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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;        2505 AA.
O00555; J3KP41; P78510; P78511; Q16290; Q92690; Q99790; Q99791;
Q99792; Q99793; Q9NS88; Q9UDC4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
25-OCT-2017, entry version 186.
RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
AltName: Full=Brain calcium channel I;
Short=BI;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
Name=CACNA1A; 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-666; ALA-714 AND LEU-1810, VARIANT THR-454, 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
1313-2505 (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 8), VARIANT SER-1105, 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 1693-1807.
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 1702-1822, 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 2038-2258 (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 1955-1975.
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-1661.
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-993, AND VARIANT FHM1 LEU-1456.
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]
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).
[16]
VARIANT EA2 LYS-1756.
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).
[17]
VARIANTS FHM1 LYS-195; GLN-583; MET-666; GLU-715; GLU-1335; CYS-1384;
TRP-1667; ARG-1683 AND ILE-1695.
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).
[18]
VARIANT EA2 CYS-1403, CHARACTERIZATION OF VARIANT EA2 CYS-1403, 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).
[19]
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).
[20]
VARIANT EA2 LEU-1736, CHARACTERIZATION OF VARIANT EA2 LEU-1736, 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).
[21]
VARIANT FHM1 GLN-1346.
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).
[22]
VARIANTS EA2 ARG-256; ARG-1482; SER-1490; ILE-1493 AND CYS-2135.
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).
[23]
VARIANTS EA2 TYR-287; ARG-293 AND MET-666.
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).
[24]
VARIANTS ASP-918; VAL-993 AND SER-1105.
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).
[25]
VARIANT SCA6 GLN-1664.
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).
[26]
VARIANT FHM1 GLN-1346.
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).
[27]
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).
[28]
VARIANT EA2 ASP-638, CHARACTERIZATION OF VARIANT EA2 ASP-638, 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).
[29]
VARIANTS ASP-918 AND VAL-993.
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).
[30]
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).
[31]
VARIANTS EA2 PHE-389; MET-501; THR-798; ARG-897; CYS-1679 AND
ARG-1869.
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).
[32]
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).
[33]
VARIANT FHM1 PHE-1502 DEL, CHARACTERIZATION OF VARIANT FHM1 PHE-1502
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).
[34]
VARIANT FHM1 PHE-1502 DEL, CHARACTERIZATION OF VARIANT FHM1 PHE-1502
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).
[35]
INVOLVEMENT IN EIEE42, AND VARIANTS EIEE42 GLN-101; THR-713 AND
SER-1508.
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).
[36]
VARIANT EIEE42 ARG-1436.
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).
-!- 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 blocked by the funnel toxin (Ftx) and by the omega-agatoxin-
IVA (omega-Aga-IVA). They are however insensitive to
dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
{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.
-!- 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=7;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=1A-1, BI-1-GGCAG;
IsoId=O00555-1; Sequence=Displayed;
Name=2; Synonyms=1A-2,BI-1;
IsoId=O00555-2; Sequence=VSP_000875;
Name=3; Synonyms=BI-1(V1);
IsoId=O00555-3; Sequence=VSP_000871, VSP_000875;
Name=4; Synonyms=BI-1(V1)-GGCAG;
IsoId=O00555-4; Sequence=VSP_000871;
Name=5; Synonyms=BI-1(V2);
IsoId=O00555-5; Sequence=VSP_000872, VSP_000875;
Name=6; Synonyms=BI-1(V2)-GGCAG;
IsoId=O00555-6; Sequence=VSP_000872;
Name=8;
IsoId=O00555-8; Sequence=VSP_046165, VSP_046166;
-!- 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: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: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: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=1955-1975.
PDBsum; 3BXK; -.
ProteinModelPortal; O00555; -.
SMR; O00555; -.
BioGrid; 107227; 100.
CORUM; O00555; -.
IntAct; O00555; 92.
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; -.
DNASU; 773; -.
Ensembl; ENST00000360228; ENSP00000353362; ENSG00000141837. [O00555-8]
Ensembl; ENST00000635895; ENSP00000490323; ENSG00000141837. [O00555-2]
Ensembl; ENST00000637276; ENSP00000489777; ENSG00000141837. [O00555-5]
Ensembl; ENST00000638009; ENSP00000489913; ENSG00000141837. [O00555-3]
GeneID; 773; -.
KEGG; hsa:773; -.
UCSC; uc002mwy.5; human. [O00555-1]
CTD; 773; -.
DisGeNET; 773; -.
EuPathDB; HostDB:ENSG00000141837.18; -.
GeneCards; CACNA1A; -.
GeneReviews; CACNA1A; -.
HGNC; HGNC:1388; CACNA1A.
HPA; HPA064258; -.
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; -.
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:1904645; P:response to amyloid-beta; IDA:ARUK-UCL.
InterPro; IPR005448; CACNA1A.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR002077; VDCCAlpha1.
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 2505 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 361 487 Cytoplasmic. {ECO:0000255}.
TRANSMEM 488 506 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 507 521 Extracellular. {ECO:0000255}.
TRANSMEM 522 541 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 542 549 Cytoplasmic. {ECO:0000255}.
TRANSMEM 550 568 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 569 578 Extracellular. {ECO:0000255}.
TRANSMEM 579 597 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 598 616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 617 636 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 637 689 Extracellular. {ECO:0000255}.
TRANSMEM 690 714 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 715 1242 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1243 1261 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1262 1277 Extracellular. {ECO:0000255}.
TRANSMEM 1278 1297 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1298 1309 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1310 1328 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1329 1339 Extracellular. {ECO:0000255}.
TRANSMEM 1340 1358 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1359 1377 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1378 1397 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1398 1484 Extracellular. {ECO:0000255}.
TRANSMEM 1485 1509 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1510 1564 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1565 1593 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1594 1598 Extracellular. {ECO:0000255}.
TRANSMEM 1599 1618 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1619 1626 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1627 1645 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1646 1652 Extracellular. {ECO:0000255}.
TRANSMEM 1653 1671 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1672 1690 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1691 1710 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1711 1782 Extracellular. {ECO:0000255}.
TRANSMEM 1783 1807 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1808 2505 Cytoplasmic. {ECO:0000255}.
REPEAT 85 363 I.
REPEAT 473 717 II.
REPEAT 1231 1514 III.
REPEAT 1551 1814 IV.
CA_BIND 1840 1851 {ECO:0000250}.
REGION 383 400 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 13 18 Poly-Gly.
COMPBIAS 727 732 Poly-Glu.
COMPBIAS 1002 1007 Poly-Arg.
COMPBIAS 1204 1207 Poly-Glu.
COMPBIAS 2211 2220 Poly-His.
COMPBIAS 2221 2224 Poly-Pro.
COMPBIAS 2314 2324 Poly-Gln.
SITE 318 318 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 668 668 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1460 1460 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1649 1649 Binds to omega-Aga-IVA. {ECO:0000250}.
SITE 1756 1756 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 409 409 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1085 1085 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1094 1094 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1822 1822 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1984 1984 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2047 2047 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2065 2065 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2077 2077 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2079 2079 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2120 2120 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2140 2140 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 419 419 Missing (in isoform 8).
{ECO:0000303|PubMed:10753886}.
/FTId=VSP_046165.
VAR_SEQ 1844 1875 WGRMPYLDMYQMLRHMSPPLGLGKKCPARVAY -> CGRIH
YKDMYSLLRVISPPLGLGKKCPHRVAC (in isoform 3
and isoform 4).
{ECO:0000303|PubMed:8898206,
ECO:0000303|PubMed:8988170}.
/FTId=VSP_000871.
VAR_SEQ 2103 2114 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:8988170}.
/FTId=VSP_000872.
VAR_SEQ 2262 2505 Missing (in isoform 2, isoform 3 and
isoform 5). {ECO:0000303|PubMed:10049321,
ECO:0000303|PubMed:8898206,
ECO:0000303|PubMed:8988170}.
/FTId=VSP_000875.
VAR_SEQ 2314 2314 Q -> QQQ (in isoform 8).
{ECO:0000303|PubMed:10753886}.
/FTId=VSP_046166.
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 454 454 A -> T (in dbSNP:rs41276886).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_063686.
VARIANT 501 501 T -> M (in EA2; dbSNP:rs121908240).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063687.
VARIANT 583 583 R -> Q (in FHM1; dbSNP:rs121908217).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043826.
VARIANT 638 638 G -> D (in EA2; reduces P/Q current
densities; dbSNP:rs121908246).
{ECO:0000269|PubMed:19232643}.
/FTId=VAR_063688.
VARIANT 666 666 T -> M (in FHM1 and EA2;
dbSNP:rs121908212).
{ECO:0000269|PubMed:11439943,
ECO:0000269|PubMed:14718690,
ECO:0000269|PubMed:8898206}.
/FTId=VAR_001492.
VARIANT 713 713 A -> T (in EIEE42).
{ECO:0000269|PubMed:27476654}.
/FTId=VAR_077072.
VARIANT 714 714 V -> A (in FHM1; dbSNP:rs121908213).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_001493.
VARIANT 715 715 D -> E (in FHM1; dbSNP:rs121908218).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043827.
VARIANT 732 732 E -> A (in dbSNP:rs16019).
/FTId=VAR_059221.
VARIANT 798 798 M -> T (in EA2; dbSNP:rs121908241).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063689.
VARIANT 897 897 P -> R (in EA2; dbSNP:rs121908242).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063690.
VARIANT 914 914 P -> S (in dbSNP:rs16020).
/FTId=VAR_014458.
VARIANT 918 918 E -> D (in dbSNP:rs16022).
{ECO:0000269|PubMed:16866717,
ECO:0000269|PubMed:19429006}.
/FTId=VAR_014459.
VARIANT 993 993 E -> V (in dbSNP:rs16023).
{ECO:0000269|PubMed:10408532,
ECO:0000269|PubMed:16866717,
ECO:0000269|PubMed:19429006}.
/FTId=VAR_043828.
VARIANT 1015 1015 E -> K (in dbSNP:rs16024).
/FTId=VAR_014461.
VARIANT 1105 1105 G -> S (in dbSNP:rs16027).
{ECO:0000269|PubMed:10753886,
ECO:0000269|PubMed:16866717}.
/FTId=VAR_014462.
VARIANT 1173 1173 P -> L (in dbSNP:rs16028).
/FTId=VAR_059222.
VARIANT 1335 1335 K -> E (in FHM1; dbSNP:rs121908223).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043829.
VARIANT 1346 1346 R -> Q (in FHM1; with progressive
cerebellar ataxia; dbSNP:rs121908230).
{ECO:0000269|PubMed:15032980,
ECO:0000269|PubMed:18400034}.
/FTId=VAR_043830.
VARIANT 1384 1384 Y -> C (in FHM1; dbSNP:rs121908219).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043831.
VARIANT 1403 1403 F -> C (in EA2; loss of function;
dbSNP:rs121908227).
{ECO:0000269|PubMed:11723274}.
/FTId=VAR_043832.
VARIANT 1436 1436 W -> R (in EIEE42).
{ECO:0000269|PubMed:27250579}.
/FTId=VAR_077073.
VARIANT 1456 1456 V -> L (in FHM1; dbSNP:rs121908237).
{ECO:0000269|PubMed:10408532}.
/FTId=VAR_043833.
VARIANT 1482 1482 G -> R (in EA2; dbSNP:rs121908232).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043834.
VARIANT 1490 1490 F -> S (in EA2; dbSNP:rs121908233).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043835.
VARIANT 1493 1493 V -> I (in EA2; dbSNP:rs121908234).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043836.
VARIANT 1502 1502 Missing (in FHM1; increased high voltage-
gated calcium channel activity).
