; Expressed in prefrontal cortex and 34 other tissues.
DR ExpressionAtlas; P58126; baseline and differential.
DR GO; GO:0043194; C:axon initial segment; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR020969; Ankyrin-G_BS.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR InterPro; IPR003948; K_chnl_volt-dep_KCNQ3.
DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR PANTHER; PTHR11537:SF5; PTHR11537:SF5; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 1.
DR Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR PRINTS; PR01462; KCNQ3CHANNEL.
DR PRINTS; PR01459; KCNQCHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW Voltage-gated channel.
FT CHAIN 1..866
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 3"
FT /id="PRO_0000054033"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..225
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..247
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..303
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 304..324
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..330
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 331..351
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..537
FT /note="Mediates interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:O43525"
FT REGION 574..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 316..321
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 589..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88944"
SQ SEQUENCE 866 AA; 95645 MW; 43996161F07A0424 CRC64;
MGLKARRPAG AAGGGGDGGG GGGGAANPAG GDAAAAGDEE RKVGLAPGDV EQVTLALGAG
ADKDGTLLLE GGGRDEGQRR TPQGIGLLAK TPLSRPVKRN NAKYRRIQTL IYDALERPRG
WALLYHALVF LIVLGCLILA VLTTFREYET VSGDWLLLLE TFAIFIFGAE FALRIWAAGC
CCRYKGWRGR LKFARKPLCM LDIFVLIASV PVVAVGNQGN VLATSLRSLR FLQILRMLRM
DRRGGTWKLL GSAICAHSKE LITAWYIGFL TLILSSFLVY LVEKDVPEVD AQGEEMKEEF
ETYADALWWG LITLATIGYG DKTPKTWEGR LIAATFSLIG VSFFALPAGI LGSGLALKVQ
EQHRQKHFEK RRKPAAELIQ AAWRYYATNP NRIDLVATWR FYESVVSFPF FRKEQLDPAA
SQKLGLLDRV RLSNPRGSNT KGKLFTPLNV DAIEESPSKE PKPVGSNNKE RFRTAFRMKA
YAFWQSSEDA GTGDPTAEDR GYGNDFLIED MIPTLKAAIR AVRILQFRLY KKKFKETLRP
YDVKDVIEQY SAGHLDMLSR IKYLQTRIDM IFTPGPPSTP KHKKSQRGAA FTYPSQQSPR
NEPYVARPST SETEDQSMMG KFVKVERQVH DMGKKLDFLV DMHLQHMERL QVHVAGFSPS
KGASSPAEAE QKEDRRDADL KTIICNYSET GAPDAPYSFH QVPVDKVGPY GFFAHDPVNL
PLGGPSSGKG HATPYAERPT VLPILTLLDS RGSYRSQVEL HGPCSDRVSP RQRRSITRDS
DTPLSLMSVN HEELERSPSG FSISQDRDDY AFGPSGGSSW MREKRYLAEG ETDTDTEPFT
PSGSLPLSST GDGISDSIWT PSGKPT
