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

 CAC1C_RABIT             Reviewed;        2171 AA.
P15381; Q03716; Q28676; Q99243;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
10-MAY-2017, entry version 142.
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=Smooth muscle calcium channel blocker receptor;
Short=CACB-receptor;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=CACNA1C; Synonyms=CACH2, CACN2, CACNL1A1, CCHL1A1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=2474130; DOI=10.1038/340230a0;
Mikami A., Imoto K., Tanabe T., Ni Idomme T., Mori Y., Takeshima H.,
Narumiya S., Numa S.;
"Primary structure and functional expression of the cardiac
dihydropyridine-sensitive calcium channel.";
Nature 340:230-233(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart, and Lung;
PubMed=2169433; DOI=10.1016/0014-5793(90)81205-3;
Biel M., Ruth P., Bosse E., Hullin R., Stuehmer W., Flockerzi V.,
Hoffmann F.;
"Primary structure and functional expression of a high voltage
activated calcium channel from rabbit lung.";
FEBS Lett. 269:409-412(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 5).
TISSUE=Heart muscle;
PubMed=1652442; DOI=10.1111/j.1432-1033.1991.tb21051.x;
Biel M., Hullin R., Freundner S., Singer D., Dascal N., Flockerzi V.,
Hofmann F.;
"Tissue-specific expression of high-voltage-activated dihydropyridine-
sensitive L-type calcium channels.";
Eur. J. Biochem. 200:81-88(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1192-1485 (ISOFORM 2).
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).
[5]
MUTAGENESIS, CALCIUM-BINDING, AND SITE.
PubMed=8232554; DOI=10.1038/366158a0;
Yang J., Ellinor P.T., Sather W.A., Zhang J.-F., Tsien R.W.;
"Molecular determinants of Ca2+ selectivity and ion permeation in L-
type Ca2+ channels.";
Nature 366:158-161(1993).
[6]
MUTAGENESIS OF CYS-168.
PubMed=9502794;
Ren D., Xu H., Eberl D.F., Chopra M., Hall L.M.;
"A mutation affecting dihydropyridine-sensitive current levels and
activation kinetics in Drosophila muscle and mammalian heart calcium
channels.";
J. Neurosci. 18:2335-2341(1998).
[7]
PHOSPHORYLATION BY PKA.
PubMed=1325377; DOI=10.1016/0014-5793(92)80804-P;
Yoshida A., Takahashi M., Nishimura S., Takeshima H., Kokubun S.;
"Cyclic AMP-dependent phosphorylation and regulation of the cardiac
dihydropyridine-sensitive Ca channel.";
FEBS Lett. 309:343-349(1992).
[8]
BETA-SUBUNIT BINDING DOMAIN.
PubMed=7509046; DOI=10.1038/368067a0;
Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P.,
Campbell K.P.;
"Calcium channel beta-subunit binds to a conserved motif in the I-II
cytoplasmic linker of the alpha 1-subunit.";
Nature 368:67-70(1994).
[9]
EF-HAND MOTIF AND CALCIUM INACTIVATION.
PubMed=7491499; DOI=10.1126/science.270.5241.1502;
de Leon M., Wang Y., Jones L., Perez-Reyes E., Wei X., Soong T.W.,
Snutch T.P., Yue D.T.;
"Essential Ca(2+)-binding motif for Ca(2+)-sensitive inactivation of
L-type Ca2+ channels.";
Science 270:1502-1505(1995).
[10]
SUBCELLULAR LOCATION.
PubMed=17525370; DOI=10.1161/CIRCRESAHA.106.146399;
Yada H., Murata M., Shimoda K., Yuasa S., Kawaguchi H., Ieda M.,
Adachi T., Murata M., Ogawa S., Fukuda K.;
"Dominant negative suppression of Rad leads to QT prolongation and
causes ventricular arrhythmias via modulation of L-type Ca2+ channels
in the heart.";
Circ. Res. 101:69-77(2007).
-!- 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|UniProtKB:P22002,
ECO:0000250|UniProtKB:Q01815, ECO:0000250|UniProtKB:Q13936}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17525370};
Multi-pass membrane protein {ECO:0000269|PubMed:17525370}. Cell
membrane {ECO:0000269|PubMed:17525370}. Note=The interaction
between RRAD and CACNB2 regulates its trafficking to the cell
membrane. {ECO:0000269|PubMed:17525370}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=CACH2A;
IsoId=P15381-1; Sequence=Displayed;
Name=2; Synonyms=CACH2C;
IsoId=P15381-2; Sequence=VSP_000906;
Name=3; Synonyms=CACH2D;
IsoId=P15381-3; Sequence=VSP_000907;
Name=4; Synonyms=Lung;
IsoId=P15381-4; Sequence=VSP_000902, VSP_000904, VSP_000905,
VSP_000906;
Name=5; Synonyms=C141;
IsoId=P15381-5; Sequence=VSP_000902, VSP_000903;
-!- TISSUE SPECIFICITY: Expression in cardiac muscle. In lung,
expressed in airway and vascular smooth muscle cells.
