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Voltage-dependent P/Q-type calcium channel subunit alpha-1A (Brain calcium channel I) (BI) (Calcium channel, L type, alpha-1 polypeptide isoform 4) (Voltage-gated calcium channel subunit alpha Cav2.1)

 CAC1A_HUMAN             Reviewed;        2506 AA.
O00555; J3KP41; P78510; P78511; Q16290; Q92690; Q99790; Q99791;
Q99792; Q99793; Q9NS88; Q9UDC4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
12-SEP-2018, sequence version 3.
10-OCT-2018, entry version 193.
RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A {ECO:0000305};
AltName: Full=Brain calcium channel I {ECO:0000303|PubMed:8988170};
Short=BI {ECO:0000303|PubMed:8988170};
AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
Name=CACNA1A {ECO:0000312|HGNC:HGNC:1388};
Synonyms=CACH4, CACN3, CACNL1A4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Neuron;
PubMed=10049321; DOI=10.1016/S0006-3495(99)77300-5;
Hans M., Urrutia A., Deal C., Brust P.F., Stauderman K., Ellis S.B.,
Harpold M.M., Johnson E.C., Williams M.E.;
"Structural elements in domain IV that influence biophysical and
pharmacological properties of human alpha1A-containing high-voltage-
activated calcium channels.";
Biophys. J. 76:1384-1400(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), VARIANTS FHM1
GLN-192; MET-665; ALA-713 AND LEU-1809, VARIANT THR-453, AND
INVOLVEMENT IN EA2.
TISSUE=Cerebellum;
PubMed=8898206; DOI=10.1016/S0092-8674(00)81373-2;
Ophoff R.A., Terwindt G.M., Vergouwe M.N., van Eijk R., Oefner P.J.,
Hoffman S.M.G., Lamerdin J.E., Mohrenweiser H.W., Bulman D.E.,
Ferrari M., Haan J., Lindhout D., van Ommen G.-J.B., Hofker M.H.,
Ferrari M.D., Frants R.R.;
"Familial hemiplegic migraine and episodic ataxia type-2 are caused by
mutations in the Ca2+ channel gene CACNL1A4.";
Cell 87:543-552(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF
1312-2506 (ISOFORMS 1; 2; 3 AND 6), ALTERNATIVE SPLICING, AND
INVOLVEMENT IN SCA6.
TISSUE=Brain;
PubMed=8988170; DOI=10.1038/ng0197-62;
Zhuchenko O., Bailey J., Bonnen P.E., Ashizawa T., Stockton D.W.,
Amos C., Dobyns W.B., Subramony S.H., Zoghbi H.Y., Lee C.C.;
"Autosomal dominant cerebellar ataxia (SCA6) associated with small
polyglutamine expansions in the alpha 1A-voltage-dependent calcium
channel.";
Nat. Genet. 15:62-69(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-1104, AND
FUNCTION.
TISSUE=Cerebellum;
PubMed=10753886; DOI=10.1074/jbc.275.15.10893;
Toru S., Murakoshi T., Ishikawa K., Saegusa H., Fujigasaki H.,
Uchihara T., Nagayama S., Osanai M., Mizusawa H., Tanabe T.;
"Spinocerebellar ataxia type 6 mutation alters P-type calcium channel
function.";
J. Biol. Chem. 275:10893-10898(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1692-1806.
TISSUE=Lung carcinoma;
PubMed=7823133;
Barry E.L.R., Viglione M.P., Kim Y.I., Froehner S.C.;
"Expression and antibody inhibition of P-type calcium channels in
human small-cell lung carcinoma cells.";
J. Neurosci. 15:274-283(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1701-1821, AND TISSUE SPECIFICITY.
TISSUE=Lung carcinoma;
PubMed=1335101; DOI=10.1016/S0025-6196(12)61144-6;
Oguro-Okano M., Griesmann G.E., Wieben E.D., Slaymaker S.J.,
Snutch T.P., Lennon V.A.;
"Molecular diversity of neuronal-type calcium channels identified in
small cell lung carcinoma.";
Mayo Clin. Proc. 67:1150-1159(1992).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2037-2257 (ISOFORMS 1/2/3/4).
TISSUE=Frontal cortex;
PubMed=8525433; DOI=10.1007/BF02255782;
Margolis R.L., Breschel T.S., Li S.H., Kidwai A.S., Antonarakis S.E.,
McInnis M.G., Ross C.A.;
"Characterization of cDNA clones containing CCA trinucleotide repeats
derived from human brain.";
Somat. Cell Mol. Genet. 21:279-284(1995).
[9]
INTERACTION WITH CABP1.
PubMed=11865310; DOI=10.1038/nn805;
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
Catterall W.A.;
"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
binding protein 1.";
Nat. Neurosci. 5:210-217(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1954-1974.
PubMed=18400181; DOI=10.1016/j.str.2008.01.011;
Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T.;
"Crystal structure of the CaV2 IQ domain in complex with
Ca2+/calmodulin: high-resolution mechanistic implications for channel
regulation by Ca2+.";
Structure 16:607-620(2008).
[11]
VARIANT SCA6 ARG-293.
PubMed=9345107; DOI=10.1086/301613;
Yue Q., Jen J.C., Nelson S.F., Baloh R.W.;
"Progressive ataxia due to a missense mutation in a calcium-channel
gene.";
Am. J. Hum. Genet. 61:1078-1087(1997).
[12]
POLYMORPHISM, AND INVOLVEMENT IN SCA6 AND EA2.
PubMed=9302278; DOI=10.1093/hmg/6.11.1973;
Jodice C., Mantuano E., Veneziano L., Trettel F., Sabbadini G.,
Calandriello L., Francia A., Spadaro M., Pierelli F., Salvi F.,
Ophoff R.A., Frants R.R., Frontali M.;
"Episodic ataxia type 2 (EA2) and spinocerebellar ataxia type 6 (SCA6)
due to CAG repeat expansion in the CACNA1A gene on chromosome 19p.";
Hum. Mol. Genet. 6:1973-1978(1997).
[13]
VARIANT EA2 HIS-1660.
PubMed=10987655; DOI=10.1007/s004390051099;
Friend K.L., Crimmins D., Phan T.G., Sue C.M., Colley A., Fung V.S.,
Morris J.G., Sutherland G.R., Richards R.I.;
"Detection of a novel missense mutation and second recurrent mutation
in the CACNA1A gene in individuals with EA-2 and FHM.";
Hum. Genet. 105:261-265(1999).
[14]
VARIANT VAL-992, AND VARIANT FHM1 LEU-1455.
