Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Voltage-gated calcium channel subunit alpha Cav1.2)

 CAC1C_HUMAN             Reviewed;        2221 AA.
Q13936; B2RUT3; E9PDJ0; Q13917; Q13918; Q13919; Q13920; Q13921;
Q13922; Q13923; Q13924; Q13925; Q13926; Q13927; Q13928; Q13929;
Q13930; Q13932; Q13933; Q14743; Q14744; Q15877; Q4VMI7; Q4VMI8;
Q4VMI9; Q6PKM7; Q8N6C0; Q99025; Q99241; Q99875;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
28-MAR-2018, entry version 207.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=CACNA1C; Synonyms=CACH2, CACN2, CACNL1A1, CCHL1A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
AND VARIANTS VAL-1869 AND ARG-1893.
TISSUE=Fetal fibroblast;
PubMed=1316612; DOI=10.1073/pnas.89.10.4628;
Soldatov N.M.;
"Molecular diversity of L-type Ca2+ channel transcripts in human
fibroblasts.";
Proc. Natl. Acad. Sci. U.S.A. 89:4628-4632(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 18 AND 28), NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 1822-1863, FUNCTION, TISSUE SPECIFICITY, AND VARIANT
ARG-84.
TISSUE=Heart;
PubMed=8392192; DOI=10.1073/pnas.90.13.6228;
Schultz D., Mikala G., Yatani A., Engle D.B., Iles D.E., Segers B.,
Sinke R.J., Weghuis D.O., Kloeckner U., Wakamori M., Wang J.-J.,
Melvin D., Varadi G., Schwartz A.;
"Cloning, chromosomal localization, and functional expression of the
alpha-1 subunit of the L-type voltage-dependent calcium channel from
normal human heart.";
Proc. Natl. Acad. Sci. U.S.A. 90:6228-6232(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF
1112-1803 (ISOFORMS 24/27), AND NUCLEOTIDE SEQUENCE [MRNA] OF
1364-1972 (ISOFORMS 11/12/19/20/21/22/23/30/31/32).
TISSUE=Hippocampus, and Lung fibroblast;
PubMed=7959794; DOI=10.1006/geno.1994.1347;
Soldatov N.M.;
"Genomic structure of human L-type Ca2+ channel.";
Genomics 22:77-87(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12; 19 AND 20), ALTERNATIVE
SPLICING, FUNCTION, AND MUTAGENESIS OF GLY-954 AND TYR-958.
TISSUE=Fibroblast;
PubMed=7737988; DOI=10.1074/jbc.270.18.10540;
Soldatov N.M., Bouron A., Reuter H.;
"Different voltage-dependent inhibition by dihydropyridines of human
Ca2+ channel splice variants.";
J. Biol. Chem. 270:10540-10543(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 16 AND 17),
ALTERNATIVE SPLICING, AND VARIANTS ARG-84; VAL-1869 AND ARG-1893.
TISSUE=Heart;
PubMed=9087614;
Kloeckner U., Mikala G., Eisfeld J., Iles D.E., Strobeck M.,
Mershon J.L., Schwartz A., Varadi G.;
"Properties of three COOH-terminal splice variants of a human cardiac
L-type Ca2+-channel alpha1-subunit.";
Am. J. Physiol. 272:H1372-H1381(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 26 AND 27), ALTERNATIVE SPLICING
(ISOFORMS 9 AND 10), AND FUNCTION.
TISSUE=Hippocampus;
PubMed=9013606; DOI=10.1074/jbc.272.6.3560;
Soldatov N.M., Zuelke R.D., Bouron A., Reuter H.;
"Molecular structures involved in L-type calcium channel inactivation.
Role of the carboxyl-terminal region encoded by exons 40-42 in alpha1C
subunit in the kinetics and Ca2+ dependence of inactivation.";
J. Biol. Chem. 272:3560-3566(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 21; 22 AND 23), AND FUNCTION.
PubMed=9607315; DOI=10.1016/S0014-5793(98)00425-6;
Zuehlke R.D., Bouron A., Soldatov N.M., Reuter H.;
"Ca2+ channel sensitivity towards the blocker isradipine is affected
by alternative splicing of the human alpha1C subunit gene.";
FEBS Lett. 427:220-224(1998).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Intestinal smooth muscle;
PubMed=12176756; DOI=10.1152/ajpcell.00140.2002;
Lyford G.L., Strege P.R., Shepard A., Ou Y., Ermilov L., Miller S.M.,
Gibbons S.J., Rae J.L., Szurszewski J.H., Farrugia G.;
"Alpha(1C) (Ca(V)1.2) L-type calcium channel mediates mechanosensitive
calcium regulation.";
Am. J. Physiol. 283:C1001-C1008(2002).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 13; 14; 15; 24 AND 25), FUNCTION,
AND TISSUE SPECIFICITY.
PubMed=17071743; DOI=10.1073/pnas.0606539103;
Tiwari S., Zhang Y., Heller J., Abernethy D.R., Soldatov N.M.;
"Atherosclerosis-related molecular alteration of the human CaV1.2
calcium channel alpha1C subunit.";
Proc. Natl. Acad. Sci. U.S.A. 103:17024-17029(2006).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 11; 28; 29; 30; 31; 32 AND 33),
ALTERNATIVE SPLICING, AND VARIANTS ARG-84; VAL-1869 AND ARG-1893.
Soldatov N.;
"Functional expression of splice variants of human l-type calcium
channel (isoform 1 gene).";
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 35).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-180 (ISOFORM 34).
PubMed=11741969; DOI=10.1074/jbc.C100642200;
Blumenstein Y., Kanevsky N., Sahar G., Barzilai R., Ivanina T.,
Dascal N.;
"A novel long N-terminal isoform of human L-type Ca2+ channel is up-
regulated by protein kinase C.";
J. Biol. Chem. 277:3419-3423(2002).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1503 (ISOFORMS 6/12/20/23/24), AND
NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1503 (ISOFORMS
7/13/16/17/18/21/22).
TISSUE=Heart;
PubMed=2173707;
Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.;
"Molecular diversity of L-type calcium channels. Evidence for
alternative splicing of the transcripts of three non-allelic genes.";
J. Biol. Chem. 265:20430-20436(1990).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1140-1206.
TISSUE=Heart;
PubMed=1653763; DOI=10.1016/0888-7543(91)90471-P;
Powers P.A., Gregg R.G., Lalley P.A., Liao M., Hogan K.;
"Assignment of the human gene for the alpha 1 subunit of the cardiac
DHP-sensitive Ca2+ channel (CCHL1A1) to chromosome 12p12-pter.";
Genomics 10:835-839(1991).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1196-1421.
TISSUE=Brain;
PubMed=1335957; DOI=10.1016/S0888-7543(05)80135-1;
Sun W., McPherson J.D., Hoang D.Q., Wasmuth J.J., Evans G.A.,
Montal M.;
"Mapping of a human brain voltage-gated calcium channel to human
chromosome 12p13-pter.";
Genomics 14:1092-1094(1992).
[17]
MUTAGENESIS, CALCIUM-BINDING, AND SITE.
PubMed=8099908;
Tang S., Mikala G., Bahinski A., Yatani A., Varadi G., Schwartz A.;
"Molecular localization of ion selectivity sites within the pore of a
human L-type cardiac calcium channel.";
J. Biol. Chem. 268:13026-13029(1993).
[18]
INTERACTION WITH CACNA2D4.
PubMed=12181424; DOI=10.1124/mol.62.3.485;
Qin N., Yagel S., Momplaisir M.-L., Codd E.E., D'Andrea M.R.;
"Molecular cloning and characterization of the human voltage-gated
calcium channel alpha(2)delta-4 subunit.";
Mol. Pharmacol. 62:485-496(2002).
[19]
INTERACTION WITH CABP1.
PubMed=15140941; DOI=10.1523/JNEUROSCI.5523-03.2004;
Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F.,
Lee A.;
"Ca2+-binding protein-1 facilitates and forms a postsynaptic complex
with Cav1.2 (L-type) Ca2+ channels.";
J. Neurosci. 24:4698-4708(2004).
[20]
INTERACTION WITH CABP1.
