KCNQ3_RAT
ID KCNQ3_RAT Reviewed; 873 AA.
AC O88944; Q9Z240;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
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|RGD:69222};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Derst C., Preisig-Mueller R., Hennighausen A., Daut J.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9836639; DOI=10.1126/science.282.5395.1890;
RA Wang H.-S., Pan Z., Shi W., Brown B.S., Wymore R.S., Cohen I.S.,
RA Dixon J.E., McKinnon D.;
RT "KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-
RT channel.";
RL Science 282:1890-1893(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
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:0000269|PubMed:9836639}.
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:0000269|PubMed:9836639};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88944-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88944-2; Sequence=VSP_001012;
CC -!- TISSUE SPECIFICITY: Expressed in brain and sympathetic ganglia. In
CC brain, expressed in cortex, hippocampus and at much lower levels in
CC cerebellum. In sympathetic ganglia, expressed at approximately equal
CC levels in both superior cervical ganglia and prevertebral ganglia.
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; AF087454; AAC36723.2; -; mRNA.
DR EMBL; AF091247; AAC79846.1; -; mRNA.
DR RefSeq; NP_113785.3; NM_031597.4. [O88944-1]
DR AlphaFoldDB; O88944; -.
DR SMR; O88944; -.
DR CORUM; O88944; -.
DR STRING; 10116.ENSRNOP00000065354; -.
DR ChEMBL; CHEMBL5531; -.
DR DrugCentral; O88944; -.
DR GuidetoPHARMACOLOGY; 562; -.
DR iPTMnet; O88944; -.
DR PhosphoSitePlus; O88944; -.
DR PaxDb; O88944; -.
DR PRIDE; O88944; -.
DR Ensembl; ENSRNOT00000109659; ENSRNOP00000093985; ENSRNOG00000005206. [O88944-1]
DR GeneID; 29682; -.
DR KEGG; rno:29682; -.
DR UCSC; RGD:69222; rat. [O88944-1]
DR CTD; 3786; -.
DR RGD; 69222; Kcnq3.
DR eggNOG; KOG1419; Eukaryota.
DR GeneTree; ENSGT00940000159760; -.
DR InParanoid; O88944; -.
DR PhylomeDB; O88944; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:O88944; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Genevisible; O88944; RN.
DR GO; GO:0043194; C:axon initial segment; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; ISO:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0071242; P:cellular response to ammonium ion; IMP:RGD.
DR GO; GO:0061548; P:ganglion development; IEP:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IMP:RGD.
DR GO; GO:0060081; P:membrane hyperpolarization; ISO:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..873
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 3"
FT /id="PRO_0000054036"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0007744|PubMed:22673903"
FT VAR_SEQ 1..83
FT /note="MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVE
FT QVTLALGTGADKDGTLLLEGGGREEGQRRTP -> MALEFPGLQPPPPPRPRTPSAPSS
FT RSSSGEGEAPSGGEADGAQGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9836639"
FT /id="VSP_001012"
FT CONFLICT 654
FT /note="H -> R (in Ref. 2; AAC79846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 96898 MW; D77AF88088051E15 CRC64;
MGLKARRAAG AAGGGGGEGG GGGGGAANPA GGDSAVAGDE ERKVGLAPGD VEQVTLALGT
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 AGTGDPMTED RGYGNDFLIE DMIPTLKAAI RAVRILQFRL YKKKFKETLR
PYDVKDVIEQ YSAGHLDMLS RIKYLQTRID MIFTPGPPST PKHKKSQKGS AFTYPSQQSP
RNEPYVARAA TSETEDQSMM GKFVKVERQV HDMGKKLDFL VDMHMQHMER LQVHVTEYYP
TKGASSPAEG EKKEDNRYSD LKTIICNYSE SGPPDPPYSF HQVPIDRVGP YGFFAHDPVK
LTRGGPSSTK AQANLPSSGS TYAERPTVLP ILTLLDSCVS YHSQTELQGP YSDHISPRQR
RSITRDSDTP LSLMSVNHEE LERSPSGFSI SQDRDDYVFG PSGGSSWMRE KRYLAEGETD
TDTDPFTPSG SMPMSSTGDG ISDSIWTPSN KPT
