KCND3

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Potassium voltage-gated channel, Shal-related subfamily, member 3
PDB rendering based on 1s1g.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols KCND3 ; KCND3L; KCND3S; KSHIVB; KV4.3; MGC142035; MGC142037
External IDs Template:OMIM5 Template:MGI HomoloGene21036
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Potassium voltage-gated channel, Shal-related subfamily, member 3, also known as KCND3 or Kv4.3, is a human gene.[1]

Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This member includes two isoforms with different sizes, which are encoded by alternatively spliced transcript variants of this gene.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: KCND3 potassium voltage-gated channel, Shal-related 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.
  • Serôdio P, Vega-Saenz de Miera E, Rudy B (1997). "Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain". J. Neurophysiol. 75 (5): 2174–9. PMID 8734615.
  • Kong W, Po S, Yamagishi T; et al. (1999). "Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing". Am. J. Physiol. 275 (6 Pt 2): H1963–70. PMID 9843794.
  • Dilks D, Ling HP, Cockett M; et al. (1999). "Cloning and expression of the human kv4.3 potassium channel". J. Neurophysiol. 81 (4): 1974–7. PMID 10200233.
  • Isbrandt D, Leicher T, Waldschütz R; et al. (2000). "Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA)". Genomics. 64 (2): 144–54. doi:10.1006/geno.2000.6117. PMID 10729221.
  • Postma AV, Bezzina CR, de Vries JF; et al. (2000). "Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3". Hum. Genet. 106 (6): 614–9. PMID 10942109.
  • Deschênes I, Tomaselli GF (2002). "Modulation of Kv4.3 current by accessory subunits". FEBS Lett. 528 (1–3): 183–8. PMID 12297301.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Ren X, Shand SH, Takimoto K (2003). "Effective association of Kv channel-interacting proteins with Kv4 channel is mediated with their unique core peptide". J. Biol. Chem. 278 (44): 43564–70. doi:10.1074/jbc.M302337200. PMID 12928444.
  • Hatano N, Ohya S, Muraki K; et al. (2004). "Two arginines in the cytoplasmic C-terminal domain are essential for voltage-dependent regulation of A-type K+ current in the Kv4 channel subfamily". J. Biol. Chem. 279 (7): 5450–9. doi:10.1074/jbc.M302034200. PMID 14645239.
  • Scannevin RH, Wang K, Jow F; et al. (2004). "Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1". Neuron. 41 (4): 587–98. PMID 14980207.
  • Zicha S, Xiao L, Stafford S; et al. (2005). "Transmural expression of transient outward potassium current subunits in normal and failing canine and human hearts". J. Physiol. (Lond.). 561 (Pt 3): 735–48. doi:10.1113/jphysiol.2004.075861. PMID 15498806.
  • Frank-Hansen R, Larsen LA, Andersen P; et al. (2005). "Mutations in the genes KCND2 and KCND3 encoding the ion channels Kv4.2 and Kv4.3, conducting the cardiac fast transient outward current (ITO,f), are not a frequent cause of long QT syndrome". Clin. Chim. Acta. 351 (1–2): 95–100. doi:10.1016/j.cccn.2004.08.017. PMID 15563876.
  • Baltaev R, Strutz-Seebohm N, Korniychuk G; et al. (2005). "Regulation of cardiac shal-related potassium channel Kv 4.3 by serum- and glucocorticoid-inducible kinase isoforms in Xenopus oocytes". Pflugers Arch. 450 (1): 26–33. doi:10.1007/s00424-004-1369-z. PMID 15578212.
  • Radicke S, Cotella D, Graf EM; et al. (2005). "Expression and function of dipeptidyl-aminopeptidase-like protein 6 as a putative beta-subunit of human cardiac transient outward current encoded by Kv4.3". J. Physiol. (Lond.). 565 (Pt 3): 751–6. doi:10.1113/jphysiol.2005.087312. PMID 15890703.
  • Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
  • Lundby A, Olesen SP (2006). "KCNE3 is an inhibitory subunit of the Kv4.3 potassium channel". Biochem. Biophys. Res. Commun. 346 (3): 958–67. doi:10.1016/j.bbrc.2006.06.004. PMID 16782062.
  • Ahmed I, Cosen-Binker LI, Leung YM; et al. (2007). "Modulation of the K(v)4.3 channel by syntaxin 1A". Biochem. Biophys. Res. Commun. 358 (3): 789–95. doi:10.1016/j.bbrc.2007.04.182. PMID 17506992.
  • Potapova IA, Cohen IS, Doronin SV (2007). "Voltage-gated ion channel Kv4.3 is associated with Rap guanine nucleotide exchange factors and regulates angiotensin receptor type 1 signaling to small G-protein Rap". FEBS J. 274 (17): 4375–84. doi:10.1111/j.1742-4658.2007.05966.x. PMID 17725712.

External links

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

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