PubMed=15980432; DOI=10.1074/jbc.M504167200;
Zhou H., Yu K., McCoy K.L., Lee A.;
"Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels
by calmodulin and Ca2+-binding protein-1.";
J. Biol. Chem. 280:29612-29619(2005).
[21]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH STAC2
AND STAC3.
PubMed=29078335; DOI=10.1073/pnas.1708852114;
Wong King Yuen S.M., Campiglio M., Tung C.C., Flucher B.E.,
Van Petegem F.;
"Structural insights into binding of STAC proteins to voltage-gated
calcium channels.";
Proc. Natl. Acad. Sci. U.S.A. 114:E9520-E9528(2017).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 428-445 IN COMPLEX WITH
CACNB2.
PubMed=15141227; DOI=10.1038/nature02588;
Van Petegem F., Clark K.A., Chatelain F.C., Minor D.L. Jr.;
"Structure of a complex between a voltage-gated calcium channel beta-
subunit and an alpha-subunit domain.";
Nature 429:671-675(2004).
[23]
VARIANT TS ARG-406, AND CHARACTERIZATION OF VARIANT TS ARG-406.
PubMed=15454078; DOI=10.1016/j.cell.2004.09.011;
Splawski I., Timothy K.W., Sharpe L.M., Decher N., Kumar P.,
Bloise R., Napolitano C., Schwartz P.J., Joseph R.M., Condouris K.,
Tager-Flusberg H., Priori S.G., Sanguinetti M.C., Keating M.T.;
"Ca(V)1.2 calcium channel dysfunction causes a multisystem disorder
including arrhythmia and autism.";
Cell 119:19-31(2004).
[24]
VARIANT TS SER-402.
PubMed=15863612; DOI=10.1073/pnas.0502506102;
Splawski I., Timothy K.W., Decher N., Kumar P., Sachse F.B.,
Beggs A.H., Sanguinetti M.C., Keating M.T.;
"Severe arrhythmia disorder caused by cardiac L-type calcium channel
mutations.";
Proc. Natl. Acad. Sci. U.S.A. 102:8089-8096(2005).
[25]
VARIANTS BRGDA3 VAL-39 AND ARG-490, AND CHARACTERIZATION OF VARIANTS
BRGDA3 VAL-39 AND ARG-490.
PubMed=17224476; DOI=10.1161/CIRCULATIONAHA.106.668392;
Antzelevitch C., Pollevick G.D., Cordeiro J.M., Casis O.,
Sanguinetti M.C., Aizawa Y., Guerchicoff A., Pfeiffer R., Oliva A.,
Wollnik B., Gelber P., Bonaros E.P. Jr., Burashnikov E., Wu Y.,
Sargent J.D., Schickel S., Oberheiden R., Bhatia A., Hsu L.F.,
Haissaguerre M., Schimpf R., Borggrefe M., Wolpert C.;
"Loss-of-function mutations in the cardiac calcium channel underlie a
new clinical entity characterized by ST-segment elevation, short QT
intervals, and sudden cardiac death.";
Circulation 115:442-449(2007).
[26]
VARIANT ARG-878.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
[27]
VARIANTS TS SER-381; ILE-456; ASP-582; HIS-858 AND CYS-1831, AND
CHARACTERIZATION OF VARIANTS TS SER-381; ILE-456; ASP-582; HIS-858 AND
CYS-1831.
PubMed=24728418; DOI=10.1093/europace/euu063;
Fukuyama M., Wang Q., Kato K., Ohno S., Ding W.G., Toyoda F., Itoh H.,
Kimura H., Makiyama T., Ito M., Matsuura H., Horie M.;
"Long QT syndrome type 8: novel CACNA1C mutations causing QT
prolongation and variant phenotypes.";
Europace 16:1828-1837(2014).
[28]
VARIANTS TS CYS-518 AND HIS-518, AND CHARACTERIZATION OF VARIANTS TS
CYS-518 AND HIS-518.
PubMed=26253506; DOI=10.1161/CIRCEP.115.002745;
Boczek N.J., Ye D., Jin F., Tester D.J., Huseby A., Bos J.M.,
Johnson A.J., Kanter R., Ackerman M.J.;
"Identification and functional characterization of a novel CACNA1C-
mediated cardiac disorder characterized by prolonged QT intervals with
hypertrophic cardiomyopathy, congenital heart defects, and sudden
cardiac death.";
Circ. Arrhythm. Electrophysiol. 8:1122-1132(2015).
[29]
VARIANT TS THR-1186, AND CHARACTERIZATION OF VARIANT TS THR-1186.
PubMed=25260352; DOI=10.1016/j.hrthm.2014.09.051;
Boczek N.J., Miller E.M., Ye D., Nesterenko V.V., Tester D.J.,
Antzelevitch C., Czosek R.J., Ackerman M.J., Ware S.M.;
"Novel Timothy syndrome mutation leading to increase in CACNA1C window
current.";
Heart Rhythm 12:211-219(2015).
[30]
VARIANTS TS THR-28; GLY-860; THR-1186; VAL-1186; MET-1523; LYS-1544;
ILE-1800 MET-1953 AND ILE-2097, CHARACTERIZATION OF VARIANTS TS
THR-28; GLY-860; THR-1186; VAL-1186; MET-1523 AND LYS-1544, AND
VARIANTS ARG-37; THR-304; LYS-477; SER-817; THR-1365; ILE-1755;
GLY-1765; ASN-1787; MET-1835; ALA-1843; LYS-1948; CYS-1972; GLN-2056;
ASN-2081; GLY-2122 AND SER-2174.
PubMed=25633834; DOI=10.1016/j.yjmcc.2015.01.002;
Wemhoener K., Friedrich C., Stallmeyer B., Coffey A.J., Grace A.,
Zumhagen S., Seebohm G., Ortiz-Bonnin B., Rinne S., Sachse F.B.,
Schulze-Bahr E., Decher N.;
"Gain-of-function mutations in the calcium channel CACNA1C (Cav1.2)
cause non-syndromic long-QT but not Timothy syndrome.";
J. Mol. Cell. Cardiol. 80:186-195(2015).
[31]
VARIANT HIS-1159.
PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
Sestan N., Walsh C.A.;
"Targeted DNA Sequencing from Autism Spectrum Disorder Brains
Implicates Multiple Genetic Mechanisms.";
Neuron 88:910-917(2015).
[32]
VARIANTS GLU-850 DEL AND SER-2091, AND CHARACTERIZATION OF VARIANTS
GLU-850 DEL AND SER-2091.
PubMed=27218670; DOI=10.1111/chd.12371;
Sutphin B.S., Boczek N.J., Barajas-Martinez H., Hu D., Ye D.,
Tester D.J., Antzelevitch C., Ackerman M.J.;
"Molecular and functional characterization of rare CACNA1C variants in
sudden unexplained death in the young.";
Congenit. Heart Dis. 11:683-692(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 (PubMed:29078335). The
isoform alpha-1C gives rise to L-type calcium currents. Long-
lasting (L-type) calcium channels belong to the 'high-voltage
activated' (HVA) group. They are blocked by dihydropyridines
(DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-
IIIA (omega-Aga-IIIA). They are however insensitive to omega-
conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-
IVA). Calcium channels containing the alpha-1C subunit play an
important role in excitation-contraction coupling in the heart.
The various isoforms display marked differences in the sensitivity
to DHP compounds. Binding of calmodulin or CABP1 at the same
regulatory sites results in opposite effects on the channel
function. STAC3 strongly decreases the rate of channel
inactivation (PubMed:29078335). {ECO:0000269|PubMed:12176756,
ECO:0000269|PubMed:17071743, ECO:0000269|PubMed:29078335,
ECO:0000269|PubMed:7737988, ECO:0000269|PubMed:8392192,
ECO:0000269|PubMed:9013606, ECO:0000269|PubMed:9607315}.