PubMed=10408532; DOI=10.1212/WNL.53.1.26;
Carrera P., Piatti M., Stenirri S., Grimaldi L.M., Marchioni E.,
Curcio M., Righetti P.G., Ferrari M., Gelfi C.;
"Genetic heterogeneity in Italian families with familial hemiplegic
migraine.";
Neurology 53:26-33(1999).
[15]
INVOLVEMENT IN EA2, AND VARIANT EA2 1545-ARG--CYS-2506 DEL.
PubMed=10408533;
Jen J., Yue Q., Nelson S.F., Yu H., Litt M., Nutt J., Baloh R.W.;
"A novel nonsense mutation in CACNA1A causes episodic ataxia and
hemiplegia.";
Neurology 53:34-37(1999).
[16]
VARIANT FHM1 LEU-218.
PubMed=11409427; DOI=10.1002/ana.1031;
Kors E.E., Terwindt G.M., Vermeulen F.L., Fitzsimons R.B.,
Jardine P.E., Heywood P., Love S., van den Maagdenberg A.M., Haan J.,
Frants R.R., Ferrari M.D.;
"Delayed cerebral edema and fatal coma after minor head trauma: role
of the CACNA1A calcium channel subunit gene and relationship with
familial hemiplegic migraine.";
Ann. Neurol. 49:753-760(2001).
[17]
VARIANT EA2 LYS-1755.
PubMed=11176968; DOI=10.1001/archneur.58.2.292;
Denier C., Ducros A., Durr A., Eymard B., Chassande B.,
Tournier-Lasserve E.;
"Missense CACNA1A mutation causing episodic ataxia type 2.";
Arch. Neurol. 58:292-295(2001).
[18]
VARIANTS FHM1 LYS-195; GLN-582; MET-665; GLU-714; GLU-1334; CYS-1383;
TRP-1666; ARG-1682 AND ILE-1694.
PubMed=11439943; DOI=10.1056/NEJM200107053450103;
Ducros A., Denier C., Joutel A., Cecillon M., Lescoat C., Vahedi K.,
Darcel F., Vicaut E., Bousser M.G., Tournier-Lasserve E.;
"The clinical spectrum of familial hemiplegic migraine associated with
mutations in a neuronal calcium channel.";
N. Engl. J. Med. 345:17-24(2001).
[19]
VARIANT EA2 CYS-1402, CHARACTERIZATION OF VARIANT EA2 CYS-1402, AND
FUNCTION.
PubMed=11723274; DOI=10.1212/WNL.57.10.1843;
Jen J., Wan J., Graves M., Yu H., Mock A.F., Coulin C.J., Kim G.,
Yue Q., Papazian D.M., Baloh R.W.;
"Loss-of-function EA2 mutations are associated with impaired
neuromuscular transmission.";
Neurology 57:1843-1848(2001).
[20]
VARIANT EA2 TYR-253.
PubMed=12420090; DOI=10.1007/s00415-002-0860-8;
van den Maagdenberg A.M., Kors E.E., Brunt E.R., van Paesschen W.,
Pascual J., Ravine D., Keeling S., Vanmolkot K.R., Vermeulen F.L.,
Terwindt G.M., Haan J., Frants R.R., Ferrari M.D.;
"Episodic ataxia type 2. Three novel truncating mutations and one
novel missense mutation in the CACNA1A gene.";
J. Neurol. 249:1515-1519(2002).
[21]
VARIANT EA2 LEU-1735, CHARACTERIZATION OF VARIANT EA2 LEU-1735, AND
FUNCTION.
PubMed=15293273; DOI=10.1002/ana.20169;
Spacey S.D., Hildebrand M.E., Materek L.A., Bird T.D., Snutch T.P.;
"Functional implications of a novel EA2 mutation in the P/Q-type
calcium channel.";
Ann. Neurol. 56:213-220(2004).
[22]
VARIANT FHM1 GLN-1345.
PubMed=15032980; DOI=10.1111/j..2004.00187.x;
Alonso I., Barros J., Tuna A., Seixas A., Coutinho P., Sequeiros J.,
Silveira I.;
"A novel R1347Q mutation in the predicted voltage sensor segment of
the P/Q-type calcium-channel alpha-subunit in a family with
progressive cerebellar ataxia and hemiplegic migraine.";
Clin. Genet. 65:70-72(2004).
[23]
VARIANTS EA2 ARG-256; ARG-1481; SER-1489; ILE-1492 AND CYS-2134.
PubMed=15173248; DOI=10.1136/jmg.2003.015396;
Mantuano E., Veneziano L., Spadaro M., Giunti P., Guida S.,
Leggio M.G., Verriello L., Wood N., Jodice C., Frontali M.;
"Clusters of non-truncating mutations of P/Q type Ca2+ channel subunit
Ca(v)2.1 causing episodic ataxia 2.";
J. Med. Genet. 41:E82-E82(2004).
[24]
VARIANTS EA2 TYR-287; ARG-293 AND MET-665.
PubMed=14718690; DOI=10.1212/01.WNL.0000101675.61074.50;
Jen J., Kim G.W., Baloh R.W.;
"Clinical spectrum of episodic ataxia type 2.";
Neurology 62:17-22(2004).
[25]
VARIANTS ASP-917; VAL-992 AND SER-1104.
PubMed=16866717; DOI=10.1111/j.1526-4610.2006.00504.x;
von Brevern M., Ta N., Shankar A., Wiste A., Siegel A., Radtke A.,
Sander T., Escayg A.;
"Migrainous vertigo: mutation analysis of the candidate genes CACNA1A,
ATP1A2, SCN1A, and CACNB4.";
Headache 46:1136-1141(2006).
[26]
VARIANT SCA6 GLN-1663.
PubMed=16325861; DOI=10.1016/j.jns.2005.10.007;
Tonelli A., D'Angelo M.G., Salati R., Villa L., Germinasi C.,
Frattini T., Meola G., Turconi A.C., Bresolin N., Bassi M.T.;
"Early onset, non fluctuating spinocerebellar ataxia and a novel
missense mutation in CACNA1A gene.";
J. Neurol. Sci. 241:13-17(2006).
[27]
VARIANT FHM1 GLN-1345.
PubMed=18400034; DOI=10.1111/j.1399-0004.2008.00996.x;
Stam A.H., Vanmolkot K.R., Kremer H.P., Gartner J., Brown J.,
Leshinsky-Silver E., Gilad R., Kors E.E., Frankhuizen W.S.,
Ginjaar H.B., Haan J., Frants R.R., Ferrari M.D.,
van den Maagdenberg A.M., Terwindt G.M.;
"CACNA1A R1347Q: a frequent recurrent mutation in hemiplegic
migraine.";
Clin. Genet. 74:481-485(2008).
[28]
VARIANT EA2 CYS-248.
