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) (MELC-CC) (Mouse brain class C) (MBC) (Voltage-gated calcium channel subunit alpha Cav1.2)

 CAC1C_MOUSE             Reviewed;        2139 AA.
Q01815; Q04476; Q61242; Q99242;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 177.
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=MELC-CC;
AltName: Full=Mouse brain class C;
Short=MBC;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=Cacna1c; Synonyms=Cach2, Cacn2, Cacnl1a1, Cchl1a1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1385406;
Ma W.-J., Holz R.W., Uhler M.D.;
"Expression of a cDNA for a neuronal calcium channel alpha1 subunit
enhances secretion from adrenal chromaffin cells.";
J. Biol. Chem. 267:22728-22732(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1162-1455 (ISOFORMS 1 AND 2).
STRAIN=ICR; TISSUE=Ovary;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 762-1070.
Chaudhari N.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 265-2139 (ISOFORM 3).
STRAIN=DBA/2J; TISSUE=Erythroleukemia;
PubMed=7814415; DOI=10.1074/jbc.270.1.483;
Ma Y., Kobrinsky E., Marks A.R.;
"Cloning and expression of a novel truncated calcium channel from non-
excitable cells.";
J. Biol. Chem. 270:483-493(1995).
[5]
INTERACTION WITH CABP5, AND TISSUE SPECIFICITY.
PubMed=18586882; DOI=10.1167/iovs.08-2236;
Rieke F., Lee A., Haeseleer F.;
"Characterization of Ca2+-binding protein 5 knockout mouse retina.";
Invest. Ophthalmol. Vis. Sci. 49:5126-5135(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469; THR-476; SER-808;
SER-815; SER-1670 AND SER-1691, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH CIB1.
PubMed=20639889; DOI=10.1038/nm.2181;
Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J.,
Yuan W., Drexler H., Parise L.V., Molkentin J.D.;
"CIB1 is a regulator of pathological cardiac hypertrophy.";
Nat. Med. 16:872-879(2010).
-!- 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-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 an opposit effects on the channel function.
{ECO:0000250|UniProtKB:Q13936}.
-!- 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.
Interacts (via C-terminal CDB motif) with CABP5; in a calcium-
dependent manner. Interacts with CABP1 and CACNA2D4 (By
similarity). Interacts with CIB1; the interaction increases upon
cardiomyocytes hypertrophy. {ECO:0000250,
ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:20639889}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P15381};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Cell
membrane {ECO:0000250|UniProtKB:P15381}. 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=3;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=CACH2A;
IsoId=Q01815-1; Sequence=Displayed;
Name=2; Synonyms=CACH2D;
IsoId=Q01815-2; Sequence=VSP_000900, VSP_000901;
Name=3; Synonyms=Truncated;
IsoId=Q01815-3; Sequence=VSP_000896, VSP_000897, VSP_000898,
VSP_000899, VSP_000901;
-!- TISSUE SPECIFICITY: High expression in heart, followed by brain
and spinal cord. Expressed in retina in rod bipolar cells.
{ECO:0000269|PubMed:18586882}.
-!- 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}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L01776; AAB59633.1; -; mRNA.
EMBL; M57973; AAA63291.1; -; mRNA.
EMBL; L06233; AAA37351.1; -; mRNA.
EMBL; U17869; AAA62612.1; -; mRNA.
CCDS; CCDS71821.1; -. [Q01815-3]
CCDS; CCDS80590.1; -. [Q01815-1]
PIR; A44467; A44467.
RefSeq; NP_001153005.1; NM_001159533.2. [Q01815-1]
UniGene; Mm.41628; -.
UniGene; Mm.436656; -.
ProteinModelPortal; Q01815; -.
SMR; Q01815; -.
BioGrid; 198432; 4.
DIP; DIP-32232N; -.
IntAct; Q01815; 4.
MINT; MINT-103522; -.
BindingDB; Q01815; -.
ChEMBL; CHEMBL2529; -.
GuidetoPHARMACOLOGY; 529; -.
TCDB; 1.A.1.11.6; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q01815; -.
PhosphoSitePlus; Q01815; -.
MaxQB; Q01815; -.
PeptideAtlas; Q01815; -.
PRIDE; Q01815; -.
Ensembl; ENSMUST00000075591; ENSMUSP00000075021; ENSMUSG00000051331. [Q01815-1]
Ensembl; ENSMUST00000078320; ENSMUSP00000077433; ENSMUSG00000051331. [Q01815-1]
Ensembl; ENSMUST00000112825; ENSMUSP00000108444; ENSMUSG00000051331. [Q01815-3]
GeneID; 12288; -.
KEGG; mmu:12288; -.
UCSC; uc009dls.3; mouse. [Q01815-3]
UCSC; uc012erl.2; mouse. [Q01815-1]
CTD; 775; -.
MGI; MGI:103013; Cacna1c.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231529; -.
HOVERGEN; HBG050763; -.
InParanoid; Q01815; -.
KO; K04850; -.
PhylomeDB; Q01815; -.
Reactome; R-MMU-419037; NCAM1 interactions.
Reactome; R-MMU-422356; Regulation of insulin secretion.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
Reactome; R-MMU-5576893; Phase 2 - plateau phase.
ChiTaRS; Cacna1c; mouse.
PRO; PR:Q01815; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000051331; -.
ExpressionAtlas; Q01815; baseline and differential.
Genevisible; Q01815; MM.
GO; GO:0002095; C:caveolar macromolecular signaling complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0043198; C:dendritic shaft; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; ISS:SynGO.