{ECO:0000269|PubMed:24836863,
ECO:0000269|PubMed:26716990}.
/FTId=VAR_077074.
VARIANT 1508 1508 A -> S (in EIEE42).
{ECO:0000269|PubMed:27476654}.
/FTId=VAR_077075.
VARIANT 1661 1661 R -> H (in EA2; dbSNP:rs121908216).
{ECO:0000269|PubMed:10987655}.
/FTId=VAR_043837.
VARIANT 1664 1664 R -> Q (in SCA6; dbSNP:rs121908247).
{ECO:0000269|PubMed:16325861}.
/FTId=VAR_063691.
VARIANT 1667 1667 R -> W (in FHM1; dbSNP:rs121908220).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043838.
VARIANT 1679 1679 R -> C (in EA2; dbSNP:rs121908243).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063692.
VARIANT 1683 1683 W -> R (in FHM1; dbSNP:rs121908221).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_043839.
VARIANT 1695 1695 V -> I (in FHM1; dbSNP:rs121908224).
{ECO:0000269|PubMed:11439943}.
/FTId=VAR_063706.
VARIANT 1736 1736 H -> L (in EA2; changed high voltage-
gated calcium channel activity;
dbSNP:rs121908229).
{ECO:0000269|PubMed:15293273}.
/FTId=VAR_043840.
VARIANT 1756 1756 E -> K (in EA2; dbSNP:rs121908226).
{ECO:0000269|PubMed:11176968}.
/FTId=VAR_043841.
VARIANT 1810 1810 I -> L (in FHM1; dbSNP:rs121908214).
{ECO:0000269|PubMed:8898206}.
/FTId=VAR_001494.
VARIANT 1869 1869 C -> R (in EA2; dbSNP:rs121908244).
{ECO:0000269|PubMed:20129625}.
/FTId=VAR_063693.
VARIANT 2135 2135 R -> C (in EA2; dbSNP:rs121908235).
{ECO:0000269|PubMed:15173248}.
/FTId=VAR_043842.
VARIANT 2394 2394 P -> S (in dbSNP:rs16056).
/FTId=VAR_014463.
CONFLICT 725 725 K -> KVEA (in Ref. 1; AAB61613/AAB61612).
{ECO:0000305}.
CONFLICT 896 896 G -> D (in Ref. 2; CAA68172 and 4;
BAA94766). {ECO:0000305}.
CONFLICT 953 953 D -> N (in Ref. 4; BAA94766).
{ECO:0000305}.
CONFLICT 964 964 R -> S (in Ref. 4; BAA94766).
{ECO:0000305}.
CONFLICT 1207 1207 E -> EE (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1313 1315 WNI -> ILP (in Ref. 3; AAB49674/AAB49675/
AAB49676/AAB49677/AAB49678).
{ECO:0000305}.
CONFLICT 1459 1459 G -> A (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1604 1604 V -> A (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1617 1617 V -> A (in Ref. 2; CAA68172).
{ECO:0000305}.
CONFLICT 1651 1651 G -> GNP (in Ref. 1; AAB61613/AAB61612).
{ECO:0000305}.
CONFLICT 1693 1693 P -> A (in Ref. 6; AAB33068).
{ECO:0000305}.
CONFLICT 2038 2038 E -> G (in Ref. 8; U06702).
{ECO:0000305}.
CONFLICT 2314 2314 Q -> QQ (in Ref. 3; AAB49676).
{ECO:0000305}.
HELIX 1956 1970 {ECO:0000244|PDB:3BXK}.