-!- 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 (PubMed:29078335). The auxiliary subunits beta
and alpha-2/delta linked by a disulfide bridge regulate the
channel activity. Interacts with CACNA2D4. Interacts (via the N-
terminus and the C-terminal C and IQ motifs) with CABP1. The
binding via the C motif is calcium independent whereas the binding
via IQ requires the presence of calcium and is mutually exclusive
with calmodulin binding. The binding to the cytoplasmic N-terminal
domain is calcium independent but is essential for the channel
modulation. Interacts (via C-terminal CDB motif) with CABP5; in a
calcium-dependent manner (By similarity). Interacts with CIB1; the
interaction increases upon cardiomyocytes hypertrophy (By
similarity). Interacts with STAC2 and STAC3 (PubMed:29078335).
{ECO:0000250, ECO:0000269|PubMed:12181424,
ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15141227,
ECO:0000269|PubMed:15980432, ECO:0000269|PubMed:29078335}.
-!- INTERACTION:
Q9NZU7:CABP1; NbExp=4; IntAct=EBI-1038838, EBI-907894;
Q9NZU7-2:CABP1; NbExp=2; IntAct=EBI-15896749, EBI-15896740;
Q02641-1:CACNB1; NbExp=2; IntAct=EBI-1038838, EBI-15707950;
Q08289-1:CACNB2; NbExp=4; IntAct=EBI-1038838, EBI-15707999;
P54284:CACNB3; NbExp=2; IntAct=EBI-1038838, EBI-1184651;
P62158:CALM3; NbExp=21; IntAct=EBI-1038838, EBI-397435;
P62161:Calm3 (xeno); NbExp=2; IntAct=EBI-1038838, EBI-397530;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P15381};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Cell
membrane {ECO:0000269|PubMed:29078335}. Note=The interaction
between RRAD and CACNB2 regulates its trafficking to the cell
membrane. {ECO:0000250|UniProtKB:P15381}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=37;
Comment=Additional isoforms seem to exist. Exons 8A, 21, 22, 31,
32, 33, 40B, 43A, 41A and 45 are alternatively spliced in a
variety of combinations. Experimental confirmation may be
lacking for some isoforms.;
Name=1; Synonyms=HFCC, Fibroblast;
IsoId=Q13936-1; Sequence=Displayed;
Name=2;
IsoId=Q13936-2; Sequence=VSP_000894;
Name=3;
IsoId=Q13936-3; Sequence=VSP_000886;
Note=Contains exon 8a.;
Name=4;
IsoId=Q13936-4; Sequence=VSP_000887;
Note=Lacks exon 21.;
Name=5;
IsoId=Q13936-5; Sequence=VSP_000888;
Note=Lacks exon 22.;
Name=6;
IsoId=Q13936-6; Sequence=VSP_000889;
Note=Lacks exon 31.;
Name=7;
IsoId=Q13936-7; Sequence=VSP_000890;
Note=Lacks exon 32.;
Name=8;
IsoId=Q13936-8; Sequence=VSP_000891;
Note=Lacks exon 33.;
Name=9;
IsoId=Q13936-9; Sequence=VSP_000892;
Note=Contains exon 40B and 43A.;
Name=10;
IsoId=Q13936-10; Sequence=VSP_000893;
Note=Contains exon 41A.;
Name=11; Synonyms=Alpha-1C.90;
IsoId=Q13936-11; Sequence=VSP_000895;
Note=Lacks exon 45.;
Name=12; Synonyms=Alpha-1C.70;
IsoId=Q13936-12; Sequence=VSP_000888, VSP_000889, VSP_000895;
Name=13; Synonyms=Alpha-1C.127;
IsoId=Q13936-13; Sequence=VSP_000888, VSP_000890, VSP_000893,
VSP_000895;
Name=14; Synonyms=Alpha-1C.126;
IsoId=Q13936-14; Sequence=VSP_000888, VSP_000889, VSP_022504,
VSP_000893, VSP_000895;
Name=15; Synonyms=Alpha-1C.125;
IsoId=Q13936-15; Sequence=VSP_000888, VSP_000889, VSP_022503,
VSP_000893, VSP_000895;
Name=16;
IsoId=Q13936-16; Sequence=VSP_000885, VSP_000886, VSP_000888,
VSP_000890;
Name=17;
IsoId=Q13936-17; Sequence=VSP_000885, VSP_000886, VSP_000888,
VSP_000890, VSP_000895;
Name=18; Synonyms=HHT-1;
IsoId=Q13936-18; Sequence=VSP_000885, VSP_000886, VSP_000888,
VSP_000890, VSP_000894;
Name=19; Synonyms=Alpha-1C.76;
IsoId=Q13936-19; Sequence=VSP_000887, VSP_000889, VSP_000891,
VSP_000895;
Name=20; Synonyms=Alpha-1C.77;
IsoId=Q13936-20; Sequence=VSP_000887, VSP_000889, VSP_000895;
Note=Predominant isoform in atherosclerotic vascular smooth
muscle cells.;
Name=21; Synonyms=Alpha-1C.69;
IsoId=Q13936-21; Sequence=VSP_000887, VSP_000890, VSP_000895;
Name=22; Synonyms=Alpha-1C.78;
IsoId=Q13936-22; Sequence=VSP_000888, VSP_000890, VSP_000895;
Name=23; Synonyms=Alpha-1C.105;
IsoId=Q13936-23; Sequence=VSP_000886, VSP_000887, VSP_000889,
VSP_000895;
Name=24; Synonyms=Alpha-1C.71;
IsoId=Q13936-24; Sequence=VSP_000888, VSP_000889, VSP_000893,
VSP_000895;
Name=25; Synonyms=Alpha-1C.73;
IsoId=Q13936-25; Sequence=VSP_000888, VSP_000889, VSP_000891,
VSP_000893, VSP_000895;
Name=26; Synonyms=Alpha-1C.86;
IsoId=Q13936-26; Sequence=VSP_000887, VSP_000889, VSP_000892,
VSP_000895;
Note=Not inhibited by calcium. Ref.3 (CAA84348) sequence is in
conflict in position: 1573:A->T. {ECO:0000305};
Name=27; Synonyms=Alpha-1C.72;
IsoId=Q13936-27; Sequence=VSP_000887, VSP_000889, VSP_000893,
VSP_000895;
Name=28;
IsoId=Q13936-28; Sequence=VSP_000885, VSP_000886, VSP_000888,
VSP_000889, VSP_000891, VSP_000894;
Name=29; Synonyms=Alpha-1C.74;
IsoId=Q13936-29; Sequence=VSP_000887, VSP_000889, VSP_000891,
VSP_000893, VSP_000895;
Name=30; Synonyms=Alpha-1C.87;
IsoId=Q13936-30; Sequence=VSP_000889, VSP_000895;
Name=31; Synonyms=Alpha-1C.88;
IsoId=Q13936-31; Sequence=VSP_000888, VSP_000895;
Name=32; Synonyms=Alpha-1C.89;
IsoId=Q13936-32; Sequence=VSP_000887, VSP_000891, VSP_000895;
Name=33; Synonyms=Alpha-1C.85;
IsoId=Q13936-33; Sequence=VSP_000887, VSP_000889;
Name=34; Synonyms=Alpha-1C,long-NT;
IsoId=Q13936-34; Sequence=VSP_035146;
Note=Enhanced by PKC activator.;
Name=35;
IsoId=Q13936-35; Sequence=VSP_035877, VSP_000888, VSP_000890,
VSP_000895;
Name=36;
IsoId=Q13936-36; Sequence=VSP_000886, VSP_000888, VSP_000890;
Note=Gene prediction based on EST data.;
Name=37;
IsoId=Q13936-37; Sequence=VSP_000886, VSP_000888, VSP_000890,
VSP_000895;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, jejunum, ovary,
pancreatic beta-cells and vascular smooth muscle. Overall
expression is reduced in atherosclerotic vascular smooth muscle.
{ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:17071743,
ECO:0000269|PubMed:8392192}.
-!- 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.
-!- DOMAIN: Binding of intracellular calcium through the EF-hand motif
inhibits the opening of the channel.
{ECO:0000250|UniProtKB:P15381}.