GO; GO:0030315; C:T-tubule; IDA:MGI.
GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0051393; F:alpha-actinin binding; ISS:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0008331; F:high voltage-gated calcium channel activity; ISS:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:1905030; F:voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0007628; P:adult walking behavior; IGI:MGI.
GO; GO:0017156; P:calcium ion regulated exocytosis; IMP:MGI.
GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:MGI.
GO; GO:0043010; P:camera-type eye development; ISO:MGI.
GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISS:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0030252; P:growth hormone secretion; IDA:MGI.
GO; GO:0007507; P:heart development; ISO:MGI.
GO; GO:0002520; P:immune system development; ISO:MGI.
GO; GO:0030073; P:insulin secretion; IMP:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
GO; GO:0046620; P:regulation of organ growth; IMP:MGI.
GO; GO:0019229; P:regulation of vasoconstriction; IMP:MGI.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
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.
PANTHER; PTHR10037:SF240; PTHR10037:SF240; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16885; CAC1F_C; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01630; LVDCCALPHA1.
PRINTS; PR01635; LVDCCALPHA1C.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
CHAIN 1 2139 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053929.
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 956 967 Cytoplasmic. {ECO:0000255}.
TRANSMEM 968 986 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 987 993 Extracellular. {ECO:0000255}.
TRANSMEM 994 1012 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1013 1031 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1032 1051 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1052 1141 Extracellular. {ECO:0000255}.
TRANSMEM 1142 1166 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1167 1219 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1220 1238 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1239 1253 Extracellular. {ECO:0000255}.
TRANSMEM 1254 1273 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1274 1281 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1282 1300 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1301 1324 Extracellular. {ECO:0000255}.
TRANSMEM 1325 1343 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1344 1362 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1363 1382 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1383 1451 Extracellular. {ECO:0000255}.
TRANSMEM 1452 1476 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1477 2139 Cytoplasmic. {ECO:0000255}.
REPEAT 111 408 I.
REPEAT 510 756 II.
REPEAT 887 1169 III.
REPEAT 1206 1479 IV.
CA_BIND 1505 1516 {ECO:0000250}.
REGION 428 445 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000250|UniProtKB:P22002}.
COMPBIAS 654 660 Poly-Leu.
COMPBIAS 768 774 Poly-Glu.
COMPBIAS 1147 1153 Poly-Ile.
SITE 363 363 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 706 706 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1115 1115 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1416 1416 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 476 476 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1487 1487 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1670 1670 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1691 1691 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1889 1889 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1897 1897 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1388 1388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1439 1439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 264 Missing (in isoform 3).
{ECO:0000303|PubMed:7814415}.
/FTId=VSP_000896.
VAR_SEQ 372 391 MQDAMGYELPWVYFVSLVIF -> VNDAVGRDWPWIYFVTL
III (in isoform 3).
{ECO:0000303|PubMed:7814415}.
/FTId=VSP_000897.
VAR_SEQ 464 464 M -> RGAPAGLHDQKKGKFAWFSHSTETHV (in
isoform 3). {ECO:0000303|PubMed:7814415}.
/FTId=VSP_000898.
VAR_SEQ 932 951 Missing (in isoform 3).
{ECO:0000303|PubMed:7814415}.
/FTId=VSP_000899.
VAR_SEQ 1277 1304 GYFSDPWNVFDFLIVIGSIIDVILSETN -> HYFCDAWNT
FDALIVVGSIVDIAITEVH (in isoform 2).
{ECO:0000303|PubMed:2173707}.
/FTId=VSP_000900.
VAR_SEQ 1305 1315 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:2173707,
ECO:0000303|PubMed:7814415}.
/FTId=VSP_000901.
