KCND2

Potassium voltage-gated channel, Shal-related subfamily, member 2
PDB rendering based on 1nn7.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1nn7​, 1s6c​
Identifiers
Symbols	KCND2 ; KIAA1044; KV4.2; MGC119702; MGC119703; RK5
External IDs	Template:OMIM5 Template:MGI HomoloGene: 40828
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
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 2, also known as KCND2 or K_v4.2, is a human gene.

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 mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.

See also

• Voltage-gated potassium channel

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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kikuno R, Nagase T, Ishikawa K; et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. PMID 10470851.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. PMID 10479680.
• Zhu XR, Wulf A, Schwarz M; et al. (1999). "Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current". Recept. Channels. 6 (5): 387–400. PMID 10551270.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• An WF, Bowlby MR, Betty M; et al. (2000). "Modulation of A-type potassium channels by a family of calcium sensors". Nature. 403 (6769): 553–6. doi:10.1038/35000592. PMID 10676964.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Petrecca K, Miller DM, Shrier A (2001). "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin". J. Neurosci. 20 (23): 8736–44. PMID 11102480.CS1 maint: Multiple names: authors list (link)
• Bähring R, Dannenberg J, Peters HC; et al. (2001). "Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating". J. Biol. Chem. 276 (26): 23888–94. doi:10.1074/jbc.M101320200. PMID 11287421.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nakamura TY, Pountney DJ, Ozaita A; et al. (2001). "A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents". Proc. Natl. Acad. Sci. U.S.A. 98 (22): 12808–13. doi:10.1073/pnas.221168498. PMID 11606724.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Morohashi Y, Hatano N, Ohya S; et al. (2002). "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4". J. Biol. Chem. 277 (17): 14965–75. doi:10.1074/jbc.M200897200. PMID 11847232.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Eldstrom J, Doerksen KW, Steele DF, Fedida D (2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. 531 (3): 529–37. PMID 12435606.CS1 maint: Multiple names: authors list (link)
• Schrader LA, Anderson AE, Mayne A; et al. (2002). "PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex". J. Neurosci. 22 (23): 10123–33. PMID 12451113.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shin BK, Wang H, Yim AM; et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Scherer SW, Cheung J, MacDonald JR; et al. (2003). "Human chromosome 7: DNA sequence and biology". Science. 300 (5620): 767–72. doi:10.1126/science.1083423. PMID 12690205.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hillier LW, Fulton RS, Fulton LA; et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wong W, Schlichter LC (2004). "Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95". J. Biol. Chem. 279 (1): 444–52. doi:10.1074/jbc.M304675200. PMID 14559911.
• Kim LA, Furst J, Butler MH; et al. (2004). "Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2". J. Biol. Chem. 279 (7): 5549–54. doi:10.1074/jbc.M311332200. PMID 14623880.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

External links

• Kv4.2+Potassium+Channel at the US National Library of Medicine Medical Subject Headings (MeSH)
• KCND2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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