KCNQ4
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| Potassium voltage-gated channel, KQT-like subfamily, member 4
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| Image:PBB Protein KCNQ4 image.jpg | ||||||||||||||||||||||||||||||||||||||
| PDB rendering based on 2ovc. | ||||||||||||||||||||||||||||||||||||||
| Available structures: For the file format that describes the 3D structures of molecules found in the Protein Data Bank, see Protein Data Bank (file format).
The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. These data, typically obtained by X-ray crystallography or NMR spectroscopy, are submitted by biologists and biochemists from around the world, are released into the public domain, and can be accessed for free. HistoryFounded in 1971 by Drs. Edgar Meyer and Walter Hamilton Brookhaven National Laboratory, management of the Protein Data Bank was transferred in 1998 to members of the Research Collaboratory for Structural Bioinformatics (RCSB). The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. The founding members are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan). The BMRB (USA) group joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single Protein Data Bank Archive of macromolecular structural data that is freely and publicly available to the global community. The PDB is a key resource in structural biology and is critical to more recent work in structural genomics. Countless derived databases and projects have been developed to integrate and classify the PDB in terms of protein structure, protein function and protein evolution. GrowthWhen the PDB was originally founded it contained just 7 protein structures. Since then it has undergone an approximate exponential growth in the number of structures, which does not show any sign of falling off. The growth rate of the PDB has been the subject of fairly extensive analysis. ContentsAs of 26 September, 2006, the database contained 39,051 released atomic coordinate entries (or "structures"), 35,767 of that proteins, the rest being nucleic acids, nucleic acid-protein complexes, and a few other molecules. About 5,000 new structures are released each year. Data are stored in the mmCIF format specifically developed for the purpose. Note that the database stores information about the exact location of all atoms in a large biomolecule (although, usually without the hydrogen atoms, as their positions are more of a statistical estimate); if one is only interested in sequence data, i.e. the list of amino acids making up a particular protein or the list of nucleotides making up a particular nucleic acid, the much larger databases from Swiss-Prot and the International Nucleotide Sequence Database Collaboration should be used. StatisticsAs of 11 September, 2007, the "PDB Holdings List" at RCSB reported the following statistics:
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| Identifiers | ||||||||||||||||||||||||||||||||||||||
| Symbol(s) | KCNQ4; DFNA2; KV7.4 | |||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603537 MGI: 1926803 Homologene: 78107 | |||||||||||||||||||||||||||||||||||||
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| RNA expression pattern | ||||||||||||||||||||||||||||||||||||||
| Orthologs | ||||||||||||||||||||||||||||||||||||||
| Human | Mouse | |||||||||||||||||||||||||||||||||||||
| Entrez | 9132 | 60613 | ||||||||||||||||||||||||||||||||||||
| Ensembl | ENSG00000117013 | ENSMUSG00000028631 | ||||||||||||||||||||||||||||||||||||
| Uniprot | P56696 | Q9JK97 | ||||||||||||||||||||||||||||||||||||
| Refseq | XM_001132376 (mRNA) XP_001132376 (protein) | XM_143960 (mRNA) XP_143960 (protein) | ||||||||||||||||||||||||||||||||||||
| Location | Chr 1: 41.02 - 41.08 Mb | Chr 4: 120.2 - 120.24 Mb | ||||||||||||||||||||||||||||||||||||
| Pubmed search | [5] | [6] | ||||||||||||||||||||||||||||||||||||
Potassium voltage-gated channel, KQT-like subfamily, member 4, also known as KCNQ4 or Kv7.4, is a human gene.[1]
The protein encoded by this gene forms a potassium channel that is thought to play a critical role in the regulation of neuronal excitability, particularly in sensory cells of the cochlea. The current generated by this channel is inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. The encoded protein can form a homomultimeric potassium channel or possibly a heteromultimeric channel in association with the protein encoded by the KCNQ3 gene. Defects in this gene are a cause of nonsyndromic sensorineural deafness type 2 (DFNA2), an autosomal dominant form of progressive hearing loss. Two transcript variants encoding different isoforms have been found for this gene.[1]
See also
References
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.
- 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.
- Coucke PJ, Van Hauwe P, Kelley PM, et al. (1999). "Mutations in the KCNQ4 gene are responsible for autosomal dominant deafness in four DFNA2 families.". Hum. Mol. Genet. 8 (7): 1321-8. PMID 10369879.