-!- PTM: Phosphorylation by PKA activates the channel.
{ECO:0000250|UniProtKB:P15381}.
-!- DISEASE: Timothy syndrome (TS) [MIM:601005]: Disorder
characterized by multiorgan dysfunction including lethal
arrhythmias, webbing of fingers and toes, congenital heart
disease, immune deficiency, intermittent hypoglycemia, cognitive
abnormalities and autism. {ECO:0000269|PubMed:15454078,
ECO:0000269|PubMed:15863612, ECO:0000269|PubMed:24728418,
ECO:0000269|PubMed:25260352, ECO:0000269|PubMed:25633834,
ECO:0000269|PubMed:26253506}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Brugada syndrome 3 (BRGDA3) [MIM:611875]: A heart disease
characterized by the association of Brugada syndrome with
shortened QT intervals. Brugada syndrome is a tachyarrhythmia
characterized by right bundle branch block and ST segment
elevation on an electrocardiogram (ECG). It can cause the
ventricles to beat so fast that the blood is prevented from
circulating efficiently in the body. When this situation occurs,
the individual will faint and may die in a few minutes if the
heart is not reset. {ECO:0000269|PubMed:17224476}. 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. CACNA1C subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA02500.2; Type=Frameshift; Positions=1844; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M92269; AAA17030.1; -; Genomic_DNA.
EMBL; M92270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M92271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M92272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M92273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M92274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M92275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L04568; AAA02500.2; ALT_FRAME; Genomic_DNA.
EMBL; L04569; AAA02501.1; -; mRNA.
EMBL; L29529; AAA51899.1; -; mRNA.
EMBL; Z26256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z26294; CAA81218.1; -; mRNA.
EMBL; Z26295; CAA81219.1; -; mRNA.
EMBL; Z26308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z34809; CAA84340.1; -; mRNA.
EMBL; Z34810; CAA84341.1; -; mRNA.
EMBL; Z34811; CAA84342.1; -; mRNA.
EMBL; Z34812; CAA84343.1; -; mRNA.
EMBL; Z34813; CAA84344.1; -; mRNA.
EMBL; Z34814; CAA84345.1; -; mRNA.
EMBL; Z34815; CAA84346.1; -; mRNA.
EMBL; Z34816; CAA84347.1; -; mRNA.
EMBL; Z34817; CAA84348.1; -; mRNA.
EMBL; Z34818; CAA84349.1; -; mRNA.
EMBL; Z34819; CAA84350.1; -; mRNA.
EMBL; Z34820; CAA84351.1; -; mRNA.
EMBL; Z34821; CAA84352.1; -; mRNA.
EMBL; Z34822; CAA84353.1; -; mRNA.
EMBL; L29530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29534; AAA51900.1; -; mRNA.
EMBL; L29535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29536; AAA51901.1; -; mRNA.
EMBL; L29537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z74996; CAA99284.1; -; mRNA.
EMBL; AJ224873; CAA12174.1; -; mRNA.
EMBL; AF465484; AAM70049.1; -; mRNA.
EMBL; AY830711; AAX37354.1; -; mRNA.
EMBL; AY830712; AAX37355.1; -; mRNA.
EMBL; AY830713; AAX37356.1; -; mRNA.
EMBL; AC005293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC146846; AAI46847.1; -; mRNA.
EMBL; AY604867; AAT02226.1; -; mRNA.
EMBL; M57971; AAA62832.1; -; mRNA.
EMBL; M57972; AAB59461.1; -; mRNA.
EMBL; M61130; AAA58409.1; -; Genomic_DNA.
EMBL; M91370; AAA74590.1; -; Genomic_DNA.
CCDS; CCDS44787.1; -. [Q13936-23]
CCDS; CCDS44788.1; -. [Q13936-11]
CCDS; CCDS44789.1; -. [Q13936-30]
CCDS; CCDS44790.1; -. [Q13936-31]
CCDS; CCDS44791.1; -. [Q13936-22]
CCDS; CCDS44792.1; -. [Q13936-14]
CCDS; CCDS44793.1; -. [Q13936-24]
CCDS; CCDS44794.1; -. [Q13936-12]
CCDS; CCDS44795.1; -. [Q13936-25]
CCDS; CCDS44796.1; -. [Q13936-15]
CCDS; CCDS44797.1; -. [Q13936-32]
CCDS; CCDS44798.1; -. [Q13936-21]
CCDS; CCDS44799.1; -. [Q13936-27]
CCDS; CCDS44800.1; -. [Q13936-20]
CCDS; CCDS44801.1; -. [Q13936-29]
CCDS; CCDS53733.1; -. [Q13936-36]
CCDS; CCDS53734.1; -. [Q13936-37]
CCDS; CCDS53735.1; -. [Q13936-13]
CCDS; CCDS53736.1; -. [Q13936-33]
PIR; A23660; A23660.
PIR; A44363; A44363.
PIR; A45290; A45290.
PIR; B23660; B23660.
PIR; C23660; C23660.
PIR; I54168; I54168.
RefSeq; NP_000710.5; NM_000719.6. [Q13936-12]
RefSeq; NP_001123299.1; NM_001129827.1. [Q13936-11]
RefSeq; NP_001123301.1; NM_001129829.1. [Q13936-14]
RefSeq; NP_001123302.2; NM_001129830.2.
RefSeq; NP_001123303.1; NM_001129831.1. [Q13936-31]
RefSeq; NP_001123304.1; NM_001129832.1. [Q13936-30]
RefSeq; NP_001123305.1; NM_001129833.1. [Q13936-13]
RefSeq; NP_001123306.1; NM_001129834.1. [Q13936-24]
RefSeq; NP_001123307.1; NM_001129835.1. [Q13936-27]
RefSeq; NP_001123308.1; NM_001129836.1. [Q13936-32]
RefSeq; NP_001123309.1; NM_001129837.1. [Q13936-25]
RefSeq; NP_001123310.1; NM_001129838.1. [Q13936-29]
RefSeq; NP_001123311.1; NM_001129839.1. [Q13936-15]
RefSeq; NP_001123312.1; NM_001129840.1. [Q13936-23]
RefSeq; NP_001123313.1; NM_001129841.1. [Q13936-21]
RefSeq; NP_001123314.1; NM_001129842.1. [Q13936-22]
RefSeq; NP_001123315.1; NM_001129843.1. [Q13936-20]
RefSeq; NP_001123316.1; NM_001129844.1. [Q13936-35]
RefSeq; NP_001123318.1; NM_001129846.1. [Q13936-19]
RefSeq; NP_001161095.1; NM_001167623.1. [Q13936-37]
RefSeq; NP_001161096.2; NM_001167624.2.
RefSeq; NP_001161097.1; NM_001167625.1.
RefSeq; NP_955630.3; NM_199460.3.
UniGene; Hs.118262; -.
UniGene; Hs.690010; -.
PDB; 1T0J; X-ray; 2.00 A; C=428-445.
PDB; 2BE6; X-ray; 2.00 A; D/E/F=1659-1692.
PDB; 2F3Y; X-ray; 1.45 A; B=1665-1685.
PDB; 2F3Z; X-ray; 1.60 A; B=1665-1685.
PDB; 2LQC; NMR; -; B=47-68.
PDB; 3G43; X-ray; 2.10 A; E/F=1609-1682.
PDB; 3OXQ; X-ray; 2.55 A; E/F=1609-1685.
PDB; 5V2P; X-ray; 2.00 A; B=427-445.
PDB; 5V2Q; X-ray; 1.70 A; B=427-445.
PDBsum; 1T0J; -.
PDBsum; 2BE6; -.
PDBsum; 2F3Y; -.
PDBsum; 2F3Z; -.
PDBsum; 2LQC; -.
PDBsum; 3G43; -.
PDBsum; 3OXQ; -.
PDBsum; 5V2P; -.
PDBsum; 5V2Q; -.
ProteinModelPortal; Q13936; -.
SMR; Q13936; -.
BioGrid; 107229; 14.
DIP; DIP-29589N; -.
IntAct; Q13936; 9.
MINT; Q13936; -.