CONFLICT 310 310 E -> K (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 477 477 E -> D (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 555 555 V -> D (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 811 812 AD -> GS (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 822 822 N -> H (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 825 825 D -> A (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 831 831 N -> P (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 837 841 HSNPD -> TPTQT (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 934 938 GNADY -> FYFDI (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 942 942 S -> T (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 946 946 L -> I (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 949 949 I -> A (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 977 978 VS -> LC (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1065 1065 T -> A (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1507 1507 E -> K (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1525 1525 Q -> H (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1633 1633 K -> E (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1959 1959 G -> A (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1963 1964 RP -> ST (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1970 1970 T -> H (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1974 1974 E -> K (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 2086 2086 A -> R (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 2097 2097 F -> L (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 2110 2110 A -> V (in Ref. 4; AAA62612).
{ECO:0000305}.
SEQUENCE 2139 AA; 240138 MW; B564C57A8644E165 CRC64;
MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR
QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA
YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR
VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN
QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI
TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE TESVNTENVA
GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT
IASEHYNQPH WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI
LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL
FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR
TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP
DTAGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT
IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF 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 SETNPAEHTQ CSPSMSAEEN
SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ
VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS
TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI
WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA
TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA
TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD
KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT
ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP
AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP SLLSTDMFSY
QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP
LHLVHHQALA VAGLSPLLQR SHSPTTFPRP CPTPPVTPGS RGRPLRPIPT LRLEGAESSE
KLNSSFPSIH CSSWSEETTA CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV
LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC
RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL


Related products :

Catalog number Product name Quantity
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
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
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
EIAAB05015 Cach2,Cacn2,Cacna1c,Cacnl1a1,Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle,Cchl1a1,MBC,MELC-CC,Mouse,Mouse brain class C,Mus musculus,Voltage-dependent L-type 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
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
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
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
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-
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
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
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
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,
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
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
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
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
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
U1344m CLIA 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
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
EIAAB05027 Cacna1f,Mouse,Mus musculus,Voltage-dependent L-type calcium channel subunit alpha-1F,Voltage-gated calcium channel subunit alpha Cav1.4
EIAAB05028 CACNA1F,CACNAF1,Homo sapiens,Human,Voltage-dependent L-type calcium channel subunit alpha-1F,Voltage-gated calcium channel subunit alpha Cav1.4
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
EIAAB05020 Cach3,Cacn4,Cacna1d,Cacnl1a2,Calcium channel, L type, alpha-1 polypeptide, isoform 2,Cchl1a2,Rat,Rat brain class D,Rattus norvegicus,RBD,Voltage-dependent L-type calcium channel subunit alpha-1D,Volta


 

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