- Talebizadeh Z, Kelley PM, Askew JW, et al. (2000). "Novel mutation in the KCNQ4 gene in a large kindred with dominant progressive hearing loss.". Hum. Mutat. 14 (6): 493-501. doi:<493::AID-HUMU8>3.0.CO;2-P 10.1002/(SICI)1098-1004(199912)14:6<493::AID-HUMU8>3.0.CO;2-P. PMID 10571947.
- 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.
- Van Hauwe P, Coucke PJ, Ensink RJ, et al. (2000). "Mutations in the KCNQ4 K+ channel gene, responsible for autosomal dominant hearing loss, cluster in the channel pore region.". Am. J. Med. Genet. 93 (3): 184-7. PMID 10925378.
- Beisel KW, Nelson NC, Delimont DC, Fritzsch B (2001). "Longitudinal gradients of KCNQ4 expression in spiral ganglion and cochlear hair cells correlate with progressive hearing loss in DFNA2.". Brain Res. Mol. Brain Res. 82 (1-2): 137-49. PMID 11042367.
- Søgaard R, Ljungstrøm T, Pedersen KA, et al. (2001). "KCNQ4 channels expressed in mammalian cells: functional characteristics and pharmacology.". Am. J. Physiol., Cell Physiol. 280 (4): C859-66. PMID 11245603.
- Van Camp G, Coucke PJ, Akita J, et al. (2002). "A mutational hot spot in the KCNQ4 gene responsible for autosomal dominant hearing impairment.". Hum. Mutat. 20 (1): 15-9. doi:10.1002/humu.10096. PMID 12112653.
- Stern RE, Lalwani AK (2003). "Audiologic evidence for further genetic heterogeneity at DFNA2.". Acta Otolaryngol. 122 (7): 730-5. PMID 12484650.
- Schwake M, Jentsch TJ, Friedrich T (2003). "A carboxy-terminal domain determines the subunit specificity of KCNQ K+ channel assembly.". EMBO Rep. 4 (1): 76-81. doi:10.1038/sj.embor.embor715. PMID 12524525.
- Li Y, Langlais P, Gamper N, et al. (2004). "Dual phosphorylations underlie modulation of unitary KCNQ K(+) channels by Src tyrosine kinase.". J. Biol. Chem. 279 (44): 45399-407. doi:10.1074/jbc.M408410200. PMID 15304482.
- Chambard JM, Ashmore JF (2005). "Regulation of the voltage-gated potassium channel KCNQ4 in the auditory pathway.". Pflugers Arch. 450 (1): 34-44. doi:10.1007/s00424-004-1366-2. PMID 15660259.
- Van Laer L, Carlsson PI, Ottschytsch N, et al. (2006). "The contribution of genes involved in potassium-recycling in the inner ear to noise-induced hearing loss.". Hum. Mutat. 27 (8): 786-95. doi:10.1002/humu.20360. PMID 16823764.
- Van Eyken E, Van Laer L, Fransen E, et al. (2006). "KCNQ4: a gene for age-related hearing impairment?". Hum. Mutat. 27 (10): 1007-16. doi:10.1002/humu.20375. PMID 16917933.
- Su CC, Yang JJ, Shieh JC, et al. (2007). "Identification of novel mutations in the KCNQ4 gene of patients with nonsyndromic deafness from Taiwan.". Audiol. Neurootol. 12 (1): 20-6. doi:10.1159/000096154. PMID 17033161.
- Jensen HS, Grunnet M, Olesen SP (2007). "Inactivation as a new regulatory mechanism for neuronal Kv7 channels.". Biophys. J. 92 (8): 2747-56. doi:10.1529/biophysj.106.101287. PMID 17237198.
- Howard RJ, Clark KA, Holton JM, Minor DL (2007). "Structural insight into KCNQ (Kv7) channel assembly and channelopathy.". Neuron 53 (5): 663-75. doi:10.1016/j.neuron.2007.02.010. PMID 17329207.
External links
Template:Membrane-protein-stub This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Ion channel, receptor: ligand-gated ion channels | |
|---|---|
| Cys-loop receptors | 5-HT receptor (5-HT3 serotonin receptor (A)) - GABA receptor (GABA A (α1, α2, α3, α5, α6, β1, β2, β3, γ2, ε), GABA C (ρ1)) - Glycine receptor (α1) - Nicotinic acetylcholine receptor (α1, α2, α3, α4, α5, α7, β2, β3, β4, δ, ε, (α4)2(β2)3, (α7)5, Ganglion type, Muscle type) |
| Ionotropic glutamate receptors | AMPA (1, 2, 3, 4) - Kainate (1, 2) - NMDA (1, 2A, 2B, 2C, 2D) |
| ATP-gated channels | Purinergic receptors (P2X (1, 4, 5, 7)) |
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
