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Voltage-dependent L-type calcium channel subunit alpha-1D (Calcium channel, L type, alpha-1 polypeptide, isoform 2) (Rat brain class D) (RBD) (Voltage-gated calcium channel subunit alpha Cav1.3)

 CAC1D_RAT               Reviewed;        2203 AA.
P27732; O09022; O09023; O09024; Q01542; Q62691; Q62815; Q63491;
Q63492;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
27-SEP-2017, entry version 146.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 2;
AltName: Full=Rat brain class D;
Short=RBD;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Insulinoma;
PubMed=7760845; DOI=10.1210/mend.9.1.7760845;
Ihara Y., Yamada Y., Fujii Y., Gonoi T., Yano H., Yasuda K.,
Inagaki N., Seino Y., Seino S.;
"Molecular diversity and functional characterization of voltage-
dependent calcium channels (CACN4) expressed in pancreatic beta-
cells.";
Mol. Endocrinol. 9:121-130(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 13).
TISSUE=Brain;
PubMed=1648940; DOI=10.1016/0896-6273(91)90072-8;
Hui A., Ellinor P.T., Krizanova O., Wang J.-J., Diebold R.J.,
Schwartz A.;
"Molecular cloning of multiple subtypes of a novel rat brain isoform
of the alpha-1 subunit of the voltage-dependent calcium channel.";
Neuron 7:35-44(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
PubMed=7553731; DOI=10.1007/BF02089942;
Kamp T.J., Mitas M., Fields K.L., Asoh S., Chin H., Marban E.,
Nirenberg M.;
"Transcriptional regulation of the neuronal L-type calcium channel
alpha 1D subunit gene.";
Cell. Mol. Neurobiol. 15:307-326(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1100-1410 (ISOFORMS 4 AND 11).
TISSUE=Kidney;
PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
"Molecular characterization and nephron distribution of a family of
transcripts encoding the pore-forming subunit of Ca2+ channels in the
kidney.";
Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1218-1498 (ISOFORM 12).
TISSUE=Osteosarcoma;
PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
"Multiple calcium channel transcripts in rat osteosarcoma cells:
selective activation of alpha 1D isoform by parathyroid hormone.";
Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1200-1493 (ISOFORMS 3; 4; 5; 9 AND 10).
TISSUE=Hepatoma;
PubMed=9232351; DOI=10.1016/S0143-4160(97)90088-9;
Brereton H.M., Harland M.L., Froscio M., Petronijevic T.,
Barritt G.J.;
"Novel variants of voltage-operated calcium channel alpha-1 subunit
transcripts in a rat liver-derived cell line: deletion in the IVS4
voltage sensing region.";
Cell Calcium 22:39-52(1997).
[7]
NUCLEOTIDE SEQUENCE OF 1307-1479 (ISOFORM 3).
PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
"Rat brain expresses a heterogeneous family of calcium channels.";
Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
[8]
FUNCTION, MUTAGENESIS OF 1656-ILE-GLN-1657, INTERACTION WITH CABP1 AND
CABP4, AND TISSUE SPECIFICITY.
PubMed=17050707; DOI=10.1523/JNEUROSCI.3236-06.2006;
Yang P.S., Alseikhan B.A., Hiel H., Grant L., Mori M.X., Yang W.,
Fuchs P.A., Yue D.T.;
"Switching of Ca2+-dependent inactivation of Ca(v)1.3 channels by
calcium binding proteins of auditory hair cells.";
J. Neurosci. 26:10677-10689(2006).
-!- 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-1D
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).
{ECO:0000269|PubMed:17050707}.
-!- 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 with CABP1 and CABP4, resulting in a near elimination of
calcium-dependent inactivation of the channel. Interacts with
RIMBP2 (By similarity). {ECO:0000250}.
-!- INTERACTION:
O88871:Gabbr2; NbExp=6; IntAct=EBI-8072674, EBI-7090239;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Comment=The region sequenced in isoforms ROB3 and RKC5 is
identical to CACN4.;
Name=1; Synonyms=CACN4A;
IsoId=P27732-1; Sequence=Displayed;
Name=2; Synonyms=CACN4B;
IsoId=P27732-2; Sequence=VSP_000923, VSP_000924;
Name=3; Synonyms=CACH3A, RB48, RBD-55;
IsoId=P27732-3; Sequence=VSP_000921;
Name=4; Synonyms=Delta-IV-S3, RKC6;
IsoId=P27732-4; Sequence=VSP_000919;
Name=5; Synonyms=Delta-IV-S4;
IsoId=P27732-5; Sequence=VSP_000922;
Name=6; Synonyms=RB9;
IsoId=P27732-6; Sequence=VSP_000920, VSP_000921;
Name=7; Synonyms=RB11;
IsoId=P27732-7; Sequence=VSP_000917;
Name=8; Synonyms=RB34;
IsoId=P27732-8; Sequence=VSP_000916;
Name=9; Synonyms=RH1;
IsoId=P27732-9; Sequence=VSP_000918;
Name=10; Synonyms=RH2;
IsoId=P27732-10; Sequence=VSP_000919, VSP_000922;
Name=11; Synonyms=RKC5;
IsoId=P27732-13; Sequence=Not described;
Name=12; Synonyms=ROB3;
IsoId=P27732-14; Sequence=Not described;
Name=13; Synonyms=Truncated;
IsoId=P27732-12; Sequence=VSP_000925, VSP_000926;
-!- TISSUE SPECIFICITY: Expressed in brain, pancreatic islets and B-
lymphocytes. {ECO:0000269|PubMed:17050707}.
