[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/kcnd2-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki7\/kcnd2-wikipedia\/","headline":"KCND2 – Wikipedia","name":"KCND2 – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens Potassium voltage-gated channel subfamily D member 2 is","datePublished":"2016-09-08","dateModified":"2016-09-08","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki7\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/c\/ca\/PDB_1nn7_EBI.jpg\/180px-PDB_1nn7_EBI.jpg","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/c\/ca\/PDB_1nn7_EBI.jpg\/180px-PDB_1nn7_EBI.jpg","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki7\/kcnd2-wikipedia\/","wordCount":6743,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensPotassium voltage-gated channel subfamily D member 2 is a protein that in humans is encoded by the KCND2 gene.[5][6][7] It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.[8]Table of ContentsDescription[edit]Interactions[edit]See also[edit]References[edit]Further reading[edit]External links[edit]Description[edit]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.[7]Interactions[edit]KCND2 has been shown to interact with FLNC.[9]See also[edit]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000184408 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060882 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Zhu XR, Wulf A, Schwarz M, Isbrandt D, Pongs O (December 1999). “Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current”. Receptors Channels. 6 (5): 387\u2013400. PMID\u00a010551270.^ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stuhmer W, Wang X (December 2005). “International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels”. Pharmacol Rev. 57 (4): 473\u2013508. doi:10.1124\/pr.57.4.10. PMID\u00a016382104. S2CID\u00a0219195192.^ a b “Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2”.^ Oudit GY, Kassiri Z, Sah R, Ramirez RJ, Zobel C, Backx PH (May 2001). “The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium”. J. Mol. Cell. Cardiol. 33 (5): 851\u2013872. doi:10.1006\/jmcc.2001.1376. PMID\u00a011343410. S2CID\u00a0829154.^ Petrecca, K; Miller D M; Shrier A (December 2000). “Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin”. J. Neurosci. 20 (23): 8736\u201344. doi:10.1523\/JNEUROSCI.20-23-08736.2000. PMC\u00a06773047. PMID\u00a011102480.Further reading[edit]Kong W, Po S, Yamagishi T,  et\u00a0al. (1999). “Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing”. Am. J. Physiol. 275 (6 Pt 2): H1963\u201370. doi:10.1152\/ajpheart.1998.275.6.H1963. PMID\u00a09843794.Kikuno R, Nagase T, Ishikawa K,  et\u00a0al. (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\u2013205. doi:10.1093\/dnares\/6.3.197. PMID\u00a010470851.Kurschner C, Yuzaki M (1999). “Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein”. J. Neurosci. 19 (18): 7770\u201380. doi:10.1523\/JNEUROSCI.19-18-07770.1999. PMC\u00a06782450. PMID\u00a010479680.An WF, Bowlby MR, Betty M,  et\u00a0al. (2000). “Modulation of A-type potassium channels by a family of calcium sensors”. Nature. 403 (6769): 553\u2013556. Bibcode:2000Natur.403..553A. doi:10.1038\/35000592. PMID\u00a010676964. S2CID\u00a04419472.Isbrandt D, Leicher T, Waldsch\u00fctz R,  et\u00a0al. (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\u2013154. doi:10.1006\/geno.2000.6117. PMID\u00a010729221. S2CID\u00a01429910.Postma AV, Bezzina CR, de Vries JF,  et\u00a0al. (2000). “Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3”. Hum. Genet. 106 (6): 614\u2013619. doi:10.1007\/s004390050033. PMID\u00a010942109.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\u201344. doi:10.1523\/JNEUROSCI.20-23-08736.2000. PMC\u00a06773047. PMID\u00a011102480.B\u00e4hring R, Dannenberg J, Peters HC,  et\u00a0al. (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\u201323894. doi:10.1074\/jbc.M101320200. PMID\u00a011287421.Nakamura TY, Pountney DJ, Ozaita A,  et\u00a0al. (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\u201312813. Bibcode:2001PNAS…9812808N. doi:10.1073\/pnas.221168498. PMC\u00a060135. PMID\u00a011606724.Morohashi Y, Hatano N, Ohya S,  et\u00a0al. (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\u201314975. doi:10.1074\/jbc.M200897200. PMID\u00a011847232.Eldstrom J, Doerksen KW, Steele DF, Fedida D (2002). “N-terminal PDZ-binding domain in Kv1 potassium channels”. FEBS Lett. 531 (3): 529\u2013537. doi:10.1016\/S0014-5793(02)03572-X. PMID\u00a012435606. S2CID\u00a040689829.Schrader LA, Anderson AE, Mayne A,  et\u00a0al. (2002). “PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex”. J. Neurosci. 22 (23): 10123\u201333. doi:10.1523\/JNEUROSCI.22-23-10123.2002. PMC\u00a06758737. PMID\u00a012451113.Strausberg RL, Feingold EA, Grouse LH,  et\u00a0al. (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\u201316903. Bibcode:2002PNAS…9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.Shin BK, Wang H, Yim AM,  et\u00a0al. (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\u20137616. doi:10.1074\/jbc.M210455200. PMID\u00a012493773.Scherer SW, Cheung J, MacDonald JR,  et\u00a0al. (2003). “Human chromosome 7: DNA sequence and biology”. Science. 300 (5620): 767\u2013772. Bibcode:2003Sci…300..767S. doi:10.1126\/science.1083423. PMC\u00a02882961. PMID\u00a012690205.Hillier LW, Fulton RS, Fulton LA,  et\u00a0al. (2003). “The DNA sequence of human chromosome 7”. Nature. 424 (6945): 157\u2013164. Bibcode:2003Natur.424..157H. doi:10.1038\/nature01782. PMID\u00a012853948.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\u2013452. doi:10.1074\/jbc.M304675200. PMID\u00a014559911.Kim LA, Furst J, Butler MH,  et\u00a0al. (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\u20135554. doi:10.1074\/jbc.M311332200. PMID\u00a014623880.External links[edit]PDB gallery1nn7: Crystal Structure Of The Tetramerization Domain Of The Shal Voltage-Gated Potassium Channel1s6c: Crystal structure of the complex between KChIP1 and Kv4.2 N1-30This article incorporates text from the United States National Library of Medicine, which is in the public domain."},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki7\/kcnd2-wikipedia\/#breadcrumbitem","name":"KCND2 – Wikipedia"}}]}]