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Identification
HMDB Protein ID HMDBP10841
Secondary Accession Numbers
  • 17131
Name Potassium voltage-gated channel subfamily KQT member 3
Synonyms
  1. KQT-like 3
  2. Potassium channel subunit alpha KvLQT3
  3. Voltage-gated potassium channel subunit Kv7.3
Gene Name KCNQ3
Protein Type Unknown
Biological Properties
General Function Involved in potassium channel activity
Specific Function Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane
cell part
ion channel complex
cation channel complex
potassium channel complex
voltage-gated potassium channel complex
macromolecular complex
protein complex
Function
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
transporter activity
ion channel activity
cation channel activity
potassium channel activity
voltage-gated potassium channel activity
Process
establishment of localization
transport
transmembrane transport
monovalent inorganic cation transport
potassium ion transport
ion transport
cation transport
Cellular Location
  1. Membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location Chromosome:8
Locus 8q24
SNPs KCNQ3
Gene Sequence
>2619 bp
ATGGGGCTCAAGGCGCGCAGGGCGGCGGGGGCGGCTGGCGGCGGCGGCGACGGGGGCGGC
GGAGGCGGCGGGGCGGCTAACCCAGCCGGAGGGGACGCGGCGGCGGCCGGCGACGAGGAG
CGGAAAGTGGGGCTGGCGCCCGGCGACGTGGAGCAAGTCACCTTGGCGCTCGGGGCCGGA
GCCGACAAAGACGGGACCCTGCTGCTGGAGGGCGGCGGCCGCGACGAGGGGCAGCGGAGG
ACCCCGCAGGGCATCGGGCTCCTGGCCAAGACCCCGCTGAGCCGCCCAGTCAAGAGAAAC
AACGCCAAGTACCGGCGCATCCAAACTTTGATCTACGACGCCCTGGAGAGACCGCGGGGC
TGGGCGCTGCTTTACCACGCGTTGGTGTTCCTGATTGTCCTGGGGTGCTTGATTCTGGCT
GTCCTGACCACATTCAAGGAGTATGAGACTGTCTCGGGAGACTGGCTTCTGTTACTGGAG
ACATTTGCTATTTTCATCTTTGGAGCCGAGTTTGCTTTGAGGATCTGGGCTGCTGGATGT
TGCTGCCGATACAAAGGCTGGCGGGGCCGACTGAAGTTTGCCAGGAAGCCCCTGTGCATG
TTGGACATCTTTGTGCTGATTGCCTCTGTGCCAGTGGTTGCTGTGGGAAACCAAGGCAAT
GTTCTGGCCACCTCCCTGCGAAGCCTGCGCTTCCTGCAGATCCTGCGCATGCTGCGGATG
GACCGGAGAGGTGGCACCTGGAAGCTTCTGGGCTCAGCCATCTGTGCCCACAGCAAAGAA
CTCATCACGGCCTGGTACATCGGTTTCCTGACACTCATCCTTTCTTCATTTCTTGTCTAC
CTGGTTGAGAAAGACGTCCCAGAGGTGGATGCACAAGGAGAGGAGATGAAAGAGGAGTTT
GAGACCTATGCAGATGCCCTGTGGTGGGGCCTGATCACACTGGCCACCATTGGCTATGGA
GACAAGACACCCAAAACGTGGGAAGGCCGTCTGATTGCCGCCACCTTTTCCTTAATTGGC
GTCTCCTTTTTTGCCCTTCCAGCGGGCATCCTGGGGTCCGGGCTGGCCCTCAAGGTGCAG
GAGCAACACCGTCAGAAGCACTTTGAGAAAAGGAGGAAGCCAGCTGCTGAGCTCATTCAG
GCTGCCTGGAGGTATTATGCTACCAACCCCAACAGGATTGACCTGGTGGCGACATGGAGA
TTTTATGAATCAGTCGTCTCTTTTCCTTTCTTCAGGAAAGAACAGCTGGAGGCAGCATCC
AGCCAAAAGCTGGGTCTCTTGGATCGGGTTCGCCTTTCTAATCCTCGTGGTAGCAATACT
AAAGGAAAGCTATTTACCCCTCTGAATGTAGATGCCATAGAAGAAAGTCCTTCTAAAGAA
CCAAAGCCTGTTGGCTTAAACAATAAAGAGCGTTTCCGCACGGCCTTCCGCATGAAAGCC
TACGCTTTCTGGCAGAGTTCTGAAGATGCCGGGACAGGTGACCCCATGGCGGAAGACAGG
GGCTATGGGAATGACTTCCCCATCGAAGACATGATCCCCACCCTGAAGGCCGCCATCCGA
GCCGTCAGAATTCTACAATTCCGTCTCTATAAAAAAAAATTCAAGGAGACTTTGAGGCCT