-!- 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
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EMBL; D38101; BAA07282.1; -; mRNA.
EMBL; D38102; BAA07283.1; -; mRNA.
EMBL; M57682; AAA42015.1; -; mRNA.
EMBL; U14005; AAB60515.1; -; Genomic_DNA.
EMBL; M99221; AAA40895.1; -; mRNA.
EMBL; U31772; AAA89156.1; -; mRNA.
EMBL; U49126; AAB61634.1; -; mRNA.
EMBL; U49127; AAB61635.1; -; mRNA.
EMBL; U49128; AAB61636.1; -; mRNA.
PIR; JH0422; JH0422.
PIR; T42742; T42742.
RefSeq; NP_058994.1; NM_017298.1. [P27732-1]
UniGene; Rn.89671; -.
ProteinModelPortal; P27732; -.
SMR; P27732; -.
DIP; DIP-60740N; -.
IntAct; P27732; 2.
MINT; MINT-7965882; -.
STRING; 10116.ENSRNOP00000051407; -.
BindingDB; P27732; -.
ChEMBL; CHEMBL4132; -.
GuidetoPHARMACOLOGY; 530; -.
TCDB; 1.A.1.11.1; the voltage-gated ion channel (vic) superfamily.
iPTMnet; P27732; -.
PhosphoSitePlus; P27732; -.
PaxDb; P27732; -.
PRIDE; P27732; -.
GeneID; 29716; -.
KEGG; rno:29716; -.
CTD; 776; -.
RGD; 70973; Cacna1d.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOVERGEN; HBG050763; -.
InParanoid; P27732; -.
KO; K04851; -.
PhylomeDB; P27732; -.
Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
PRO; PR:P27732; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0032590; C:dendrite membrane; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0005891; C:voltage-gated calcium channel complex; IC:RGD.
GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0070509; P:calcium ion import; IMP:RGD.
GO; GO:0006816; P:calcium ion transport; IDA:BHF-UCL.
GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
GO; GO:0070838; P:divalent metal ion transport; IMP:RGD.
GO; GO:0007507; P:heart development; IEP:RGD.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IMP:RGD.
GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR005452; LVDCC_a1dsu.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF239; PTHR10037:SF239; 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; PR01636; LVDCCALPHA1D.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
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 2203 Voltage-dependent L-type calcium channel
subunit alpha-1D.
/FTId=PRO_0000053936.
TOPO_DOM 1 126 Cytoplasmic. {ECO:0000255}.
TRANSMEM 127 145 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 146 163 Extracellular. {ECO:0000255}.
TRANSMEM 164 183 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 184 195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 196 214 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 215 235 Extracellular. {ECO:0000255}.
TRANSMEM 236 254 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 255 273 Cytoplasmic. {ECO:0000255}.
TRANSMEM 274 293 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 294 381 Extracellular. {ECO:0000255}.
TRANSMEM 382 406 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 407 582 Cytoplasmic. {ECO:0000255}.
TRANSMEM 583 602 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 603 617 Extracellular. {ECO:0000255}.
TRANSMEM 618 636 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 637 644 Cytoplasmic. {ECO:0000255}.
TRANSMEM 645 663 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 664 673 Extracellular. {ECO:0000255}.
TRANSMEM 674 692 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 693 711 Cytoplasmic. {ECO:0000255}.
TRANSMEM 712 732 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 733 786 Extracellular. {ECO:0000255}.
TRANSMEM 787 811 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 812 945 Cytoplasmic. {ECO:0000255}.
TRANSMEM 946 964 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 965 980 Extracellular. {ECO:0000255}.
TRANSMEM 981 1000 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1001 1012 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1013 1031 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1032 1037 Extracellular. {ECO:0000255}.
TRANSMEM 1038 1057 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1058 1076 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1077 1096 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1097 1186 Extracellular. {ECO:0000255}.
TRANSMEM 1187 1207 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1208 1264 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1265 1283 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1284 1298 Extracellular. {ECO:0000255}.
TRANSMEM 1299 1318 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1319 1325 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1326 1347 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1348 1357 Extracellular. {ECO:0000255}.
TRANSMEM 1358 1377 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1378 1396 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1397 1416 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1417 1483 Extracellular. {ECO:0000255}.
TRANSMEM 1484 1508 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1509 2203 Cytoplasmic. {ECO:0000255}.
REPEAT 112 408 I.
REPEAT 528 774 II.
REPEAT 892 1174 III.
REPEAT 1211 1486 IV.
CA_BIND 1537 1548 {ECO:0000255}.
