KvLQT3

From Wikipedia, the free encyclopedia

Potassium voltage-gated channel, KQT-like subfamily, member 3

Identifiers

KCNQ3; BFNC2; EBN2; KV7.3

External IDs

OMIM: 602232 MGI: 1336181 HomoloGene: 20949

Gene ontology
Molecular Function:	• ion channel activity • voltage-gated potassium channel activity • potassium ion binding
Cellular Component:	• membrane fraction • voltage-gated potassium channel complex • membrane • integral to membrane
Biological Process:	• ion transport • potassium ion transport • synaptic transmission

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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 (K_v7.3) 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]

[edit] References

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

[edit] 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.

[edit] External links

MeSH KCNQ3+Potassium+Channel

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel