KvLQT3

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Potassium voltage-gated channel, KQT-like subfamily, member 3
Identifiers
Symbols KCNQ3; BFNC2; EBN2; KV7.3
External IDs OMIM: 602232 MGI: 1336181 HomoloGene: 20949
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3786 110862
Ensembl ENSG00000184156 ENSMUSG00000056258
Uniprot O43525 Q14B66
Refseq NM_004519 (mRNA)
NP_004510 (protein)		 NM_152923 (mRNA)
NP_690887 (protein)
Location Chr 8: 133.21 - 133.56 Mb Chr 15: 65.82 - 66.12 Mb
Pubmed search [1] [2]

KvLQT3 (Kv7.3) is a potassium channel protein coded for by the gene KCNQ3.[1]

It is associated with benign familial neonatal convulsions.

The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein encoded by this gene and one of two related proteins encoded by the KCNQ2 and KCNQ5 genes, both integral membrane proteins. M channel currents are inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. Defects in this gene are a cause of benign familial neonatal convulsions type 2 (BFNC2), also known as epilepsy, benign neonatal type 2 (EBN2).[1]

References

  1. ^ a b "Entrez Gene: KCNQ3 potassium voltage-gated channel, KQT-like subfamily, member 3".

Further reading

  • Gutman GA, Chandy KG, Grissmer S, et al. (2006). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels.". Pharmacol. Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. 
  • Ryan SG, Wiznitzer M, Hollman C, et al. (1991). "Benign familial neonatal convulsions: evidence for clinical and genetic heterogeneity.". Ann. Neurol. 29 (5): 469–73. doi:10.1002/ana.410290504. PMID 1859177. 
  • Lewis TB, Leach RJ, Ward K, et al. (1993). "Genetic heterogeneity in benign familial neonatal convulsions: identification of a new locus on chromosome 8q.". Am. J. Hum. Genet. 53 (3): 670–5. PMID 8102508. 
  • Charlier C, Singh NA, Ryan SG, et al. (1998). "A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family.". Nat. Genet. 18 (1): 53–5. doi:10.1038/ng0198-53. PMID 9425900. 
  • Yang WP, Levesque PC, Little WA, et al. (1998). "Functional expression of two KvLQT1-related potassium channels responsible for an inherited idiopathic epilepsy.". J. Biol. Chem. 273 (31): 19419–23. PMID 9677360. 
  • Wang HS, Pan Z, Shi W, et al. (1998). "KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel.". Science 282 (5395): 1890–3. PMID 9836639. 
  • Schroeder BC, Kubisch C, Stein V, Jentsch TJ (1999). "Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy.". Nature 396 (6712): 687–90. doi:10.1038/25367. PMID 9872318. 
  • Kubisch C, Schroeder BC, Friedrich T, et al. (1999). "KCNQ4, a novel potassium channel expressed in sensory outer hair cells, is mutated in dominant deafness.". Cell 96 (3): 437–46. PMID 10025409. 
  • Selyanko AA, Hadley JK, Wood IC, et al. (1999). "Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute to the M-like current in a mammalian neuronal cell.". J. Neurosci. 19 (18): 7742–56. PMID 10479678. 
  • Shapiro MS, Roche JP, Kaftan EJ, et al. (2000). "Reconstitution of muscarinic modulation of the KCNQ2/KCNQ3 K(+) channels that underlie the neuronal M current.". J. Neurosci. 20 (5): 1710–21. PMID 10684873. 
  • Rundfeldt C, Netzer R (2000). "The novel anticonvulsant retigabine activates M-currents in Chinese hamster ovary-cells tranfected with human KCNQ2/3 subunits.". Neurosci. Lett. 282 (1-2): 73–6. PMID 10713399. 
  • Selyanko AA, Hadley JK, Wood IC, et al. (2000). "Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors.". J. Physiol. (Lond.) 522 Pt 3: 349–55. PMID 10713961. 
  • Cooper EC, Aldape KD, Abosch A, et al. (2000). "Colocalization and coassembly of two human brain M-type potassium channel subunits that are mutated in epilepsy.". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4914–9. doi:10.1073/pnas.090092797. PMID 10781098. 
  • Schwake M, Pusch M, Kharkovets T, Jentsch TJ (2000). "Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy.". J. Biol. Chem. 275 (18): 13343–8. PMID 10788442. 
  • Hirose S, Zenri F, Akiyoshi H, et al. (2000). "A novel mutation of KCNQ3 (c.925T-->C) in a Japanese family with benign familial neonatal convulsions.". Ann. Neurol. 47 (6): 822–6. PMID 10852552. 
  • Main MJ, Cryan JE, Dupere JR, et al. (2000). "Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine.". Mol. Pharmacol. 58 (2): 253–62. PMID 10908292. 
  • Wickenden AD, Yu W, Zou A, et al. (2000). "Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3 potassium channels.". Mol. Pharmacol. 58 (3): 591–600. PMID 10953053. 
  • Tinel N, Diochot S, Lauritzen I, et al. (2000). "M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2 subunit.". FEBS Lett. 480 (2-3): 137–41. PMID 11034315. 
  • Wickenden AD, Zou A, Wagoner PK, Jegla T (2001). "Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells.". Br. J. Pharmacol. 132 (2): 381–4. doi:10.1038/sj.bjp.0703861. PMID 11159685. 
  • Yus-Najera E, Santana-Castro I, Villarroel A (2002). "The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels.". J. Biol. Chem. 277 (32): 28545–53. doi:10.1074/jbc.M204130200. PMID 12032157. 

External links

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 This membrane protein-related article is a stub. You can help Wikipedia by expanding it.
v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channel
L-type/Cavα (1.1, 1.2, 1.3, 1.4) • N-type/Cavα2.2 • P-type/Cavα(2.1) • Q-type/Cavα2.1 • R-type/Cavα2.3 • T-type/Cavα(3.2)
α2δ-subunits (1, 2) • β-subunits (β1, β2, β3, β4) • γ-subunits (γ1, γ2, γ3, γ4)
Cation channels of sperm • Two-pore channel (1, 2)
Ligand-gated
Na+: Sodium channel
Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) • Navβ (1, 2, 3, 4)
Other
K+: Potassium channel
Kvα (1-6) (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.10, 2.1, 2.2, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 4.3, 5.1, 6.1, 6.2, 6.3, 6.4)
Kvα (7-12) (7.1, 7.2, 7.3, 7.4, 7.5, 8.1, 8.2, 9.1, 9.2, 9.3, 10.1, 10.2, 11.1/hERG, 11.2, 11.3, 12.1, 12.2, 12.3)
Kvβ (1, 2, 3) • KCNIP (1, 2, 3, 4) • minK/ISK • MiRP (1, 2, 3) • Shaker gene
Kir (1.1, 2.1, 2.2, 2.3, 2.4) • GIRK/Kir (3.1, 3.2, 3.3, 3.4) • Kir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)
K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)
M+: TRP cation channel
TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (1, 2, 3) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)
Cl-: Chloride channel
CFTR • CLCA (1, 2, 3, 4) • CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) • CLIC (1, 2, 3, 4, 5, 6, L1) • CLNS (1A, 1B)
Cyclic nucleotide-gated
α1, α2, α3, α4, β1, β3, H1, H2, H3, H4
Porin
Other/general

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