STRING; 9606.ENSP00000266376; -.
BindingDB; Q13936; -.
ChEMBL; CHEMBL1940; -.
DrugBank; DB00381; Amlodipine.
DrugBank; DB01373; Calcium.
DrugBank; DB00568; Cinnarizine.
DrugBank; DB04920; Clevidipine.
DrugBank; DB04855; Dronedarone.
DrugBank; DB06751; Drotaverine.
DrugBank; DB00898; Ethanol.
DrugBank; DB01023; Felodipine.
DrugBank; DB00308; Ibutilide.
DrugBank; DB00270; Isradipine.
DrugBank; DB00653; Magnesium Sulfate.
DrugBank; DB01388; Mibefradil.
DrugBank; DB00622; Nicardipine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB06712; Nilvadipine.
DrugBank; DB00393; Nimodipine.
DrugBank; DB00401; Nisoldipine.
DrugBank; DB01054; Nitrendipine.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00661; Verapamil.
GuidetoPHARMACOLOGY; 529; -.
TCDB; 1.A.1.11.4; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q13936; -.
PhosphoSitePlus; Q13936; -.
BioMuta; CACNA1C; -.
DMDM; 308153651; -.
PaxDb; Q13936; -.
PeptideAtlas; Q13936; -.
PRIDE; Q13936; -.
Ensembl; ENST00000344100; ENSP00000341092; ENSG00000151067. [Q13936-14]
Ensembl; ENST00000347598; ENSP00000266376; ENSG00000151067. [Q13936-11]
Ensembl; ENST00000399591; ENSP00000382500; ENSG00000151067. [Q13936-29]
Ensembl; ENST00000399595; ENSP00000382504; ENSG00000151067. [Q13936-25]
Ensembl; ENST00000399597; ENSP00000382506; ENSG00000151067. [Q13936-22]
Ensembl; ENST00000399601; ENSP00000382510; ENSG00000151067. [Q13936-20]
Ensembl; ENST00000399603; ENSP00000382512; ENSG00000151067. [Q13936-37]
Ensembl; ENST00000399606; ENSP00000382515; ENSG00000151067. [Q13936-30]
Ensembl; ENST00000399621; ENSP00000382530; ENSG00000151067. [Q13936-24]
Ensembl; ENST00000399629; ENSP00000382537; ENSG00000151067. [Q13936-32]
Ensembl; ENST00000399637; ENSP00000382546; ENSG00000151067. [Q13936-27]
Ensembl; ENST00000399638; ENSP00000382547; ENSG00000151067. [Q13936-31]
Ensembl; ENST00000399641; ENSP00000382549; ENSG00000151067. [Q13936-23]
Ensembl; ENST00000399644; ENSP00000382552; ENSG00000151067. [Q13936-21]
Ensembl; ENST00000399649; ENSP00000382557; ENSG00000151067. [Q13936-15]
Ensembl; ENST00000399655; ENSP00000382563; ENSG00000151067. [Q13936-12]
Ensembl; ENST00000402845; ENSP00000385724; ENSG00000151067. [Q13936-13]
GeneID; 775; -.
KEGG; hsa:775; -.
UCSC; uc001qjz.3; human. [Q13936-1]
CTD; 775; -.
DisGeNET; 775; -.
EuPathDB; HostDB:ENSG00000151067.20; -.
GeneCards; CACNA1C; -.
GeneReviews; CACNA1C; -.
H-InvDB; HIX0010327; -.
HGNC; HGNC:1390; CACNA1C.
HPA; HPA039796; -.
MalaCards; CACNA1C; -.
MIM; 114205; gene.
MIM; 601005; phenotype.
MIM; 611875; phenotype.
neXtProt; NX_Q13936; -.
OpenTargets; ENSG00000151067; -.
Orphanet; 130; Brugada syndrome.
Orphanet; 65283; Timothy syndrome.
PharmGKB; PA83; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128247; -.
HOVERGEN; HBG050763; -.
InParanoid; Q13936; -.
KO; K04850; -.
PhylomeDB; Q13936; -.
TreeFam; TF312805; -.
Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
SIGNOR; Q13936; -.
ChiTaRS; CACNA1C; human.
EvolutionaryTrace; Q13936; -.
GeneWiki; Cav1.2; -.
GenomeRNAi; 775; -.
PRO; PR:Q13936; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000151067; -.
ExpressionAtlas; Q13936; baseline and differential.
Genevisible; Q13936; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; IPI:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; IMP:BHF-UCL.
GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:BHF-UCL.
GO; GO:0060402; P:calcium ion transport into cytosol; TAS:BHF-UCL.
GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; TAS:BHF-UCL.
GO; GO:0043010; P:camera-type eye development; IMP:BHF-UCL.
GO; GO:0061337; P:cardiac conduction; IMP:UniProtKB.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:BHF-UCL.
GO; GO:0007507; P:heart development; IMP:BHF-UCL.
GO; GO:0002520; P:immune system development; IMP:BHF-UCL.
GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; IMP:BHF-UCL.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; TAS:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
Gene3D; 1.20.120.350; -; 6.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005451; VDCC_L_a1csu.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16885; CAC1F_C; 2.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 5.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01630; LVDCCALPHA1.
PRINTS; PR01635; LVDCCALPHA1C.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autism; Autism spectrum disorder;
Brugada syndrome; Calcium; Calcium channel; Calcium transport;
Cell membrane; Complete proteome; Disease mutation; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Long QT syndrome; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 2221 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053928.
TOPO_DOM 1 124 Cytoplasmic. {ECO:0000255}.
TRANSMEM 125 143 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 144 160 Extracellular. {ECO:0000255}.
TRANSMEM 161 181 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 182 193 Cytoplasmic. {ECO:0000255}.
TRANSMEM 194 212 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 213 232 Extracellular. {ECO:0000255}.
TRANSMEM 233 251 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 252 270 Cytoplasmic. {ECO:0000255}.
TRANSMEM 271 290 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 291 380 Extracellular. {ECO:0000255}.
TRANSMEM 381 405 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 406 524 Cytoplasmic. {ECO:0000255}.
TRANSMEM 525 543 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 544 558 Extracellular. {ECO:0000255}.
TRANSMEM 559 578 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 579 586 Cytoplasmic. {ECO:0000255}.
TRANSMEM 587 605 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 606 615 Extracellular. {ECO:0000255}.
TRANSMEM 616 634 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 635 653 Cytoplasmic. {ECO:0000255}.
TRANSMEM 654 673 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 674 728 Extracellular. {ECO:0000255}.
TRANSMEM 729 753 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 754 900 Cytoplasmic. {ECO:0000255}.
TRANSMEM 901 919 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 920 935 Extracellular. {ECO:0000255}.
TRANSMEM 936 955 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 956 987 Cytoplasmic. {ECO:0000255}.
TRANSMEM 988 1006 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1007 1013 Extracellular. {ECO:0000255}.
TRANSMEM 1014 1032 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1033 1051 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1052 1071 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1072 1161 Extracellular. {ECO:0000255}.
TRANSMEM 1162 1186 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1187 1239 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1240 1258 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1259 1273 Extracellular. {ECO:0000255}.
TRANSMEM 1274 1293 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1294 1301 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1302 1320 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1321 1372 Extracellular. {ECO:0000255}.
TRANSMEM 1373 1391 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1392 1410 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1411 1430 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1431 1499 Extracellular. {ECO:0000255}.
TRANSMEM 1500 1524 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1525 2221 Cytoplasmic. {ECO:0000255}.
REPEAT 111 408 I.
REPEAT 510 756 II.
REPEAT 887 1189 III.
REPEAT 1226 1527 IV.
CA_BIND 1553 1564 {ECO:0000250}.
REGION 428 445 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000250|UniProtKB:P22002}.
REGION 829 876 Interaction with STAC2.
{ECO:0000269|PubMed:29078335}.
REGION 1109 1199 Dihydropyridine binding. {ECO:0000250}.
REGION 1478 1546 Dihydropyridine binding. {ECO:0000250}.
REGION 1492 1535 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 654 660 Poly-Leu.