TACGATGTGAAGGATGTGATTGAGCAGTATTCTGCCGGGCATCTCGACATGCTTTCCAGG
ATAAAGTACCTTCAGACGAGAATAGATATGATTTTCACCCCTGGACCTCCCTCCACGCCA
AAACACAAGAAGTCTCAGAAAGGGTCAGCATTCACCTTCCCATCCCAGCAATCTCCCAGG
AATGAACCATATGTAGCCAGACCATCCACATCAGAAATCGAAGACCAAAGCATGATGGGG
AAGTTTGTAAAAGTTGAAAGACAGGTTCAGGACATGGGGAAGAAGCTGGACTTCCTCGTG
GATATGCACATGCAACACATGGAACGGTTGCAGGTGCAGGTCACGGAGTATTACCCAACC
AAGGGCACCTCCTCGCCAGCTGAAGCAGAGAAGAAGGAGGACAACAGGTATTCCGATTTG
AAAACCATCATCTGCAACTATTCTGAGACAGGCCCCCCGGAACCACCCTACAGCTTCCAC
CAGGTGACCATTGACAAAGTCAGCCCCTATGGGTTTTTTGCACATGACCCTGTGAACCTG
CCCCGAGGGGGACCCAGTTCTGGAAAGGTTCAGGCAACTCCTCCTTCCTCAGCAACAACG
TATGTGGAGAGGCCCACGGTCCTGCCTATCTTGACTCTTCTCGACTCCCGAGTGAGCTGC
CACTCCCAGGCTGACCTGCAGGGCCCCTACTCGGACCGAATCTCCCCCCGGCAGAGACGT
AGCATCACGCGAGACAGTGACACACCTCTGTCCCTGATGTCGGTCAACCACGAGGAGCTG
GAGAGGTCTCCAAGTGGCTTCAGCATCTCCCAGGACAGAGATGATTATGTGTTCGGCCCC
AATGGGGGGTCGAGCTGGATGAGGGAGAAGCGGTACCTCGCCGAGGGTGAGACGGACACA
GACACGGACCCCTTCACGCCCAGCGGCTCCATGCCTCTGTCGTCCACAGGGGATGGGATT
TCTGATTCAGTATGGACCCCTTCCAATAAGCCCATTTAA
Protein Properties
Number of Residues 872
Molecular Weight 96741.5
Theoretical pI 9.2
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • 122-142
  • 153-173
  • 197-217
  • 226-247
  • 262-282
  • 331-351
Protein Sequence
>Potassium voltage-gated channel subfamily KQT member 3
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAG
ADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRG
WALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGC
CCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRM
DRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEF
ETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQ
EQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAAS
SQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKA
YAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRP
YDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPR
NEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPT
KGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNL
PRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRR
SITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDT
DTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
GenBank ID Protein 4758630
UniProtKB/Swiss-Prot ID O43525
UniProtKB/Swiss-Prot Entry Name KCNQ3_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_004519.2
GeneCard ID KCNQ3
GenAtlas ID KCNQ3
HGNC ID HGNC:6297
References
General References
  1. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: 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. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  2. Selyanko AA, Hadley JK, Wood IC, Abogadie FC, Jentsch TJ, Brown DA: Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors. J Physiol. 2000 Feb 1;522 Pt 3:349-55. [PubMed:10713961 ]