SEQUENCE 2505 AA; 282365 MW; 2F2F378ACE02FD56 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 GEQRHPFDGA
LRRTTIKKSK TDLLNPEEAE DQLADIASVG SPFARASIKS AKLENSTFFH KKERRMRFYI
RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG
LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT
VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA
QELTKDEQEE EEAANQKLAL QKAKEVAEVS PLSAANMSIA VKEQQKNQKP AKSVWEQRTS
EMRKQNLLAS REALYNEMDP DERWKAAYTR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR
AAEPTVDQRL GQQRAEDFLR KQARYHDRAR DPSGSAGLDA RRPWAGSQEA ELSREGPYGR
ESDHHAREGS LEQPGFWEGE AERGKAGDPH RRHVHRQGGS RESRSGSPRT GADGEHRRHR
AHRRPGEEGP EDKAERRARH REGSRPARGG EGEGEGPDGG ERRRRHRHGA PATYEGDARR
EDKERRHRRR KENQGSGVPV SGPNLSTTRP IQQDLGRQDP PLAEDIDNMK NNKLATAESA
APHGSLGHAG LPQSPAKMGN STDPGPMLAI PAMATNPQNA ASRRTPNNPG NPSNPGPPKT
PENSLIVTNP SGTQTNSAKT ARKPDHTTVD IPPACPPPLN HTVVQVNKNA NPDPLPKKEE
EKKEEEEDDR GEDGPKPMPP YSSMFILSTT NPLRRLCHYI LNLRYFEMCI LMVIAMSSIA
LAAEDPVQPN APRNNVLRYF DYVFTGVFTF EMVIKMIDLG LVLHQGAYFR DLWNILDFIV
VSGALVAFAF TGNSKGKDIN TIKSLRVLRV LRPLKTIKRL PKLKAVFDCV VNSLKNVFNI
LIVYMLFMFI FAVVAVQLFK GKFFHCTDES KEFEKDCRGK YLLYEKNEVK ARDREWKKYE
FHYDNVLWAL LTLFTVSTGE GWPQVLKHSV DATFENQGPS PGYRMEMSIF YVVYFVVFPF
FFVNIFVALI IITFQEQGDK MMEEYSLEKN ERACIDFAIS AKPLTRHMPQ NKQSFQYRMW
QFVVSPPFEY TIMAMIALNT IVLMMKFYGA SVAYENALRV FNIVFTSLFS LECVLKVMAF
GILNYFRDAW NIFDFVTVLG SITDILVTEF GNNFINLSFL RLFRAARLIK LLRQGYTIRI
LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG MQVFGNIGID VEDEDSDEDE FQITEHNNFR
TFFQALMLLF RSATGEAWHN IMLSCLSGKP CDKNSGILTR ECGNEFAYFY FVSFIFLCSF
LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EYVRVWAEYD PAAWGRMPYL DMYQMLRHMS
PPLGLGKKCP ARVAYKRLLR MDLPVADDNT VHFNSTLMAL IRTALDIKIA KGGADKQQMD
AELRKEMMAI WPNLSQKTLD LLVTPHKSTD LTVGKIYAAM MIMEYYRQSK AKKLQAMREE
QDRTPLMFQR MEPPSPTQEG GPGQNALPST QLDPGGALMA HESGLKESPS WVTQRAQEMF
QKTGTWSPEQ GPPTDMPNSQ PNSQSVEMRE MGRDGYSDSE HYLPMEGQGR AASMPRLPAE
NQRRRGRPRG NNLSTISDTS PMKRSASVLG PKARRLDDYS LERVPPEENQ RHHQRRRDRS
HRASERSLGR YTDVDTGLGT DLSMTTQSGD LPSKERDQER GRPKDRKHRQ HHHHHHHHHH
PPPPDKDRYA QERPDHGRAR ARDQRWSRSP SEGREHMAHR QGSSSVSGSP APSTSGTSTP
RRGRRQLPQT PSTPRPHVSY SPVIRKAGGS GPPQQQQQQQ QQQQAVARPG RAATSGPRRY
PGPTAEPLAG DRPPTGGHSS GRSPRMERRV PGPARSESPR ACRHGGARWP ASGPHVSEGP
PGPRHHGYYR GSDYDEADGP GSGGGEEAMA GAYDAPPPVR HASSGATGRS PRTPRASGPA
CASPSRHGRR LPNGYYPAHG LARPRGPGSR KGLHEPYSES DDDWC


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