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1.A.1.15.3
6 TMS voltage-gated K+ channel, KCNQ3 or Kv7.3.  Mutations cause benign familial neonatal convulsions (BNFC; epilepsy; Maljevic et al. 2016). Forms homotetramers or heterotetramers with KCNQ2 (Soldovieri et al., 2006; Uehara et al., 2008).  Retigabine and ICA73, two anti-epileptic drugs, act via distinct mechanisms due to interactions with specific residues that underlie subtype specificity of KCNQ channel openers (Wang et al. 2016).

Accession Number:O43525
Protein Name:KCNQ3
Length:872
Molecular Weight:96742.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate K+

Cross database links:

Genevestigator: O43525
HEGENOM: HBG714141
RefSeq: NP_004510.1   
Entrez Gene ID: 3786   
Pfam: PF00520    PF03520    PF11956   
Drugbank: Drugbank Link   
OMIM: 121201  phenotype
602232  gene
KEGG: hsa:3786   

Gene Ontology

GO:0008076 C:voltage-gated potassium channel complex
GO:0005249 F:voltage-gated potassium channel activity
GO:0006813 P:potassium ion transport
GO:0007268 P:synaptic transmission
GO:0055085 P:transmembrane transport

References (15)

[1] “Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy.”  Schroeder B.C.et.al.   9872318
[2] “A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family.”  Charlier C.et.al.   9425900
[3] “Functional expression of two KvLQT1-related potassium channels responsible for an inherited idiopathic epilepsy.”  Yang W.-P.et.al.   9677360
[4] “Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute to the M-like current in a mammalian neuronal cell.”  Selyanko A.A.et.al.   10479678
[5] “M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2 subunit.”  Tinel N.et.al.   11034315
[6] “Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy.”  Schwake M.et.al.   10788442
[7] “Reconstitution of muscarinic modulation of the KCNQ2/KCNQ3 K(+) channels that underlie the neuronal M current.”  Shapiro M.S.et.al.   10684873
[8] “Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors.”  Selyanko A.A.et.al.   10713961
[9] “Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine.”  Main M.J.et.al.   10908292
[10] “Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3 potassium channels.”  Wickenden A.D.et.al.   10953053
[11] “The novel anticonvulsant retigabine activates M-currents in Chinese hamster ovary-cells tranfected with human KCNQ2/3 subunits.”  Rundfeldt C.et.al.   10713399
[12] “Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells.”  Wickenden A.D.et.al.   11159685
[13] “Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.”  Yu L.-R.et.al.   17924679
[14] “A novel mutation of KCNQ3 (c.925T-->C) in a Japanese family with benign familial neonatal convulsions.”  Hirose S.et.al.   10852552
[15] “KCNQ2 and KCNQ3 potassium channel genes in benign familial neonatal convulsions: expansion of the functional and mutation spectrum.”  Singh N.A.et.al.   14534157

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGLKARRAAG AAGGGGDGGG GGGGAANPAG GDAAAAGDEE RKVGLAPGDV EQVTLALGAG 
61:	ADKDGTLLLE GGGRDEGQRR TPQGIGLLAK TPLSRPVKRN NAKYRRIQTL IYDALERPRG 
121:	WALLYHALVF LIVLGCLILA VLTTFKEYET VSGDWLLLLE TFAIFIFGAE FALRIWAAGC 
181:	CCRYKGWRGR LKFARKPLCM LDIFVLIASV PVVAVGNQGN VLATSLRSLR FLQILRMLRM 
241:	DRRGGTWKLL GSAICAHSKE LITAWYIGFL TLILSSFLVY LVEKDVPEVD AQGEEMKEEF 
301:	ETYADALWWG LITLATIGYG DKTPKTWEGR LIAATFSLIG VSFFALPAGI LGSGLALKVQ 
361:	EQHRQKHFEK RRKPAAELIQ AAWRYYATNP NRIDLVATWR FYESVVSFPF FRKEQLEAAS 
421:	SQKLGLLDRV RLSNPRGSNT KGKLFTPLNV DAIEESPSKE PKPVGLNNKE RFRTAFRMKA 
481:	YAFWQSSEDA GTGDPMAEDR GYGNDFPIED MIPTLKAAIR AVRILQFRLY KKKFKETLRP 
541:	YDVKDVIEQY SAGHLDMLSR IKYLQTRIDM IFTPGPPSTP KHKKSQKGSA FTFPSQQSPR 
601:	NEPYVARPST SEIEDQSMMG KFVKVERQVQ DMGKKLDFLV DMHMQHMERL QVQVTEYYPT 
661:	KGTSSPAEAE KKEDNRYSDL KTIICNYSET GPPEPPYSFH QVTIDKVSPY GFFAHDPVNL 
721:	PRGGPSSGKV QATPPSSATT YVERPTVLPI LTLLDSRVSC HSQADLQGPY SDRISPRQRR 
781:	SITRDSDTPL SLMSVNHEEL ERSPSGFSIS QDRDDYVFGP NGGSSWMREK RYLAEGETDT 
841:	DTDPFTPSGS MPLSSTGDGI SDSVWTPSNK PI