  3. Yang WP, Levesque PC, Little WA, Conder ML, Ramakrishnan P, Neubauer MG, Blanar MA: Functional expression of two KvLQT1-related potassium channels responsible for an inherited idiopathic epilepsy. J Biol Chem. 1998 Jul 31;273(31):19419-23. [PubMed:9677360 ]
  4. Schroeder BC, Kubisch C, Stein V, Jentsch TJ: Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy. Nature. 1998 Dec 17;396(6712):687-90. [PubMed:9872318 ]
  5. Selyanko AA, Hadley JK, Wood IC, Abogadie FC, Delmas P, Buckley NJ, London B, Brown DA: Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute to the M-like current in a mammalian neuronal cell. J Neurosci. 1999 Sep 15;19(18):7742-56. [PubMed:10479678 ]
  6. Tinel N, Diochot S, Lauritzen I, Barhanin J, Lazdunski M, Borsotto M: M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2 subunit. FEBS Lett. 2000 Sep 1;480(2-3):137-41. [PubMed:11034315 ]
  7. Schwake M, Pusch M, Kharkovets T, Jentsch TJ: Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy. J Biol Chem. 2000 May 5;275(18):13343-8. [PubMed:10788442 ]
  8. Shapiro MS, Roche JP, Kaftan EJ, Cruzblanca H, Mackie K, Hille B: Reconstitution of muscarinic modulation of the KCNQ2/KCNQ3 K(+) channels that underlie the neuronal M current. J Neurosci. 2000 Mar 1;20(5):1710-21. [PubMed:10684873 ]
  9. Main MJ, Cryan JE, Dupere JR, Cox B, Clare JJ, Burbidge SA: Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine. Mol Pharmacol. 2000 Aug;58(2):253-62. [PubMed:10908292 ]
  10. Wickenden AD, Yu W, Zou A, Jegla T, Wagoner PK: Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3 potassium channels. Mol Pharmacol. 2000 Sep;58(3):591-600. [PubMed:10953053 ]
  11. Rundfeldt C, Netzer R: The novel anticonvulsant retigabine activates M-currents in Chinese hamster ovary-cells tranfected with human KCNQ2/3 subunits. Neurosci Lett. 2000 Mar 17;282(1-2):73-6. [PubMed:10713399 ]
  12. Singh NA, Westenskow P, Charlier C, Pappas C, Leslie J, Dillon J, Anderson VE, Sanguinetti MC, Leppert MF: KCNQ2 and KCNQ3 potassium channel genes in benign familial neonatal convulsions: expansion of the functional and mutation spectrum. Brain. 2003 Dec;126(Pt 12):2726-37. Epub 2003 Oct 8. [PubMed:14534157 ]
  13. Charlier C, Singh NA, Ryan SG, Lewis TB, Reus BE, Leach RJ, Leppert M: A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family. Nat Genet. 1998 Jan;18(1):53-5. [PubMed:9425900 ]
  14. Wickenden AD, Zou A, Wagoner PK, Jegla T: Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells. Br J Pharmacol. 2001 Jan;132(2):381-4. [PubMed:11159685 ]
  15. Hirose S, Zenri F, Akiyoshi H, Fukuma G, Iwata H, Inoue T, Yonetani M, Tsutsumi M, Muranaka H, Kurokawa T, Hanai T, Wada K, Kaneko S, Mitsudome A: A novel mutation of KCNQ3 (c.925T-->C) in a Japanese family with benign familial neonatal convulsions. Ann Neurol. 2000 Jun;47(6):822-6. [PubMed:10852552 ]