-!- 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:0000269|PubMed:7491499}.
-!- PTM: Phosphorylation by PKA activates the channel.
{ECO:0000269|PubMed:1325377}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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EMBL; X15539; CAA33546.1; -; mRNA.
EMBL; X55763; CAA39289.1; -; mRNA.
EMBL; X60782; CAA43196.1; -; mRNA.
EMBL; M57974; AAA31182.1; -; mRNA.
PIR; S05054; S05054.
PIR; S11339; S11339.
RefSeq; NP_001129994.1; NM_001136522.1. [P15381-1]
UniGene; Ocu.1835; -.
UniGene; Ocu.3254; -.
PDB; 4DEY; X-ray; 1.95 A; B=435-539.
PDBsum; 4DEY; -.
ProteinModelPortal; P15381; -.
SMR; P15381; -.
DIP; DIP-61286N; -.
BindingDB; P15381; -.
ChEMBL; CHEMBL2830; -.
iPTMnet; P15381; -.
PRIDE; P15381; -.
GeneID; 100101555; -.
KEGG; ocu:100101555; -.
CTD; 775; -.
HOVERGEN; HBG050763; -.
InParanoid; P15381; -.
KO; K04850; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016021; C:integral component of membrane; ISS: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; ISS:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
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; IDA:BHF-UCL.
GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0098903; P:regulation of membrane repolarization during action potential; IDA:BHF-UCL.
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; 2.
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;
3D-structure; 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 2171 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053930.
TOPO_DOM 1 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 173 Helical; Name=S1 of repeat I.
TOPO_DOM 174 190 Extracellular. {ECO:0000255}.
TRANSMEM 191 211 Helical; Name=S2 of repeat I.
TOPO_DOM 212 223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 224 242 Helical; Name=S3 of repeat I.
TOPO_DOM 243 262 Extracellular. {ECO:0000255}.
TRANSMEM 263 281 Helical; Name=S4 of repeat I.
TOPO_DOM 282 300 Cytoplasmic. {ECO:0000255}.
TRANSMEM 301 320 Helical; Name=S5 of repeat I.
TOPO_DOM 321 410 Extracellular. {ECO:0000255}.
TRANSMEM 411 435 Helical; Name=S6 of repeat I.
TOPO_DOM 436 554 Cytoplasmic. {ECO:0000255}.
TRANSMEM 555 573 Helical; Name=S1 of repeat II.
TOPO_DOM 574 588 Extracellular. {ECO:0000255}.
TRANSMEM 589 608 Helical; Name=S2 of repeat II.
TOPO_DOM 609 616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 617 635 Helical; Name=S3 of repeat II.
TOPO_DOM 636 645 Extracellular. {ECO:0000255}.
TRANSMEM 646 664 Helical; Name=S4 of repeat II.
TOPO_DOM 665 683 Cytoplasmic. {ECO:0000255}.
TRANSMEM 684 703 Helical; Name=S5 of repeat II.
TOPO_DOM 704 758 Extracellular. {ECO:0000255}.
TRANSMEM 759 783 Helical; Name=S6 of repeat II.
TOPO_DOM 784 930 Cytoplasmic. {ECO:0000255}.
TRANSMEM 931 949 Helical; Name=S1 of repeat III.
TOPO_DOM 950 965 Extracellular. {ECO:0000255}.
TRANSMEM 966 985 Helical; Name=S2 of repeat III.
TOPO_DOM 986 997 Cytoplasmic. {ECO:0000255}.
TRANSMEM 998 1016 Helical; Name=S3 of repeat III.
TOPO_DOM 1017 1023 Extracellular. {ECO:0000255}.
TRANSMEM 1024 1042 Helical; Name=S4 of repeat III.
TOPO_DOM 1043 1061 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1062 1081 Helical; Name=S5 of repeat III.
TOPO_DOM 1082 1171 Extracellular. {ECO:0000255}.
TRANSMEM 1172 1196 Helical; Name=S6 of repeat III.
TOPO_DOM 1197 1249 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1250 1268 Helical; Name=S1 of repeat IV.
TOPO_DOM 1269 1283 Extracellular. {ECO:0000255}.
TRANSMEM 1284 1303 Helical; Name=S2 of repeat IV.
TOPO_DOM 1304 1311 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1312 1330 Helical; Name=S3 of repeat IV.
TOPO_DOM 1331 1354 Extracellular. {ECO:0000255}.
TRANSMEM 1355 1373 Helical; Name=S4 of repeat IV.
TOPO_DOM 1374 1392 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1393 1412 Helical; Name=S5 of repeat IV.
TOPO_DOM 1413 1481 Extracellular. {ECO:0000255}.
TRANSMEM 1482 1506 Helical; Name=S6 of repeat IV.
TOPO_DOM 1507 2171 Cytoplasmic. {ECO:0000255}.
REPEAT 141 438 I.
REPEAT 540 786 II.
REPEAT 917 1199 III.
REPEAT 1236 1509 IV.
CA_BIND 1535 1546
REGION 458 475 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000250|UniProtKB:P22002}.