PubMed=18602318; DOI=10.1016/j.ejpn.2008.02.011;
Zafeiriou D.I., Lehmann-Horn F., Vargiami E., Teflioudi E.,
Ververi A., Jurkat-Rott K.;
"Episodic ataxia type 2 showing ictal hyperhidrosis with hypothermia
and interictal chronic diarrhea due to a novel CACNA1A mutation.";
Eur. J. Paediatr. Neurol. 13:191-193(2009).
[29]
VARIANT EA2 ASP-637, CHARACTERIZATION OF VARIANT EA2 ASP-637, AND
FUNCTION.
PubMed=19232643; DOI=10.1016/j.jns.2009.01.005;
Cuenca-Leon E., Banchs I., Serra S.A., Latorre P.,
Fernandez-Castillo N., Corominas R., Valverde M.A., Volpini V.,
Fernandez-Fernandez J.M., Macaya A., Cormand B.;
"Late-onset episodic ataxia type 2 associated with a novel loss-of-
function mutation in the CACNA1A gene.";
J. Neurol. Sci. 280:10-14(2009).
[30]
VARIANTS ASP-917 AND VAL-992.
PubMed=19429006; DOI=10.1016/j.neulet.2009.01.081;
D'Onofrio M., Ambrosini A., Di Mambro A., Arisi I., Santorelli F.M.,
Grieco G.S., Nicoletti F., Nappi G., Pierelli F., Schoenen J.,
Buzzi M.G.;
"The interplay of two single nucleotide polymorphisms in the CACNA1A
gene may contribute to migraine susceptibility.";
Neurosci. Lett. 453:12-15(2009).
[31]
VARIANT SCA6 THR-405.
PubMed=20682717; DOI=10.1136/jnnp.2008.163402;
Romaniello R., Zucca C., Tonelli A., Bonato S., Baschirotto C.,
Zanotta N., Epifanio R., Righini A., Bresolin N., Bassi M.T.,
Borgatti R.;
"A wide spectrum of clinical, neurophysiological and neuroradiological
abnormalities in a family with a novel CACNA1A mutation.";
J. Neurol. Neurosurg. Psych. 81:840-843(2010).
[32]
VARIANTS EA2 PHE-389; MET-500; THR-797; ARG-896; CYS-1678 AND
ARG-1868.
PubMed=20129625; DOI=10.1016/j.jns.2010.01.010;
Mantuano E., Romano S., Veneziano L., Gellera C., Castellotti B.,
Caimi S., Testa D., Estienne M., Zorzi G., Bugiani M., Rajabally Y.A.,
Barcina M.J., Servidei S., Panico A., Frontali M., Mariotti C.;
"Identification of novel and recurrent CACNA1A gene mutations in
fifteen patients with episodic ataxia type 2.";
J. Neurol. Sci. 291:30-36(2010).
[33]
VARIANT EA2 LYS-388.
PubMed=21696515; DOI=10.1111/j.1442-200X.2011.03390.x;
Nikaido K., Tachi N., Ohya K., Wada T., Tsutsumi H.;
"New mutation of CACNA1A gene in episodic ataxia type 2.";
Pediatr. Int. 53:415-416(2011).
[34]
VARIANT FHM1 PHE-1501 DEL, CHARACTERIZATION OF VARIANT FHM1 PHE-1501
DEL, AND FUNCTION.
PubMed=24836863; DOI=10.1016/j.jns.2014.04.027;
Garcia Segarra N., Gautschi I., Mittaz-Crettol L., Kallay Zetchi C.,
Al-Qusairi L., Van Bemmelen M.X., Maeder P., Bonafe L., Schild L.,
Roulet-Perez E.;
"Congenital ataxia and hemiplegic migraine with cerebral edema
associated with a novel gain of function mutation in the calcium
channel CACNA1A.";
J. Neurol. Sci. 342:69-78(2014).
[35]
VARIANT FHM1 PHE-1501 DEL, CHARACTERIZATION OF VARIANT FHM1 PHE-1501
DEL, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26716990; DOI=10.1371/journal.pone.0146035;
Bahamonde M.I., Serra S.A., Drechsel O., Rahman R., Marce-Grau A.,
Prieto M., Ossowski S., Macaya A., Fernandez-Fernandez J.M.;
"A single amino acid deletion (deltaf1502) in the s6 segment of cav2.1
domain iii associated with congenital ataxia increases channel
activity and promotes ca2+ influx.";
PLoS ONE 10:E0146035-E0146035(2015).
[36]
INVOLVEMENT IN EIEE42, AND VARIANTS EIEE42 GLN-101; THR-712 AND
SER-1507.
PubMed=27476654; DOI=10.1016/j.ajhg.2016.06.003;
Epi4K Consortium;
"De novo mutations in SLC1A2 and CACNA1A are important causes of
epileptic encephalopathies.";
Am. J. Hum. Genet. 99:287-298(2016).
[37]
VARIANT EIEE42 ARG-1435.
PubMed=27250579; DOI=10.1002/ajmg.a.37678;
Reinson K., Oiglane-Shlik E., Talvik I., Vaher U., Ounapuu A.,
Ennok M., Teek R., Pajusalu S., Murumets U., Tomberg T., Puusepp S.,
Piirsoo A., Reimand T., Ounap K.;
"Biallelic CACNA1A mutations cause early onset epileptic
encephalopathy with progressive cerebral, cerebellar, and optic nerve
atrophy.";
Am. J. Med. Genet. A 170:2173-2176(2016).
[38]
VARIANTS SCA6 GLN-582; TYR-1337 AND 1545-ARG--CYS-2506 DEL.
PubMed=29053796; DOI=10.1093/brain/awx251;
Nibbeling E.A.R., Duarri A., Verschuuren-Bemelmans C.C., Fokkens M.R.,
Karjalainen J.M., Smeets C.J.L.M., de Boer-Bergsma J.J.,
van der Vries G., Dooijes D., Bampi G.B., van Diemen C., Brunt E.,
Ippel E., Kremer B., Vlak M., Adir N., Wijmenga C.,
van de Warrenburg B.P.C., Franke L., Sinke R.J., Verbeek D.S.;
"Exome sequencing and network analysis identifies shared mechanisms
underlying spinocerebellar ataxia.";
Brain 140:2860-2878(2017).
[39]
VARIANT FHM1 GLN-582.
PubMed=28900389; DOI=10.3389/fncel.2017.00263;
Khaiboullina S.F., Mendelevich E.G., Shigapova L.H.,
Shagimardanova E., Gazizova G., Nikitin A., Martynova E.,
Davidyuk Y.N., Bogdanov E.I., Gusev O., van den Maagdenberg A.M.J.M.,
Giniatullin R.A., Rizvanov A.A.;
"Cerebellar Atrophy and Changes in Cytokines Associated with the
CACNA1A R583Q Mutation in a Russian Familial Hemiplegic Migraine Type
1 Family.";
Front. Cell. Neurosci. 11:263-263(2017).