COMPBIAS 768 774 Poly-Glu.
COMPBIAS 1167 1173 Poly-Ile.
COMPBIAS 2084 2087 Poly-Gly.
SITE 363 363 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8099908}.
SITE 706 706 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1135 1135 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8099908}.
SITE 1464 1464 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8099908}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 476 476 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1535 1535 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1718 1718 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1739 1739 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1973 1973 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1981 1981 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1436 1436 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1487 1487 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 29 Missing (in isoform 16, isoform 17,
isoform 18 and isoform 28).
{ECO:0000303|PubMed:8392192,
ECO:0000303|PubMed:9087614,
ECO:0000303|Ref.10}.
/FTId=VSP_000885.
VAR_SEQ 1 16 MVNENTRMYIPEENHQ -> MLRAFVQPGTPAYQPLPSHLS
ANTEVKFKGTLVHEAQLNYFYISPG (in isoform
34). {ECO:0000303|PubMed:11741969}.
/FTId=VSP_035146.
VAR_SEQ 306 308 Missing (in isoform 35).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035877.
VAR_SEQ 372 391 VNDAVGRDWPWIYFVTLIII -> MQDAMGYELPWVYFVSL
VIF (in isoform 3, isoform 16, isoform
17, isoform 18, isoform 23, isoform 28,
isoform 36 and isoform 37).
{ECO:0000303|PubMed:8392192,
ECO:0000303|PubMed:9087614,
ECO:0000303|PubMed:9607315,
ECO:0000303|Ref.10}.
/FTId=VSP_000886.
VAR_SEQ 932 951 Missing (in isoform 4, isoform 19,
isoform 20, isoform 21, isoform 23,
isoform 26, isoform 27, isoform 29,
isoform 32 and isoform 33).
{ECO:0000303|PubMed:7737988,
ECO:0000303|PubMed:9013606,
ECO:0000303|PubMed:9607315,
ECO:0000303|Ref.10}.
/FTId=VSP_000887.
VAR_SEQ 952 971 Missing (in isoform 5, isoform 12,
isoform 13, isoform 14, isoform 15,
isoform 16, isoform 17, isoform 18,
isoform 22, isoform 24, isoform 25,
isoform 28, isoform 31, isoform 35,
isoform 36 and isoform 37).
{ECO:0000303|PubMed:12176756,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17071743,
ECO:0000303|PubMed:7737988,
ECO:0000303|PubMed:8392192,
ECO:0000303|PubMed:9087614,
ECO:0000303|PubMed:9607315,
ECO:0000303|Ref.10}.
/FTId=VSP_000888.
VAR_SEQ 1297 1324 Missing (in isoform 6, isoform 12,
isoform 14, isoform 15, isoform 19,
isoform 20, isoform 23, isoform 24,
isoform 25, isoform 26, isoform 27,
isoform 28, isoform 29, isoform 30 and
isoform 33).
{ECO:0000303|PubMed:12176756,
ECO:0000303|PubMed:17071743,
ECO:0000303|PubMed:7737988,
ECO:0000303|PubMed:8392192,
ECO:0000303|PubMed:9013606,
ECO:0000303|PubMed:9607315,
ECO:0000303|Ref.10}.
/FTId=VSP_000889.
VAR_SEQ 1325 1352 Missing (in isoform 7, isoform 13,
isoform 16, isoform 17, isoform 18,
isoform 21, isoform 22, isoform 35,
isoform 36 and isoform 37).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17071743,
ECO:0000303|PubMed:8392192,
ECO:0000303|PubMed:9087614,
ECO:0000303|PubMed:9607315}.
/FTId=VSP_000890.
VAR_SEQ 1351 1363 Missing (in isoform 15).
{ECO:0000303|PubMed:17071743}.
/FTId=VSP_022503.
VAR_SEQ 1353 1363 Missing (in isoform 8, isoform 19,
isoform 25, isoform 28, isoform 29 and
isoform 32).
{ECO:0000303|PubMed:17071743,
ECO:0000303|PubMed:7737988,
ECO:0000303|PubMed:8392192,
ECO:0000303|Ref.10}.
/FTId=VSP_000891.
VAR_SEQ 1363 1363 M -> MGPSCSHPPLAVLTAPPVADGFQ (in isoform
14). {ECO:0000303|PubMed:17071743}.
/FTId=VSP_022504.
VAR_SEQ 1618 1699 LRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGD
DEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSL
-> LREAELSSQVQYQAKEASLLERRRKSSHPKSSTKPNKL
LSSGGSTGWVEDARALEGQVLARGCGWLGSLEERERGPHHP
PLGF (in isoform 9 and isoform 26).
{ECO:0000303|PubMed:9013606}.
/FTId=VSP_000892.
VAR_SEQ 1623 1623 E -> EEGPSPSEAHQGAEDPFRPA (in isoform 10,
isoform 13, isoform 14, isoform 15,
isoform 24, isoform 25, isoform 27 and
isoform 29).
{ECO:0000303|PubMed:17071743,
ECO:0000303|PubMed:9013606,
ECO:0000303|Ref.10}.
/FTId=VSP_000893.
VAR_SEQ 1864 1898 Missing (in isoform 11, isoform 12,
isoform 13, isoform 14, isoform 15,
isoform 17, isoform 19, isoform 20,
isoform 21, isoform 22, isoform 23,
isoform 24, isoform 25, isoform 26,
isoform 27, isoform 29, isoform 30,
isoform 31, isoform 32, isoform 35 and
isoform 37).
{ECO:0000303|PubMed:12176756,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17071743,
ECO:0000303|PubMed:7737988,
ECO:0000303|PubMed:9013606,
ECO:0000303|PubMed:9087614,
ECO:0000303|PubMed:9607315,
ECO:0000303|Ref.10}.
/FTId=VSP_000895.
VAR_SEQ 1864 1897 ERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPS -> MHC
CDMLDGGTFPPALGPRRAPPCLHQQLQGSLAGLREDTPCIV
PGHASLCCSSRVGEWLPAGCTAPQHA (in isoform 2,
isoform 18 and isoform 28).
{ECO:0000303|PubMed:8392192,
ECO:0000303|Ref.10}.
/FTId=VSP_000894.
VARIANT 28 28 A -> T (in TS; only with cardiac
manifestation; unknown pathological
significance; increased channel
activity). {ECO:0000269|PubMed:25633834}.
/FTId=VAR_075148.
VARIANT 37 37 G -> R (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075149.
VARIANT 39 39 A -> V (in BRGDA3; loss of function).
{ECO:0000269|PubMed:17224476}.
/FTId=VAR_044039.
VARIANT 84 84 Q -> R (in dbSNP:rs1051345).
{ECO:0000269|PubMed:8392192,
ECO:0000269|PubMed:9087614,
ECO:0000269|Ref.10}.
/FTId=VAR_045987.
VARIANT 304 304 I -> T (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075150.
VARIANT 381 381 P -> S (in TS; only with cardiac
manifestation; unknown pathological
significance; no effect on channel
activity). {ECO:0000269|PubMed:24728418}.
/FTId=VAR_075151.
VARIANT 391 391 I -> L (in dbSNP:rs1051356).
/FTId=VAR_045988.
VARIANT 402 402 G -> S (in TS).
{ECO:0000269|PubMed:15863612}.
/FTId=VAR_026741.
VARIANT 406 406 G -> R (in TS; causes a nearly complete
loss of voltage-dependent channel
inactivation).
{ECO:0000269|PubMed:15454078}.
/FTId=VAR_026742.
VARIANT 456 456 M -> I (in TS; only with cardiac
manifestation; unknown pathological
significance; no effect on channel
activity). {ECO:0000269|PubMed:24728418}.
/FTId=VAR_075152.
VARIANT 477 477 E -> K (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075153.
VARIANT 490 490 G -> R (in BRGDA3; loss of function).
{ECO:0000269|PubMed:17224476}.
/FTId=VAR_044040.
VARIANT 518 518 R -> C (in TS; only with cardiac
manifestation; decreased current density;
associated with slower inactivation;
altered localization).
{ECO:0000269|PubMed:26253506}.
/FTId=VAR_075154.
VARIANT 518 518 R -> H (in TS; only with cardiac
manifestation; decreased current density;
associated with slower inactivation).
{ECO:0000269|PubMed:26253506}.
/FTId=VAR_075155.
VARIANT 582 582 A -> D (in TS; only with cardiac
manifestation; gain of function effect on
channel activity; slower inactivation).
{ECO:0000269|PubMed:24728418}.
/FTId=VAR_075156.
VARIANT 752 752 A -> T.
/FTId=VAR_001495.
VARIANT 817 817 P -> S (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075157.
VARIANT 850 850 Missing (rare variant; found in a case of
sudden unexplained death in the young;
unknown pathological significance;
results in reduced whole-cell calcium
currents). {ECO:0000269|PubMed:27218670}.
/FTId=VAR_076414.
VARIANT 858 858 R -> H (in TS; only with cardiac
manifestation; gain of function effect on
channel activity; slower inactivation).
{ECO:0000269|PubMed:24728418}.
/FTId=VAR_075158.
VARIANT 860 860 R -> G (in TS; only with cardiac
manifestation; gain of function
activity). {ECO:0000269|PubMed:25633834}.
/FTId=VAR_075159.
VARIANT 878 878 S -> R (found in a clear cell renal
carcinoma case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064700.
VARIANT 1159 1159 R -> H (found in a patient with autism;
unknown pathological significance).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078701.
VARIANT 1186 1186 I -> T (in TS; electrophysiological
phenotype, characterized by loss of
current density and gain-of-function
shift in activation leading to increased
steady-state current; gain of function
activity). {ECO:0000269|PubMed:25260352,
ECO:0000269|PubMed:25633834}.
/FTId=VAR_072381.
VARIANT 1186 1186 I -> V (in TS; only with cardiac
manifestation; gain of function
activity). {ECO:0000269|PubMed:25633834}.
/FTId=VAR_075160.
VARIANT 1365 1365 A -> T (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075161.
VARIANT 1523 1523 I -> M (in TS; only with cardiac
manifestation; gain of function
activity). {ECO:0000269|PubMed:25633834}.
/FTId=VAR_075162.
VARIANT 1544 1544 E -> K (in TS; only with cardiac
manifestation; gain of function
activity). {ECO:0000269|PubMed:25633834}.
/FTId=VAR_075163.
VARIANT 1755 1755 V -> I (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075164.
VARIANT 1765 1765 A -> G (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075165.
VARIANT 1787 1787 D -> N (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075166.
VARIANT 1800 1800 T -> I (in TS; only with cardiac
manifestation; unknown pathological
significance).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075167.
VARIANT 1831 1831 G -> C (in TS; only with cardiac
manifestation; unknown pathological
significance; no effect on channel
activity). {ECO:0000269|PubMed:24728418}.
/FTId=VAR_075168.
VARIANT 1835 1835 T -> M (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075169.
VARIANT 1843 1843 G -> A (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075170.
VARIANT 1868 1868 P -> L (in dbSNP:rs10848683).
/FTId=VAR_059223.
VARIANT 1869 1869 M -> V (in dbSNP:rs10774053).
{ECO:0000269|PubMed:1316612,
ECO:0000269|PubMed:9087614,
ECO:0000269|Ref.10}.
/FTId=VAR_059224.
VARIANT 1893 1893 K -> R (in dbSNP:rs10774054).
{ECO:0000269|PubMed:1316612,
ECO:0000269|PubMed:9087614,
ECO:0000269|Ref.10}.
/FTId=VAR_061102.
VARIANT 1948 1948 E -> K (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075171.
VARIANT 1953 1953 T -> M (in TS; only with cardiac
manifestation; unknown pathological
significance).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075172.
VARIANT 1972 1972 R -> C (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075173.
VARIANT 2056 2056 R -> Q (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075174.
VARIANT 2081 2081 T -> N (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075175.
VARIANT 2091 2091 A -> S (rare variant; found in a case of
sudden unexplained death in the young;
unknown pathological significance;
results in increased whole-cell calcium
currents). {ECO:0000269|PubMed:27218670}.
/FTId=VAR_076415.
VARIANT 2097 2097 V -> I (in TS; only with cardiac
manifestation; unknown pathological
significance).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075176.
VARIANT 2122 2122 A -> G (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075177.
VARIANT 2169 2169 A -> T.
/FTId=VAR_001496.
VARIANT 2174 2174 N -> S (polymorphism).
{ECO:0000269|PubMed:25633834}.
/FTId=VAR_075178.
MUTAGEN 363 363 E->K: Loss of selectivity for divalent
over monovalent cations.
{ECO:0000269|PubMed:8099908}.
MUTAGEN 954 954 G->F: Affects voltage-dependent
inhibition by dihydropyridines; when
associated with I-958.
{ECO:0000269|PubMed:7737988}.
MUTAGEN 958 958 Y->I: Affects voltage-dependent
inhibition by dihydropyridines; when
associated with F-954.
{ECO:0000269|PubMed:7737988}.
MUTAGEN 1135 1135 E->K: Loss of selectivity for divalent
over monovalent cations.
{ECO:0000269|PubMed:8099908}.
MUTAGEN 1464 1464 E->K: Loss of selectivity for divalent
over monovalent cations.
{ECO:0000269|PubMed:8099908}.
CONFLICT 1072 1072 K -> Q (in Ref. 3; Z26272).
{ECO:0000305}.
CONFLICT 1157 1157 N -> K (in Ref. 15; AAA58409).
{ECO:0000305}.
CONFLICT 1244 1244 L -> P (in Ref. 16; AAA74590).
{ECO:0000305}.
CONFLICT 1384 1384 L -> P (in Ref. 16; AAA74590).
{ECO:0000305}.
CONFLICT 1412 1412 A -> V (in Ref. 12; AAI46847).
{ECO:0000305}.
CONFLICT 1459 1459 R -> K (in Ref. 3; CAA81219).
{ECO:0000305}.
CONFLICT 2205 2205 R -> A (in Ref. 3; CAA84340/CAA84341/
CAA84342/CAA84343/CAA84344/CAA84345/
CAA84346/CAA84347/CAA84348/CAA84349/
CAA84350/CAA84351, 7; CAA12174 and 9;
AAX37354/AAX37355/AAX37356).
{ECO:0000305}.
CONFLICT 2205 2205 R -> G (in Ref. 1; AAA17030).
{ECO:0000305}.
HELIX 48 65 {ECO:0000244|PDB:2LQC}.
HELIX 429 443 {ECO:0000244|PDB:5V2Q}.
HELIX 1609 1651 {ECO:0000244|PDB:3G43}.
TURN 1661 1663 {ECO:0000244|PDB:2BE6}.
HELIX 1666 1680 {ECO:0000244|PDB:2F3Z}.