REGION 1119 1209 Dihydropyridine binding. {ECO:0000250}.
REGION 1460 1517 Dihydropyridine binding. {ECO:0000250}.
REGION 1474 1520 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 684 690 Poly-Leu.
COMPBIAS 798 804 Poly-Glu.
COMPBIAS 1177 1183 Poly-Ile.
SITE 393 393 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
SITE 736 736 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
SITE 1145 1145 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
SITE 1446 1446 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 506 506 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 845 845 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1517 1517 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1700 1700 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1721 1721 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1920 1920 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1928 1928 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1418 1418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1469 1469 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 46 MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHF
YISPG -> MVNENTRMYIPEENHQ (in isoform 4
and isoform 5).
{ECO:0000303|PubMed:1652442}.
/FTId=VSP_000902.
VAR_SEQ 66 79 Missing (in isoform 5).
{ECO:0000303|PubMed:1652442}.
/FTId=VSP_000903.
VAR_SEQ 402 421 MQDAMGYELPWVYFVSLVIF -> VNDAVGRDWPWIYFVTL
III (in isoform 4). {ECO:0000305}.
/FTId=VSP_000904.
VAR_SEQ 494 494 M -> RGTPAGLHAQKKGKFAWFSHSTETHV (in
isoform 4). {ECO:0000305}.
/FTId=VSP_000905.
VAR_SEQ 1307 1334 GYFSDPWNVFDFLIVIGSIIDVILSETN -> HYFCDAWNT
FDALIVVGSIVDIAITEVH (in isoform 2 and
isoform 4). {ECO:0000303|PubMed:2173707}.
/FTId=VSP_000906.
VAR_SEQ 1335 1345 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_000907.
MUTAGEN 168 168 C->G: Small reduction of current
amplitude. {ECO:0000269|PubMed:9502794}.
MUTAGEN 168 168 C->K,W: No current.
{ECO:0000269|PubMed:9502794}.
MUTAGEN 168 168 C->S: No effect.
{ECO:0000269|PubMed:9502794}.
MUTAGEN 168 168 C->Y: Slower channel activation and
reduction of current amplitude.
{ECO:0000269|PubMed:9502794}.
MUTAGEN 393 393 E->K: Drastic reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 393 393 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 736 736 E->K: Drastic reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 736 736 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1145 1145 E->K: Drastic reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1145 1145 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1446 1446 E->K: Moderate reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1446 1446 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
CONFLICT 1346 1346 N -> S (in Ref. 4; AAA31182).
{ECO:0000305}.
CONFLICT 1468 1468 H -> S (in Ref. 4; AAA31182).
{ECO:0000305}.
HELIX 451 475 {ECO:0000244|PDB:4DEY}.
SEQUENCE 2171 AA; 242784 MW; B64F08F09D71C65D CRC64;
MLRALVQPAT PAYQPLPSHL SAETESTCKG TVVHEAQLNH FYISPGGSNY 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 QEGVADVPAE DDPSPCALET GHGRQCQNGT
VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI
FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
NEDEGMDEEK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN
RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKV MSPLGISVLR CVRLLRIFKI
TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV VGKPALEEAK EEKIELKSIT
ADGESPPTTK INMDDLQPNE SEDKSPYPNP ETTGEEDEEE PEMPVGPRPR PLSELHLKEK
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN
HILFYFDIVF TTIFTIEIAL 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 CSPSMNAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL
WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF
RCATGEAWQD IMLACMPGKK CAPESEPHNS 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 GLFGNHVSYY
QSDSRSAFPQ TFTTQRPLHI SKAGNNQGDT ESPSHEKLVD STFTPSSYSS TGSNANINNA
NNTALGRLPR PAGYPSTVST VEGHGSPLSP AVRAQEAAWK LSSKRCHSQE SQIAMACQEG
ASQDDNYDVR IGEDAECCSE PSLLSTEMLS YQDDENRQLA PPEEEKRDIR LSPKKGFLRS
ASLGRRASFH LECLKRQKNQ GGDISQKTVL PLHLVHHQAL AVAGLSPLLQ RSHSPTSLPR
PCATPPATPG SRGWPPQPIP TLRLEGADSS EKLNSSFPSI HCGSWSGENS PCRGDSSAAR
RARPVSLTVP SQAGAQGRQF HGSASSLVEA VLISEGLGQF AQDPKFIEVT TQELADACDL
TIEEMENAAD DILSGGARQS PNGTLLPFVN RRDPGRDRAG QNEQDASGAC APGCGQSEEA
LADRRAGVSS L


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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
EIAAB05016 CACB-receptor,CACH2,CACN2,CACNA1C,CACNL1A1,Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle,CCHL1A1,Oryctolagus cuniculus,Rabbit,Smooth muscle calcium channel blocker receptor,V
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
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
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
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
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
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
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-
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
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
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
EIAAB05038 Cach1,Cacn1,Cacna1s,Cacnl1a3,Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle,Cchl1a3,Rat,Rattus norvegicus,ROB1,Voltage-dependent L-type calcium channel subunit alpha-1S,Volta
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
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
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


 

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