[40]
VARIANTS GLN-1663 AND PRO-1672, AND CHARACTERIZATION OF VARIANTS
GLN-1663 AND PRO-1672.
PubMed=28742085; DOI=10.1371/journal.pgen.1006905;
Members of the UDN;
Luo X., Rosenfeld J.A., Yamamoto S., Harel T., Zuo Z., Hall M.,
Wierenga K.J., Pastore M.T., Bartholomew D., Delgado M.R.,
Rotenberg J., Lewis R.A., Emrick L., Bacino C.A., Eldomery M.K.,
Coban Akdemir Z., Xia F., Yang Y., Lalani S.R., Lotze T., Lupski J.R.,
Lee B., Bellen H.J., Wangler M.F.;
"Clinically severe CACNA1A alleles affect synaptic function and
neurodegeneration differentially.";
PLoS Genet. 13:E1006905-E1006905(2017).
-!- FUNCTION: Voltage-sensitive calcium channels (VSCC) 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, gene expression,
cell motility, cell division and cell death. The isoform alpha-1A
gives rise to P and/or Q-type calcium currents. P/Q-type calcium
channels belong to the 'high-voltage activated' (HVA) group and
are specifically blocked by the spider omega-agatoxin-IVA (AC
P54282) (By similarity). They are however insensitive to
dihydropyridines (DHP). {ECO:0000250|UniProtKB:P54282,
ECO:0000269|PubMed:10049321, ECO:0000269|PubMed:10753886,
ECO:0000269|PubMed:11723274, ECO:0000269|PubMed:15293273,
ECO:0000269|PubMed:19232643, ECO:0000269|PubMed:24836863,
ECO:0000269|PubMed:26716990}.
-!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
complexes, consisting of alpha-1, alpha-2, beta and delta subunits
in a 1:1:1:1 ratio. The channel activity is directed by the pore-
forming and voltage-sensitive alpha-1 subunit. In many cases, this
subunit is sufficient to generate voltage-sensitive calcium
channel activity. The auxiliary subunits beta and alpha-2/delta
linked by a disulfide bridge regulate the channel activity.
Interact (via C-terminal CDB motif) with CABP1 in the pre- and
postsynaptic membranes. Interacts with the spider omega-agatoxin-
IVA (AC P30288). {ECO:0000250|UniProtKB:P54282,
ECO:0000269|PubMed:11865310}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=2; IntAct=EBI-766279, EBI-375446;
O94910:ADGRL1; NbExp=2; IntAct=EBI-766279, EBI-3389315;
Q86SJ2:AMIGO2; NbExp=2; IntAct=EBI-766279, EBI-3866830;
Q7Z5H3:ARHGAP22; NbExp=2; IntAct=EBI-766279, EBI-3866859;
P67870:CSNK2B; NbExp=2; IntAct=EBI-766279, EBI-348169;
O75953:DNAJB5; NbExp=2; IntAct=EBI-766279, EBI-5655937;
P28799:GRN; NbExp=2; IntAct=EBI-766279, EBI-747754;
P15822:HIVEP1; NbExp=2; IntAct=EBI-766279, EBI-722264;
Q8N2S1:LTBP4; NbExp=2; IntAct=EBI-766279, EBI-947718;
O00339:MATN2; NbExp=2; IntAct=EBI-766279, EBI-949020;
O75095:MEGF6; NbExp=2; IntAct=EBI-766279, EBI-947597;
Q7Z7M0:MEGF8; NbExp=2; IntAct=EBI-766279, EBI-947617;
Q9UHX1:PUF60; NbExp=2; IntAct=EBI-766279, EBI-1053259;
Q8IXT5:RBM12B; NbExp=2; IntAct=EBI-766279, EBI-3044077;
O95153:TSPOAP1; NbExp=2; IntAct=EBI-766279, EBI-5915931;
Q9BVA1:TUBB2B; NbExp=2; IntAct=EBI-766279, EBI-355665;
P22695:UQCRC2; NbExp=2; IntAct=EBI-766279, EBI-1051424;
P49750:YLPM1; NbExp=2; IntAct=EBI-766279, EBI-712871;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10049321,
ECO:0000269|PubMed:26716990}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=1A-1, BI-1-GGCAG {ECO:0000303|PubMed:8988170};
IsoId=O00555-8; Sequence=Displayed;
Name=2; Synonyms=1A-2, BI-1 {ECO:0000303|PubMed:8988170};
IsoId=O00555-2; Sequence=VSP_059675, VSP_059676, VSP_059677,
VSP_059681;
Name=3; Synonyms=BI-1(V1) {ECO:0000303|PubMed:8988170};
IsoId=O00555-3; Sequence=VSP_059675, VSP_059678, VSP_059679,
VSP_059681;
Name=4; Synonyms=BI-1(V1)-GGCAG {ECO:0000303|PubMed:8988170};
IsoId=O00555-4; Sequence=VSP_059675, VSP_059678, VSP_059679,
VSP_059682;
Name=5; Synonyms=BI-1(V2) {ECO:0000303|PubMed:8988170};
IsoId=O00555-5; Sequence=VSP_059675, VSP_059680, VSP_059681;
Name=6; Synonyms=BI-1(V2)-GGCAG {ECO:0000303|PubMed:8988170};
IsoId=O00555-6; Sequence=VSP_059675, VSP_059680, VSP_059682;
-!- TISSUE SPECIFICITY: Brain specific; mainly found in cerebellum,
cerebral cortex, thalamus and hypothalamus. Expressed in the small
cell lung carcinoma cell line SCC-9. No expression in heart,
kidney, liver or muscle. Purkinje cells contain predominantly P-
type VSCC, the Q-type being a prominent calcium current in
cerebellar granule cells. {ECO:0000269|PubMed:1335101}.
-!- DOMAIN: Each of the four internal repeats contains five
hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
positively charged transmembrane segment (S4). S4 segments
probably represent the voltage-sensor and are characterized by a
series of positively charged amino acids at every third position.
-!- POLYMORPHISM: The poly-Gln region of CACNA1A is polymorphic: 6 to
17 repeats in the normal population, expanded to about 21 to 30
repeats in SCA6. Repeat expansion has been reported also in a EA2
family. {ECO:0000269|PubMed:9302278}.