SEQUENCE 2221 AA; 248977 MW; 7E755F7AF4C86769 CRC64;
MVNENTRMYI PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR
QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGSTTATRP PRALLCLTLK NPIRRACISI
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA
YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR
VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN
QEGIADVPAE DDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI
TMEGWTDVLY WVNDAVGRDW PWIYFVTLII IGSFFVLNLV LGVLSGEFSK EREKAKARGD
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEEK PRNMSMPTSE TESVNTENVA
GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT
IASEHYNQPN WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFVVCGGI
LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL
FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR
TASPEKKQEL VEKPAVGESK EEKIELKSIT ADGESPPATK INMDDLQPNE NEDKSPYPNP
ETTGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSSNNRFR LQCHRIVNDT
IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILFYFDIVF TTIFTIEIAL KILGNADYVF
TSIFTLEIIL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL
RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD
SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL
LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC
ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH
YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL
SETNHYFCDA WNTFDALIVV GSIVDIAITE VNPAEHTQCS PSMNAEENSR ISITFFRLFR
VMRLVKLLSR GEGIRTLLWT FIKSFQALPY VALLIVMLFF IYAVIGMQVF GKIALNDTTE
INRNNNFQTF PQAVLLLFRC ATGEAWQDIM LACMPGKKCA PESEPSNSTE GETPCGSSFA
VFYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWA EYDPEAKGRI
KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVSMNMPLNS DGTVMFNATL FALVRTALRI
KTEGNLEQAN EELRAIIKKI WKRTSMKLLD QVVPPAGDDE VTVGKFYATF LIQEYFRKFK
KRKEQGLVGK PSQRNALSLQ AGLRTLHDIG PEIRRAISGD LTAEEELDKA MKEAVSAASE
DDIFRRAGGL FGNHVSYYQS DGRSAFPQTF TTQRPLHINK AGSSQGDTES PSHEKLVDST
FTPSSYSSTG SNANINNANN TALGRLPRPA GYPSTVSTVE GHGPPLSPAI RVQEVAWKLS
SNRERHVPMC EDLELRRDSG SAGTQAHCLL LRKANPSRCH SRESQAAMAG QEETSQDETY
EVKMNHDTEA CSEPSLLSTE MLSYQDDENR QLTLPEEDKR DIRQSPKRGF LRSASLGRRA
SFHLECLKRQ KDRGGDISQK TVLPLHLVHH QALAVAGLSP LLQRSHSPAS FPRPFATPPA
TPGSRGWPPQ PVPTLRLEGV ESSEKLNSSF PSIHCGSWAE TTPGGGGSSA ARRVRPVSLM
VPSQAGAPGR QFHGSASSLV EAVLISEGLG QFAQDPKFIE VTTQELADAC DMTIEEMESA
ADNILSGGAP QSPNGALLPF VNCRDAGQDR AGGEEDAGCV RARGRPSEEE LQDSRVYVSS
L


Related products :

Catalog number Product name Quantity
EIAAB05018 CACH2,CACN2,CACNA1C,CACNL1A1,Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle,CCHL1A1,Homo sapiens,Human,Voltage-dependent L-type calcium channel subunit alpha-1C,Voltage-gated
EIAAB05039 CACH1,CACN1,CACNA1S,CACNL1A3,Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle,Homo sapiens,Human,Voltage-dependent L-type calcium channel subunit alpha-1S,Voltage-gated calcium
EIAAB05013 BIII,Brain calcium channel III,CACH5,CACNA1B,CACNL1A5,Calcium channel, L type, alpha-1 polypeptide isoform 5,Homo sapiens,Human,Voltage-dependent N-type calcium channel subunit alpha-1B,Voltage-gated
EIAAB05022 CACH3,CACN4,CACNA1D,CACNL1A2,Calcium channel, L type, alpha-1 polypeptide, isoform 2,CCHL1A2,Homo sapiens,Human,Voltage-dependent L-type calcium channel subunit alpha-1D,Voltage-gated calcium channel
EIAAB05019 Cach3,Cacn4,Cacna1d,Cacnl1a2,Calcium channel, L type, alpha-1 polypeptide isoform 2,Cchl1a2,Mouse,Mus musculus,Voltage-dependent L-type calcium channel subunit alpha-1D,Voltage-gated calcium channel s
EIAAB05026 BII,Brain calcium channel II,CACH6,CACNA1E,CACNL1A6,Calcium channel, L type, alpha-1 polypeptide, isoform 6,Homo sapiens,Human,Voltage-dependent R-type calcium channel subunit alpha-1E,Voltage-gated c
EIAAB05037 CACH1,CACNA1S,CACNL1A3,Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle,Oryctolagus cuniculus,Rabbit,Voltage-dependent L-type calcium channel subunit alpha-1S,Voltage-gated cal
EIAAB05036 Cach1,Cach1b,Cacn1,Cacna1s,Cacnl1a3,Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle,Mouse,Mus musculus,Voltage-dependent L-type calcium channel subunit alpha-1S,Voltage-gated
EIAAB05033 CACNA1H,Homo sapiens,Human,Low-voltage-activated calcium channel alpha1 3.2 subunit,Voltage-dependent T-type calcium channel subunit alpha-1H,Voltage-gated calcium channel subunit alpha Cav3.2
EIAAB05010 BIII,Brain calcium channel III,Cach5,Cacna1b,Cacnl1a5,Calcium channel, L type, alpha-1 polypeptide isoform 5,Cchn1a,Mouse,Mus musculus,Voltage-dependent N-type calcium channel subunit alpha-1B,Voltage
EIAAB05024 BII,Brain calcium channel II,Cach6,Cacna1e,Cacnl1a6,Calcium channel, L type, alpha-1 polypeptide, isoform 6,Cchra1,Mouse,Mus musculus,Voltage-dependent R-type calcium channel subunit alpha-1E,Voltage-
EIAAB05012 BIII,Brain calcium channel III,Cach5,Cacna1b,Cacnl1a5,Calcium channel, L type, alpha-1 polypeptide isoform 5,Rat,Rattus norvegicus,Voltage-dependent N-type calcium channel subunit alpha-1B,Voltage-gat
EIAAB05028 CACNA1F,CACNAF1,Homo sapiens,Human,Voltage-dependent L-type calcium channel subunit alpha-1F,Voltage-gated calcium channel subunit alpha Cav1.4
EIAAB05027 Cacna1f,Mouse,Mus musculus,Voltage-dependent L-type calcium channel subunit alpha-1F,Voltage-gated calcium channel subunit alpha Cav1.4
EIAAB05025 BII,Brain calcium channel II,CACH6,CACNA1E,CACNL1A6,Calcium channel, L type, alpha-1 polypeptide, isoform 6,Oryctolagus cuniculus,Rabbit,Voltage-dependent R-type calcium channel subunit alpha-1E,Volta
EIAAB05023 BII,Brain calcium channel II,Cach6,Cacna1e,Cacnl1a6,Calcium channel, L type, alpha-1 polypeptide, isoform 6,Rat,Rattus norvegicus,RBE2,RBE-II,Voltage-dependent R-type calcium channel subunit alpha-1E,
EIAAB05009 BIII,Brain calcium channel III,CACH5,CACNA1B,CACNL1A5,Calcium channel, L type, alpha-1 polypeptide isoform 5,Oryctolagus cuniculus,Rabbit,Voltage-dependent N-type calcium channel subunit alpha-1B,Volt
E1344h ELISA kit BI,Brain calcium channel I,CACH4,CACN3,CACNA1A,CACNL1A4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Homo sapiens,Human,Voltage-dependent P_Q-type calcium channel subunit alpha-1A 96T
E1344h ELISA BI,Brain calcium channel I,CACH4,CACN3,CACNA1A,CACNL1A4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Homo sapiens,Human,Voltage-dependent P_Q-type calcium channel subunit alpha-1A,Volt 96T
U1344h CLIA BI,Brain calcium channel I,CACH4,CACN3,CACNA1A,CACNL1A4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Homo sapiens,Human,Voltage-dependent P_Q-type calcium channel subunit alpha-1A,Volta 96T
E1344Rb ELISA BI,Brain calcium channel I,CACH4,CACN3,CACNA1A,CACNL1A4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Oryctolagus cuniculus,Rabbit,Voltage-dependent P_Q-type calcium channel subunit alp 96T
EIAAB05021 CACNA1D,CHCACHA1D,Chicken,Gallus gallus,Voltage-dependent L-type calcium channel subunit alpha-1D,Voltage-gated calcium channel subunit alpha Cav1.3
EIAAB05017 CACNA1C,CHCACHA1C,Chicken,Gallus gallus,Voltage-dependent L-type calcium channel subunit alpha-1C,Voltage-gated calcium channel subunit alpha Cav1.2
E1344m ELISA BI,Brain calcium channel I,Caca1a,Cach4,Cacn3,Cacna1a,Cacnl1a4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Ccha1a,Mouse,Mus musculus,Voltage-dependent P_Q-type calcium channel subunit 96T
U1344Rb CLIA BI,Brain calcium channel I,CACH4,CACN3,CACNA1A,CACNL1A4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Oryctolagus cuniculus,Rabbit,Voltage-dependent P_Q-type calcium channel subunit alph 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur