[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/cav2-1-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/cav2-1-wikipedia\/","headline":"Cav2.1 – Wikipedia","name":"Cav2.1 – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens CACNA1A Identifiers Aliases CACNA1A, APCA, BI, CACNL1A4, CAV2.1,","datePublished":"2019-07-11","dateModified":"2019-07-11","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/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:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/cav2-1-wikipedia\/","wordCount":8007,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensCACNA1AIdentifiersAliasesCACNA1A, APCA, BI, CACNL1A4, CAV2.1, EA2, FHM, HPCA, MHP, MHP1, SCA6, Cav2.1, calcium voltage-gated channel subunit alpha1 A, EIEE42, DEE42External IDsOMIM: 601011 MGI: 109482 HomoloGene: 56383 GeneCards: CACNA1A WikidataCav2.1, also called the P\/Q voltage-dependent calcium channel, is a calcium channel found mainly in the brain.[5] Specifically, it is found on the presynaptic terminals of neurons in the brain and cerebellum.[5] Cav2.1 plays an important role in controlling the release of neurotransmitters between neurons.[5] It is composed of multiple subunits, including alpha-1, beta, alpha-2\/delta, and gamma subunits.[6] The alpha-1 subunit is the pore-forming subunit, meaning that the calcium ions flow through it.[6] Different kinds of calcium channels have different isoforms (versions) of the alpha-1 subunit. Cav2.1 has the alpha-1A subunit,[6] which is encoded by the CACNA1A gene.[a][5] Mutations in CACNA1A  have been associated with various neurologic disorders, including familial hemiplegic migraine, episodic ataxia type 2, and spinocerebellar ataxia type 6.[5]Table of ContentsFunction[edit]Clinical significance[edit]Interactions[edit]References[edit]Further reading[edit]Further reading[edit]Function[edit]“Voltage-dependent calcium channels mediate the entry of calcium ions into excitable cells, and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, and gene expression. Calcium channels are multisubunit complexes composed of alpha-1, beta, alpha-2\/delta, and gamma subunits. The channel activity is directed by the pore-forming alpha-1 subunit, whereas, the others act as auxiliary subunits regulating this activity. The distinctive properties of the calcium channel types are related primarily to the expression of a variety of alpha-1 isoforms, alpha-1A, B, C, D, E, and S. This gene encodes the alpha-1A subunit, which is predominantly expressed in neuronal tissue.”[6]Clinical significance[edit]Mutations in the CACNA1A gene are associated with multiple neurologic disorders, many of which are episodic, such as familial hemiplegic migraine, movement disorders such as episodic ataxia, and epilepsy with multiple seizure types.[8]“This gene also exhibits polymorphic variation due to (CAG)n-repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In one set of transcript variants, the (CAG)n-repeats occur in the 3′ UTR, and are not associated with any disease. However, in another set of variants, an insertion extends the coding region to include the (CAG)n-repeats which encode a polyglutamine tract. Expansion of the (CAG)n-repeats from the normal 4-16 to 21-28 in the coding region is associated with spinocerebellar ataxia 6.”[6]Interactions[edit]Cav2.1 has been shown to interact with CACNB4.[9][10]^ “CACNA1A is an abbreviation of the gene’s full name, CAlcium voltage-gated ChaNnel subunit AIpha 1A, which is a description of the protein coded for by the gene.”[7]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000141837 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034656 – 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.^ a b c d e Sutherland HG, Albury CL, Griffiths LR (21 June 2019). “Advances in genetics of migraine”. The Journal of Headache and Pain. 20 (1): 72. doi:10.1186\/s10194-019-1017-9. PMC\u00a06734342. PMID\u00a031226929.^ a b c d e “CACNA1A”. Gene. National Center for Biotechnology Information. 16 March 2021. Retrieved 28 March 2021.{{cite web}}:  CS1 maint: url-status (link)^ “The Science of CACNA1A”. CACNA1A Foundation. Retrieved 28 March 2021.^ Papandreou A, Danti FR, Spaull R, Leuzzi V, Mctague A, Kurian MA (February 2020). “The expanding spectrum of movement disorders in genetic epilepsies”. Developmental Medicine and Child Neurology. 62 (2): 178\u2013191. doi:10.1111\/dmcn.14407. PMID\u00a031784983. S2CID\u00a0208498567.^ Walker D, Bichet D, Campbell KP, De Waard M (January 1998). “A beta 4 isoform-specific interaction site in the carboxyl-terminal region of the voltage-dependent Ca2+ channel alpha 1A subunit”. The Journal of Biological Chemistry. 273 (4): 2361\u20137. doi:10.1074\/jbc.273.4.2361. PMID\u00a09442082.^ Walker D, Bichet D, Geib S, Mori E, Cornet V, Snutch TP,  et\u00a0al. (April 1999). “A new beta subtype-specific interaction in alpha1A subunit controls P\/Q-type Ca2+ channel activation”. The Journal of Biological Chemistry. 274 (18): 12383\u201390. doi:10.1074\/jbc.274.18.12383. PMID\u00a010212211.Further reading[edit]Terwindt G, Kors E, Haan J, Vermeulen F, Van den Maagdenberg A, Frants R, Ferrari M (June 2002). “Mutation analysis of the CACNA1A calcium channel subunit gene in 27 patients with sporadic hemiplegic migraine”. Archives of Neurology. 59 (6): 1016\u20138. doi:10.1001\/archneur.59.6.1016. PMID\u00a012056940.Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (December 2005). “International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels”. Pharmacological Reviews. 57 (4): 411\u201325. doi:10.1124\/pr.57.4.5. PMID\u00a016382099. S2CID\u00a010386627.Perez-Reyes E, Castellano A, Kim HS, Bertrand P, Baggstrom E, Lacerda AE,  et\u00a0al. (January 1992). “Cloning and expression of a cardiac\/brain beta subunit of the L-type calcium channel”. The Journal of Biological Chemistry. 267 (3): 1792\u20137. doi:10.1016\/S0021-9258(18)46015-2. PMID\u00a01370480.Barry EL, Viglione MP, Kim YI, Froehner SC (January 1995). “Expression and antibody inhibition of P-type calcium channels in human small-cell lung carcinoma cells”. The Journal of Neuroscience. 15 (1 Pt 1): 274\u201383. doi:10.1523\/JNEUROSCI.15-01-00274.1995. PMC\u00a06578292. PMID\u00a07823133.Joutel A, Bousser MG, Biousse V, Labauge P, Chabriat H, Nibbio A,  et\u00a0al. (September 1993). “A gene for familial hemiplegic migraine maps to chromosome 19”. Nature Genetics. 5 (1): 40\u20135. doi:10.1038\/ng0993-40. PMID\u00a08220421. S2CID\u00a06493091.Margolis RL, Breschel TS, Li SH, Kidwai AS, Antonarakis SE, McInnis MG, Ross CA (July 1995). “Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain”. Somatic Cell and Molecular Genetics. 21 (4): 279\u201384. doi:10.1007\/BF02255782. PMID\u00a08525433. S2CID\u00a022174220.Rettig J, Sheng ZH, Kim DK, Hodson CD, Snutch TP, Catterall WA (July 1996). “Isoform-specific interaction of the alpha1A subunits of brain Ca2+ channels with the presynaptic proteins syntaxin and SNAP-25”. Proceedings of the National Academy of Sciences of the United States of America. 93 (14): 7363\u20138. doi:10.1073\/pnas.93.14.7363. PMC\u00a038990. PMID\u00a08692999.Diriong S, Lory P, Williams ME, Ellis SB, Harpold MM, Taviaux S (December 1995). “Chromosomal localization of the human genes for alpha 1A, alpha 1B, and alpha 1E voltage-dependent Ca2+ channel subunits”. Genomics. 30 (3): 605\u20139. doi:10.1006\/geno.1995.1284. PMID\u00a08825650.Ophoff RA, Terwindt GM, Vergouwe MN, van Eijk R, Oefner PJ, Hoffman SM,  et\u00a0al. (November 1996). “Familial hemiplegic migraine and episodic ataxia type-2 are caused by mutations in the Ca2+ channel gene CACNL1A4”. Cell. 87 (3): 543\u201352. doi:10.1016\/S0092-8674(00)81373-2. hdl:1765\/57576. PMID\u00a08898206. S2CID\u00a016840573.Zhuchenko O, Bailey J, Bonnen P, Ashizawa T, Stockton DW, Amos C,  et\u00a0al. (January 1997). “Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel”. Nature Genetics. 