-!- DISEASE: Spinocerebellar ataxia 6 (SCA6) [MIM:183086]:
Spinocerebellar ataxia is a clinically and genetically
heterogeneous group of cerebellar disorders. Patients show
progressive incoordination of gait and often poor coordination of
hands, speech and eye movements, due to degeneration of the
cerebellum with variable involvement of the brainstem and spinal
cord. SCA6 is an autosomal dominant cerebellar ataxia (ADCA),
mainly caused by expansion of a CAG repeat in the coding region of
CACNA1A. There seems to be a correlation between the repeat number
and earlier onset of the disorder. {ECO:0000269|PubMed:16325861,
ECO:0000269|PubMed:20682717, ECO:0000269|PubMed:29053796,
ECO:0000269|PubMed:8988170, ECO:0000269|PubMed:9302278,
ECO:0000269|PubMed:9345107}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Migraine, familial hemiplegic, 1 (FHM1) [MIM:141500]: A
subtype of migraine with aura associated with ictal hemiparesis
and, in some families, cerebellar ataxia and atrophy. Migraine is
a disabling symptom complex of periodic headaches, usually
temporal and unilateral. Headaches are often accompanied by
irritability, nausea, vomiting and photophobia, preceded by
constriction of the cranial arteries. Migraine with aura is
characterized by recurrent attacks of reversible neurological
symptoms (aura) that precede or accompany the headache. Aura may
include a combination of sensory disturbances, such as blurred
vision, hallucinations, vertigo, numbness and difficulty in
concentrating and speaking. {ECO:0000269|PubMed:10408532,
ECO:0000269|PubMed:11409427, ECO:0000269|PubMed:11439943,
ECO:0000269|PubMed:15032980, ECO:0000269|PubMed:18400034,
ECO:0000269|PubMed:24836863, ECO:0000269|PubMed:26716990,
ECO:0000269|PubMed:28900389, ECO:0000269|PubMed:8898206}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Episodic ataxia 2 (EA2) [MIM:108500]: An autosomal
dominant disorder characterized by acetozolamide-responsive
attacks of ataxia, migraine-like symptoms, interictal nystagmus,
and cerebellar atrophy. {ECO:0000269|PubMed:10408533,
ECO:0000269|PubMed:10987655, ECO:0000269|PubMed:11176968,
ECO:0000269|PubMed:11723274, ECO:0000269|PubMed:12420090,
ECO:0000269|PubMed:14718690, ECO:0000269|PubMed:15173248,
ECO:0000269|PubMed:15293273, ECO:0000269|PubMed:18602318,
ECO:0000269|PubMed:19232643, ECO:0000269|PubMed:20129625,
ECO:0000269|PubMed:21696515, ECO:0000269|PubMed:8898206,
ECO:0000269|PubMed:9302278}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epileptic encephalopathy, early infantile, 42 (EIEE42)
[MIM:617106]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent. EIEE42
inheritance is autosomal dominant. {ECO:0000269|PubMed:27250579,
ECO:0000269|PubMed:27476654}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB49678.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Calcium channel, voltage-dependent, P/Q type,
alpha 1A subunit (CACNA1A); Note=Leiden Open Variation Database
(LOVD);
URL="http://chromium.lovd.nl/LOVD2/home.php?select_db=CACNA1A";
-!- WEB RESOURCE: Name=Familial hemiplegic migraine (FHM) variation
database, calcium channel, voltage-dependent, P/Q type, alpha 1A
subunit (CACNA1A); Note=Leiden Open Variation Database (LOVD);
URL="http://grenada.lumc.nl/LOVD2/FHM/home.php?select_db=CACNA1A";
-!- WEB RESOURCE: Name=Undiagnosed Disease Network; Note=CACNA1A;
URL="https://undiagnosed.hms.harvard.edu/updates/genes-of-interest/cacna1a-gene/";
-----------------------------------------------------------------------
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EMBL; AF004883; AAB61612.1; -; mRNA.
EMBL; AF004884; AAB61613.1; -; mRNA.
EMBL; X99897; CAA68172.1; -; mRNA.
EMBL; Z80114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z80115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U79663; AAB49674.1; -; mRNA.
EMBL; U79664; AAB49675.1; -; mRNA.
EMBL; U79665; AAB49676.1; -; mRNA.
EMBL; U79666; AAB64179.1; -; mRNA.
EMBL; U79667; AAB49677.1; -; mRNA.
EMBL; U79668; AAB49678.1; ALT_SEQ; mRNA.
EMBL; AB035727; BAA94766.2; -; mRNA.
EMBL; AC005305; AAC26839.1; -; Genomic_DNA.
EMBL; AC005513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S76537; AAB33068.1; -; mRNA.
EMBL; U06702; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS45998.1; -. [O00555-8]
CCDS; CCDS45999.1; -. [O00555-3]
RefSeq; NP_000059.3; NM_000068.3.
RefSeq; NP_001120693.1; NM_001127221.1. [O00555-3]
RefSeq; NP_001120694.1; NM_001127222.1. [O00555-8]
RefSeq; NP_001167551.1; NM_001174080.1.
RefSeq; NP_075461.2; NM_023035.2.
UniGene; Hs.501632; -.
PDB; 3BXK; X-ray; 2.55 A; B/D=1954-1974.
PDBsum; 3BXK; -.
ProteinModelPortal; O00555; -.
SMR; O00555; -.
BioGrid; 107227; 100.
CORUM; O00555; -.
IntAct; O00555; 92.
MINT; O00555; -.
STRING; 9606.ENSP00000353362; -.
BindingDB; O00555; -.
ChEMBL; CHEMBL4266; -.
DrugBank; DB01244; Bepridil.
DrugBank; DB00836; Loperamide.
DrugBank; DB00230; Pregabalin.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00661; Verapamil.
TCDB; 1.A.1.11.27; the voltage-gated ion channel (vic) superfamily.
iPTMnet; O00555; -.
PhosphoSitePlus; O00555; -.
BioMuta; CACNA1A; -.
MaxQB; O00555; -.
PaxDb; O00555; -.
PeptideAtlas; O00555; -.
PRIDE; O00555; -.
ProteomicsDB; 47966; -.
ProteomicsDB; 47967; -. [O00555-2]
ProteomicsDB; 47968; -. [O00555-3]
ProteomicsDB; 47969; -. [O00555-4]
ProteomicsDB; 47970; -. [O00555-5]
ProteomicsDB; 47971; -. [O00555-6]
DNASU; 773; -.
Ensembl; ENST00000360228; ENSP00000353362; ENSG00000141837. [O00555-8]
Ensembl; ENST00000637276; ENSP00000489777; ENSG00000141837. [O00555-5]
Ensembl; ENST00000637432; ENSP00000490617; ENSG00000141837. [O00555-2]
Ensembl; ENST00000638009; ENSP00000489913; ENSG00000141837. [O00555-3]
GeneID; 773; -.
KEGG; hsa:773; -.
UCSC; uc002mwy.5; human. [O00555-8]
CTD; 773; -.
DisGeNET; 773; -.
EuPathDB; HostDB:ENSG00000141837.18; -.
GeneCards; CACNA1A; -.
GeneReviews; CACNA1A; -.
HGNC; HGNC:1388; CACNA1A.
HPA; HPA064258; -.
HPA; HPA071902; -.
MalaCards; CACNA1A; -.
MIM; 108500; phenotype.
MIM; 141500; phenotype.
MIM; 183086; phenotype.
MIM; 601011; gene.
MIM; 617106; phenotype.
neXtProt; NX_O00555; -.
OpenTargets; ENSG00000141837; -.
Orphanet; 2131; Alternating hemiplegia of childhood.
Orphanet; 71518; Benign paroxysmal torticollis of infancy.
Orphanet; 569; Familial or sporadic hemiplegic migraine.
Orphanet; 97; Familial paroxysmal ataxia.
Orphanet; 98758; Spinocerebellar ataxia type 6.
PharmGKB; PA26007; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; O00555; -.
KO; K04344; -.
PhylomeDB; O00555; -.
TreeFam; TF312805; -.
Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-HSA-422356; Regulation of insulin secretion.
ChiTaRS; CACNA1A; human.
EvolutionaryTrace; O00555; -.
GeneWiki; Cav2.1; -.
GenomeRNAi; 773; -.
PRO; PR:O00555; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000141837; Expressed in 198 organ(s), highest expression level in right hemisphere of cerebellum.
ExpressionAtlas; O00555; baseline and differential.
Genevisible; O00555; HS.
GO; GO:0042995; C:cell projection; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019905; F:syntaxin binding; IDA:UniProtKB.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0008219; P:cell death; IDA:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
GO; GO:0051899; P:membrane depolarization; TAS:Reactome.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:1904645; P:response to amyloid-beta; IDA:ARUK-UCL.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR005448; CACNA1A.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR002077; VDCCAlpha1.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01632; PQVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Cell membrane; Complete proteome; Disease mutation;
Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport;
Membrane; Metal-binding; Neurodegeneration; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Spinocerebellar ataxia;
Transmembrane; Transmembrane helix; Transport;
Triplet repeat expansion; Voltage-gated channel.
CHAIN 1 2506 Voltage-dependent P/Q-type calcium
channel subunit alpha-1A.
/FTId=PRO_0000053916.
TOPO_DOM 1 98 Cytoplasmic. {ECO:0000255}.
TRANSMEM 99 117 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 118 135 Extracellular. {ECO:0000255}.
TRANSMEM 136 155 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 156 167 Cytoplasmic. {ECO:0000255}.
TRANSMEM 168 185 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 186 190 Extracellular. {ECO:0000255}.
TRANSMEM 191 209 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 210 228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 229 248 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 249 335 Extracellular. {ECO:0000255}.
TRANSMEM 336 360 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 361 486 Cytoplasmic. {ECO:0000255}.
TRANSMEM 487 505 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 506 520 Extracellular. {ECO:0000255}.
TRANSMEM 521 540 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 541 548 Cytoplasmic. {ECO:0000255}.
TRANSMEM 549 567 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 568 577 Extracellular. {ECO:0000255}.
TRANSMEM 578 596 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 597 615 Cytoplasmic. {ECO:0000255}.
TRANSMEM 616 635 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 636 688 Extracellular. {ECO:0000255}.
TRANSMEM 689 713 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 714 1241 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1242 1260 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1261 1276 Extracellular. {ECO:0000255}.
TRANSMEM 1277 1296 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1297 1308 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1309 1327 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1328 1338 Extracellular. {ECO:0000255}.
TRANSMEM 1339 1357 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1358 1376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1377 1396 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1397 1483 Extracellular. {ECO:0000255}.
TRANSMEM 1484 1508 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1509 1563 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1564 1592 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1593 1597 Extracellular. {ECO:0000255}.
TRANSMEM 1598 1617 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1618 1625 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1626 1644 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1645 1651 Extracellular. {ECO:0000255}.
TRANSMEM 1652 1670 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1671 1689 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1690 1709 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1710 1781 Extracellular. {ECO:0000255}.
TRANSMEM 1782 1806 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1807 2506 Cytoplasmic. {ECO:0000255}.
REPEAT 85 363 I.
REPEAT 472 716 II.
REPEAT 1230 1513 III.
REPEAT 1550 1813 IV.
CA_BIND 1839 1850 {ECO:0000250}.
REGION 383 400 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 13 18 Poly-Gly.
COMPBIAS 726 731 Poly-Glu.
COMPBIAS 1001 1006 Poly-Arg.
COMPBIAS 1203 1206 Poly-Glu.
COMPBIAS 2210 2219 Poly-His.
COMPBIAS 2220 2223 Poly-Pro.
COMPBIAS 2313 2323 Poly-Gln.
SITE 318 318 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 667 667 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1459 1459 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1648 1648 Binds to omega-Aga-IVA. {ECO:0000250}.
SITE 1755 1755 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 409 409 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 749 749 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 789 789 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1084 1084 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1093 1093 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1821 1821 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1983 1983 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2046 2046 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2064 2064 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2076 2076 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2078 2078 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2119 2119 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2139 2139 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 418 418 D -> DG (in isoform 2, isoform 3, isoform
4, isoform 5 and isoform 6).
/FTId=VSP_059675.
VAR_SEQ 724 724 K -> KVEA (in isoform 2).
/FTId=VSP_059676.
VAR_SEQ 1650 1650 G -> GNP (in isoform 2).
/FTId=VSP_059677.
VAR_SEQ 1843 1858 WGRMPYLDMYQMLRHM -> CGRIHYKDMYSLLRVI (in
isoform 3 and isoform 4).
/FTId=VSP_059678.
VAR_SEQ 1870 1874 ARVAY -> HRVAC (in isoform 3 and isoform
4).
/FTId=VSP_059679.
VAR_SEQ 2102 2113 Missing (in isoform 5 and isoform 6).
/FTId=VSP_059680.
VAR_SEQ 2261 2506 Missing (in isoform 2, isoform 3 and
isoform 5).
/FTId=VSP_059681.
VAR_SEQ 2323 2324 Missing (in isoform 4 and isoform 6).
/FTId=VSP_059682.
VARIANT 21 21 A -> V (in dbSNP:rs15999).
/FTId=VAR_014456.
VARIANT 101 101 E -> Q (in EIEE42).
{ECO:0000269|PubMed:27476654}.
/FTId=VAR_077071.
VARIANT 192 192 R -> Q (in FHM1; dbSNP:rs121908211).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_001491.
VARIANT 195 195 R -> K (in FHM1; dbSNP:rs121908222).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043820.
VARIANT 218 218 S -> L (in FHM1; dbSNP:rs121908225).
{ECO:0000269|PubMed:11409427}.
/FTId=VAR_043821.
VARIANT 248 248 Y -> C (in EA2; dbSNP:rs121908238).
{ECO:0000269|PubMed:18602318}.
/FTId=VAR_063683.
VARIANT 253 253 H -> Y (in EA2; dbSNP:rs121908228).
{ECO:0000269|PubMed:12420090}.
/FTId=VAR_043822.
VARIANT 256 256 C -> R (in EA2; dbSNP:rs121908231).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043823.
VARIANT 287 287 C -> Y (in EA2; dbSNP:rs121908236).
{ECO:0000269|PubMed:14718690}.
/FTId=VAR_043824.
VARIANT 293 293 G -> R (in EA2 and SCA6;
dbSNP:rs121908215).
{ECO:0000269|PubMed:14718690,
ECO:0000269|PubMed:9345107}.
/FTId=VAR_043825.
VARIANT 388 388 E -> K (in EA2).
{ECO:0000269|PubMed:21696515}.
/FTId=VAR_067342.
VARIANT 389 389 L -> F (in EA2; dbSNP:rs121908239).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063684.
VARIANT 405 405 A -> T (in SCA6; dbSNP:rs121908245).
{ECO:0000269|PubMed:20682717}.
/FTId=VAR_063685.
VARIANT 453 453 A -> T (in dbSNP:rs41276886).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_063686.
VARIANT 500 500 T -> M (in EA2; dbSNP:rs121908240).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063687.
VARIANT 582 582 R -> Q (in FHM1 and SCA6;
dbSNP:rs121908217).
{ECO:0000269|PubMed:11439943,
ECO:0000269|PubMed:28900389,
ECO:0000269|PubMed:29053796}.
/FTId=VAR_043826.
VARIANT 637 637 G -> D (in EA2; reduces P/Q current
densities; dbSNP:rs121908246).
{ECO:0000269|PubMed:19232643}.
/FTId=VAR_063688.
VARIANT 665 665 T -> M (in FHM1 and EA2;
dbSNP:rs121908212).
{ECO:0000269|PubMed:11439943,
ECO:0000269|PubMed:14718690,
ECO:0000269|PubMed:8898206}.
/FTId=VAR_001492.
VARIANT 712 712 A -> T (in EIEE42).
{ECO:0000269|PubMed:27476654}.
/FTId=VAR_077072.
VARIANT 713 713 V -> A (in FHM1; dbSNP:rs121908213).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_001493.
VARIANT 714 714 D -> E (in FHM1; dbSNP:rs121908218).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043827.
VARIANT 731 731 E -> A (in dbSNP:rs16019).
/FTId=VAR_059221.
VARIANT 797 797 M -> T (in EA2; dbSNP:rs121908241).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063689.
VARIANT 896 896 P -> R (in EA2; dbSNP:rs121908242).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063690.
VARIANT 913 913 P -> S (in dbSNP:rs16020).
/FTId=VAR_014458.
VARIANT 917 917 E -> D (in dbSNP:rs16022).
{ECO:0000269|PubMed:16866717,
ECO:0000269|PubMed:19429006}.
/FTId=VAR_014459.
VARIANT 992 992 E -> V (in dbSNP:rs16023).
{ECO:0000269|PubMed:10408532,
ECO:0000269|PubMed:16866717,
ECO:0000269|PubMed:19429006}.
/FTId=VAR_043828.
VARIANT 1014 1014 E -> K (in dbSNP:rs16024).
/FTId=VAR_014461.
VARIANT 1104 1104 G -> S (in dbSNP:rs16027).
{ECO:0000269|PubMed:10753886,
ECO:0000269|PubMed:16866717}.
/FTId=VAR_014462.
VARIANT 1172 1172 P -> L (in dbSNP:rs16028).
/FTId=VAR_059222.
VARIANT 1334 1334 K -> E (in FHM1; dbSNP:rs121908223).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043829.
VARIANT 1337 1337 D -> Y (in SCA6).
{ECO:0000269|PubMed:29053796}.
/FTId=VAR_080738.
VARIANT 1345 1345 R -> Q (in FHM1; with progressive
cerebellar ataxia; dbSNP:rs121908230).
{ECO:0000269|PubMed:15032980,
ECO:0000269|PubMed:18400034}.
/FTId=VAR_043830.
VARIANT 1383 1383 Y -> C (in FHM1; dbSNP:rs121908219).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043831.
VARIANT 1402 1402 F -> C (in EA2; loss of function;
dbSNP:rs121908227).
{ECO:0000269|PubMed:11723274}.
/FTId=VAR_043832.
VARIANT 1435 1435 W -> R (in EIEE42).
{ECO:0000269|PubMed:27250579}.
/FTId=VAR_077073.
VARIANT 1455 1455 V -> L (in FHM1; dbSNP:rs121908237).
{ECO:0000269|PubMed:10408532}.
/FTId=VAR_043833.
VARIANT 1481 1481 G -> R (in EA2; dbSNP:rs121908232).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043834.
VARIANT 1489 1489 F -> S (in EA2; dbSNP:rs121908233).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043835.
VARIANT 1492 1492 V -> I (in EA2; dbSNP:rs121908234).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043836.
VARIANT 1501 1501 Missing (in FHM1; increased high voltage-
gated calcium channel activity).
{ECO:0000269|PubMed:24836863,
ECO:0000269|PubMed:26716990}.
/FTId=VAR_077074.
VARIANT 1507 1507 A -> S (in EIEE42).
{ECO:0000269|PubMed:27476654}.
/FTId=VAR_077075.
VARIANT 1545 2506 Missing (in EA2 and SCA6).
{ECO:0000269|PubMed:10408533,
ECO:0000269|PubMed:29053796}.
/FTId=VAR_080739.
VARIANT 1660 1660 R -> H (in EA2; dbSNP:rs121908216).
{ECO:0000269|PubMed:10987655}.
/FTId=VAR_043837.
VARIANT 1663 1663 R -> Q (in SCA6; also found in patients
with global developmental delay and
congenital ataxia; loss of function
observed in the Drosophila homolog;
dbSNP:rs121908247).
{ECO:0000250|UniProtKB:P91645,
ECO:0000269|PubMed:16325861,
ECO:0000269|PubMed:28742085}.
/FTId=VAR_063691.
VARIANT 1666 1666 R -> W (in FHM1; dbSNP:rs121908220).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043838.
VARIANT 1672 1672 R -> P (also found in patients with
global developmental delay and congenital
ataxia; gain of function observed in the
Drosophila homolog).
{ECO:0000250|UniProtKB:P91645,
ECO:0000269|PubMed:28742085}.
