KCNQ3_MOUSE
ID KCNQ3_MOUSE Reviewed; 873 AA.
AC Q8K3F6; E9QJY5;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
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:0000312|MGI:MGI:1336181};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Isbrandt D., Peters H.C., Pongs O.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH IQCJ-SCHIP1.
RX PubMed=27979964; DOI=10.1074/jbc.m116.758029;
RA Martin P.M., Cifuentes-Diaz C., Devaux J., Garcia M., Bureau J.,
RA Thomasseau S., Klingler E., Girault J.A., Goutebroze L.;
RT "Schwannomin-interacting protein 1 isoform IQCJ-SCHIP1 is a multipartner
RT ankyrin- and spectrin-binding protein involved in the organization of nodes
RT of Ranvier.";
RL J. Biol. Chem. 292:2441-2456(2017).
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
CC (PubMed:27979964). {ECO:0000250|UniProtKB:O43525,
CC ECO:0000269|PubMed:27979964}.
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; AY118171; AAM81579.1; -; mRNA.
DR EMBL; AC091276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49619.1; -.
DR RefSeq; NP_690887.2; NM_152923.2.
DR AlphaFoldDB; Q8K3F6; -.
DR SMR; Q8K3F6; -.
DR BioGRID; 225968; 6.
DR IntAct; Q8K3F6; 1.
DR STRING; 10090.ENSMUSP00000063380; -.
DR iPTMnet; Q8K3F6; -.
DR PhosphoSitePlus; Q8K3F6; -.
DR SwissPalm; Q8K3F6; -.
DR PaxDb; Q8K3F6; -.
DR PRIDE; Q8K3F6; -.
DR ProteomicsDB; 263417; -.
DR Antibodypedia; 14124; 158 antibodies from 24 providers.
DR DNASU; 110862; -.
DR Ensembl; ENSMUST00000070256; ENSMUSP00000063380; ENSMUSG00000056258.
DR GeneID; 110862; -.
DR KEGG; mmu:110862; -.
DR UCSC; uc007wab.2; mouse.
DR CTD; 3786; -.
DR MGI; MGI:1336181; Kcnq3.
DR VEuPathDB; HostDB:ENSMUSG00000056258; -.
DR eggNOG; KOG1419; Eukaryota.
DR GeneTree; ENSGT00940000159760; -.
DR HOGENOM; CLU_011722_8_2_1; -.
DR InParanoid; Q8K3F6; -.
DR OMA; QDRDDYM; -.
DR OrthoDB; 1168835at2759; -.
DR PhylomeDB; Q8K3F6; -.
DR TreeFam; TF315186; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 110862; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Kcnq3; mouse.
DR PRO; PR:Q8K3F6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8K3F6; protein.
DR Bgee; ENSMUSG00000056258; Expressed in medial geniculate body and 120 other tissues.
DR Genevisible; Q8K3F6; MM.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
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:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0005516; F:calmodulin binding; IPI:MGI.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IMP:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IGI:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0071242; P:cellular response to ammonium ion; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0060081; P:membrane hyperpolarization; IMP:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:MGI.
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 1: Evidence at protein 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..873
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 3"
FT /id="PRO_0000054035"
FT TOPO_DOM 1..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..248
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 305..325
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..538
FT /note="Mediates interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:O43525"
FT REGION 575..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 317..322
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 580..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88944"
FT CONFLICT 7
FT /note="R -> T (in Ref. 1; AAM81579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 96852 MW; EB98ABA9BE87E3A7 CRC64;
MGLKARRAAG AAGGGGGEGG GGGGGAANPA GGDSAVAGDE ERKVGLAPGD VEQVTLALGA
GADKDGTLLL EGGGREEGQR RTPQGIGLLA KTPLSRPVKR NNAKYRRIQT LIYDALERPR
GWALLYHALV FLIVLGCLIL AVLTTFKEYE TVSGDWLLLL ETFAIFIFGA EFALRIWAAG
CCCRYKGWRG RLKFARKPLC MLDIFVLIAS VPVVAVGNQG NVLATSLRSL RFLQILRMLR
MDRRGGTWKL LGSAICAHSK ELITAWYIGF LTLILSSFLV YLVEKDVPEM DAQGEEMKEE
FETYADALWW GLITLATIGY GDKTPKTWEG RLIAATFSLI GVSFFALPAG ILGSGLALKV
QEQHRQKHFE KRRKPAAELI QAAWRYYATN PNRLDLVATW RFYESVVSFP FFRKEQLEAA
ASQKLGLLDR VRLSNPRGSN TKGKLFTPLN VDAIEESPSK EPKPVGLNNK ERFRTAFRMK
AYAFWQSSED AGTGDPMAED RGYGNDFLIE DMIPTLKAAI RAVRILQFRL YKKKFKETLR
PYDVKDVIEQ YSAGHLDMLS RIKYLQTRID MIFTPGPPST PKHKKSQKGS AFTYPSQQSP
RNEPYVARAA TSETEDQSMM GKFVKVERQV HDMGKKLDFL VDMHMQHMER LQVHVTEYYP
TKGASSPAEG EKKEDNRYSD LKTIICNYSE TGPPDPPYSF HQVPIDRVGP YGFFAHDPVK
LTRGGPSSTK AQANLPSSGS TYAERPTVLP ILTLLDSCVS YHSQTELQGP YSDHISPRQR
RSITRDSDTP LSLMSVNHEE LERSPSGFSI SQDRDDYVFG PSGGSSWMRE KRYLAEGETD
TDTDPFTPSG SMPMSSTGDG ISDSIWTPSN KPT