15 (1): 62\u20139. doi:10.1038\/ng0197-62. PMID\u00a08988170. S2CID\u00a09116828.De Waard M, Liu H, Walker D, Scott VE, Gurnett CA, Campbell KP (January 1997). “Direct binding of G-protein betagamma complex to voltage-dependent calcium channels”. Nature. 385 (6615): 446\u201350. doi:10.1038\/385446a0. PMID\u00a09009193. S2CID\u00a04287544.Qin N, Platano D, Olcese R, Stefani E, Birnbaumer L (August 1997). “Direct interaction of gbetagamma with a C-terminal gbetagamma-binding domain of the Ca2+ channel alpha1 subunit is responsible for channel inhibition by G protein-coupled receptors”. Proceedings of the National Academy of Sciences of the United States of America. 94 (16): 8866\u201371. doi:10.1073\/pnas.94.16.8866. PMC\u00a023172. PMID\u00a09238069.Riess O, Sch\u00f6ls L, Bottger H, Nolte D, Vieira-Saecker AM, Schimming C,  et\u00a0al. (August 1997). “SCA6 is caused by moderate CAG expansion in the alpha1A-voltage-dependent calcium channel gene”. Human Molecular Genetics. 6 (8): 1289\u201393. doi:10.1093\/hmg\/6.8.1289. PMID\u00a09259275.Jodice C, Mantuano E, Veneziano L, Trettel F, Sabbadini G, Calandriello L,  et\u00a0al. (October 1997). “Episodic ataxia type 2 (EA2) and spinocerebellar ataxia type 6 (SCA6) due to CAG repeat expansion in the CACNA1A gene on chromosome 19p”. Human Molecular Genetics. 6 (11): 1973\u20138. doi:10.1093\/hmg\/6.11.1973. PMID\u00a09302278.Charvin N, L’ev\u00eaque C, Walker D, Berton F, Raymond C, Kataoka M,  et\u00a0al. (August 1997). “Direct interaction of the calcium sensor protein synaptotagmin I with a cytoplasmic domain of the alpha1A subunit of the P\/Q-type calcium channel”. The EMBO Journal. 16 (15): 4591\u20136. doi:10.1093\/emboj\/16.15.4591. PMC\u00a01170085. PMID\u00a09303303.Ishikawa K, Tanaka H, Saito M, Ohkoshi N, Fujita T, Yoshizawa K,  et\u00a0al. (August 1997). “Japanese families with autosomal dominant pure cerebellar ataxia map to chromosome 19p13.1-p13.2 and are strongly associated with mild CAG expansions in the spinocerebellar ataxia type 6 gene in chromosome 19p13.1”. American Journal of Human Genetics. 61 (2): 336\u201346. doi:10.1086\/514867. PMC\u00a01715894. PMID\u00a09311738.Walker D, Bichet D, Campbell KP, De Waard M (January 1998). “A beta 4 isoform-specific interaction site in the carboxyl-terminal region of the voltage-dependent Ca2+ channel alpha 1A subunit”. The Journal of Biological Chemistry. 273 (4): 2361\u20137. doi:10.1074\/jbc.273.4.2361. PMID\u00a09442082.Yue Q, Jen JC, Thwe MM, Nelson SF, Baloh RW (May 1998). “De novo mutation in CACNA1A caused acetazolamide-responsive episodic ataxia”. American Journal of Medical Genetics. 77 (4): 298\u2013301. doi:10.1002\/(SICI)1096-8628(19980526)77:43.0.CO;2-J. PMID\u00a09600739.Hans M, Urrutia A, Deal C, Brust PF, Stauderman K, Ellis SB,  et\u00a0al. (March 1999). “Structural elements in domain IV that influence biophysical and pharmacological properties of human alpha1A-containing high-voltage-activated calcium channels”. Biophysical Journal. 76 (3): 1384\u2013400. doi:10.1016\/S0006-3495(99)77300-5. PMC\u00a01300117. PMID\u00a010049321.Walker D, Bichet D, Geib S, Mori E, Cornet V, Snutch TP,  et\u00a0al. (April 1999). “A new beta subtype-specific interaction in alpha1A subunit controls P\/Q-type Ca2+ channel activation”. The Journal of Biological Chemistry. 274 (18): 12383\u201390. doi:10.1074\/jbc.274.18.12383. PMID\u00a010212211.Further reading[edit]  "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/cav2-1-wikipedia\/#breadcrumbitem","name":"Cav2.1 – Wikipedia"}}]}]