/FTId=VAR_079826.
VARIANT 1678 1678 R -> C (in EA2; dbSNP:rs121908243).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063692.
VARIANT 1682 1682 W -> R (in FHM1; dbSNP:rs121908221).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043839.
VARIANT 1694 1694 V -> I (in FHM1; dbSNP:rs121908224).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_063706.
VARIANT 1735 1735 H -> L (in EA2; changed high voltage-
gated calcium channel activity;
dbSNP:rs121908229).
{ECO:0000269|PubMed:15293273}.
/FTId=VAR_043840.
VARIANT 1755 1755 E -> K (in EA2; dbSNP:rs121908226).
{ECO:0000269|PubMed:11176968}.
/FTId=VAR_043841.
VARIANT 1809 1809 I -> L (in FHM1; dbSNP:rs121908214).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_001494.
VARIANT 1868 1868 C -> R (in EA2; dbSNP:rs121908244).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063693.
VARIANT 2134 2134 R -> C (in EA2; dbSNP:rs121908235).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043842.
VARIANT 2395 2395 P -> S (in dbSNP:rs16056).
/FTId=VAR_014463.
CONFLICT 895 895 G -> D (in Ref. 2; CAA68172 and 4;
BAA94766). {ECO:0000305}.
CONFLICT 952 952 D -> N (in Ref. 4; BAA94766).
{ECO:0000305}.
CONFLICT 963 963 R -> S (in Ref. 4; BAA94766).
{ECO:0000305}.
CONFLICT 1206 1206 E -> EE (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1312 1314 WNI -> ILP (in Ref. 3; AAB49674/AAB49675/
AAB49676/AAB49677/AAB49678).
{ECO:0000305}.
CONFLICT 1458 1458 G -> A (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1603 1603 V -> A (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1616 1616 V -> A (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1692 1692 P -> A (in Ref. 6; AAB33068).
{ECO:0000305}.
CONFLICT 2037 2037 E -> G (in Ref. 8; U06702).
{ECO:0000305}.
CONFLICT 2325 2325 Missing (in Ref. 3; AAB49676/AAB49677).
{ECO:0000305}.
HELIX 1 1969 {ECO:0000244|PDB:3BXK}.
SEQUENCE 2506 AA; 282564 MW; AEDF4D2A5E49263F CRC64;
MARFGDEMPA RYGGGGSGAA AGVVVGSGGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA
LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH
LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG
ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF
AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTKCQPY WEGPNNGITQ
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS
GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD GEQRHPFDAL
RRTTIKKSKT DLLNPEEAED QLADIASVGS PFARASIKSA KLENSTFFHK KERRMRFYIR
RMVKTQAFYW TVLSLVALNT LCVAIVHYNQ PEWLSDFLYY AEFIFLGLFM SEMFIKMYGL
GTRPYFHSSF NCFDCGVIIG SIFEVIWAVI KPGTSFGISV LRALRLLRIF KVTKYWASLR
NLVVSLLNSM KSIISLLFLL FLFIVVFALL GMQLFGGQFN FDEGTPPTNF DTFPAAIMTV
FQILTGEDWN EVMYDGIKSQ GGVQGGMVFS IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ
ELTKDEQEEE EAANQKLALQ KAKEVAEVSP LSAANMSIAV KEQQKNQKPA KSVWEQRTSE
MRKQNLLASR EALYNEMDPD ERWKAAYTRH LRPDMKTHLD RPLVVDPQEN RNNNTNKSRA
AEPTVDQRLG QQRAEDFLRK QARYHDRARD PSGSAGLDAR RPWAGSQEAE LSREGPYGRE
SDHHAREGSL EQPGFWEGEA ERGKAGDPHR RHVHRQGGSR ESRSGSPRTG ADGEHRRHRA
HRRPGEEGPE DKAERRARHR EGSRPARGGE GEGEGPDGGE RRRRHRHGAP ATYEGDARRE
DKERRHRRRK ENQGSGVPVS GPNLSTTRPI QQDLGRQDPP LAEDIDNMKN NKLATAESAA
PHGSLGHAGL PQSPAKMGNS TDPGPMLAIP AMATNPQNAA SRRTPNNPGN PSNPGPPKTP
ENSLIVTNPS GTQTNSAKTA RKPDHTTVDI PPACPPPLNH TVVQVNKNAN PDPLPKKEEE
KKEEEEDDRG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL NLRYFEMCIL MVIAMSSIAL
AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE MVIKMIDLGL VLHQGAYFRD LWNILDFIVV
SGALVAFAFT GNSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVFNIL
IVYMLFMFIF AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA RDREWKKYEF
HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY VVYFVVFPFF
FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA KPLTRHMPQN KQSFQYRMWQ
FVVSPPFEYT IMAMIALNTI VLMMKFYGAS VAYENALRVF NIVFTSLFSL ECVLKVMAFG
ILNYFRDAWN IFDFVTVLGS ITDILVTEFG NNFINLSFLR LFRAARLIKL LRQGYTIRIL
LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIGIDV EDEDSDEDEF QITEHNNFRT
FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTRE CGNEFAYFYF VSFIFLCSFL
MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP AAWGRMPYLD MYQMLRHMSP
PLGLGKKCPA RVAYKRLLRM DLPVADDNTV HFNSTLMALI RTALDIKIAK GGADKQQMDA
ELRKEMMAIW PNLSQKTLDL LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA KKLQAMREEQ
DRTPLMFQRM EPPSPTQEGG PGQNALPSTQ LDPGGALMAH ESGLKESPSW VTQRAQEMFQ
KTGTWSPEQG PPTDMPNSQP NSQSVEMREM GRDGYSDSEH YLPMEGQGRA ASMPRLPAEN
QRRRGRPRGN NLSTISDTSP MKRSASVLGP KARRLDDYSL ERVPPEENQR HHQRRRDRSH
RASERSLGRY TDVDTGLGTD LSMTTQSGDL PSKERDQERG RPKDRKHRQH HHHHHHHHHP
PPPDKDRYAQ ERPDHGRARA RDQRWSRSPS EGREHMAHRQ GSSSVSGSPA PSTSGTSTPR
RGRRQLPQTP STPRPHVSYS PVIRKAGGSG PPQQQQQQQQ QQQQQAVARP GRAATSGPRR
YPGPTAEPLA GDRPPTGGHS SGRSPRMERR VPGPARSESP RACRHGGARW PASGPHVSEG
PPGPRHHGYY RGSDYDEADG PGSGGGEEAM AGAYDAPPPV RHASSGATGR SPRTPRASGP
ACASPSRHGR RLPNGYYPAH GLARPRGPGS RKGLHEPYSE SDDDWC


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