REGION 429 446 Binding to the beta subunit.
{ECO:0000250}.
REGION 1134 1224 Dihydropyridine binding. {ECO:0000250}.
REGION 1464 1530 Dihydropyridine binding. {ECO:0000250}.
REGION 1476 1519 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 1 7 Poly-Met.
COMPBIAS 712 718 Poly-Leu.
COMPBIAS 886 897 Poly-Glu.
SITE 364 364 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 763 763 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1160 1160 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1450 1450 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 1519 1519 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 481 492 Missing (in isoform 8).
{ECO:0000303|PubMed:1648940}.
/FTId=VSP_000916.
VAR_SEQ 493 512 Missing (in isoform 7).
{ECO:0000303|PubMed:1648940}.
/FTId=VSP_000917.
VAR_SEQ 1322 1392 Missing (in isoform 9).
{ECO:0000303|PubMed:9232351}.
/FTId=VSP_000918.
VAR_SEQ 1322 1349 Missing (in isoform 4 and isoform 10).
{ECO:0000303|PubMed:1279681,
ECO:0000303|PubMed:9232351}.
/FTId=VSP_000919.
VAR_SEQ 1322 1348 GYFSDAWNTFDSLIVIGSIIDVALSEA -> HYFTDAWNTF
DALIVVGSVVDIAITEVN (in isoform 6).
{ECO:0000303|PubMed:1648940}.
/FTId=VSP_000920.
VAR_SEQ 1349 1349 D -> DPSDSENIPLPTATPG (in isoform 6 and
isoform 3). {ECO:0000303|PubMed:1648940,
ECO:0000303|PubMed:9232351}.
/FTId=VSP_000921.
VAR_SEQ 1354 1368 Missing (in isoform 10 and isoform 5).
{ECO:0000303|PubMed:9232351}.
/FTId=VSP_000922.
VAR_SEQ 1642 1668 DDEVTVGKFYATFLIQDYFRKFKKRKE -> GNSRSGKSKA
WWGNTLRRTPRSPYRRD (in isoform 2).
{ECO:0000303|PubMed:7760845}.
/FTId=VSP_000923.
VAR_SEQ 1669 2203 Missing (in isoform 2).
{ECO:0000303|PubMed:7760845}.
/FTId=VSP_000924.
VAR_SEQ 1686 1691 AGLRTL -> MLERML (in isoform 13).
{ECO:0000303|PubMed:1648940}.
/FTId=VSP_000925.
VAR_SEQ 1692 2203 Missing (in isoform 13).
{ECO:0000303|PubMed:1648940}.
/FTId=VSP_000926.
MUTAGEN 1656 1657 IQ->AA: Loss of calcium-dependent
inactivation related to the C-terminal
lobe of calmodulin.
{ECO:0000269|PubMed:17050707}.
CONFLICT 124 124 D -> N (in Ref. 2; AAA42015).
{ECO:0000305}.
CONFLICT 183 183 S -> Y (in Ref. 2; AAA42015).
{ECO:0000305}.
CONFLICT 192 192 S -> Y (in Ref. 2; AAA42015).
{ECO:0000305}.
CONFLICT 513 513 G -> C (in Ref. 2). {ECO:0000305}.
CONFLICT 522 560 Missing (in Ref. 2). {ECO:0000305}.
CONFLICT 1452 1452 W -> R (in Ref. 5; AAA89156).
{ECO:0000305}.
SEQUENCE 2203 AA; 250136 MW; 8E746A8D988050C6 CRC64;
MMMMMMMKKM QHQRQQQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
SIVDWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
IASGLLLHPN ASVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
CFFADSDIVA EEDPAPCAFS GNGRQCAANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
GEGETQGCCG SLWCWWKRRG AAKTGPSGCR RWGQAISKSK LRSHGAREAL CVCRCSLESL
VKLWTSRFSA HLQAAYVRPY SRRWRRWNRF NRRRCRAAVK SVTFYWLVIV LVFLNTLTIS
SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD CFVVCGGITE
TILVELELMS PLGVSVFRCV RLLRIFKVTR HWTSLSNLVA SLLNSMKSIA SLLLLLFLFI
IIFSLLGMQL FGGKFNFDET QTKRSTFDNF PQALLTVFQI LTGEDWNAVM YDGIMAYGGP
SSSGMIVCIY FIILFICGNY ILLKLFLAIA VDNLADAESL NTAQKEEAEE KERKKIARKE
SLENKKNNKP EVNQIANSDN KVTIDDYQEE AEDKDPYPPC DVPVGEEEEE EEEDEPEVPA
GPRPRRISEL NMKEKIAPIP EGSAFFILSK TNPIRVGCHK LINHHIFTNL ILVFIMLSSA
ALAAEDPIRS HSFRNTILGY FDYAFTAIFT VEILLKMTTF GAFLHKGAFC RNYFNLLDML
VVGVSLVSFG IQSSAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIMIV
TTLLQFMFAC IGVQLFKGKF YRCTDEAKSN PEECRGLFIL YKDGDVDSPV VRERIWQNSD
FNFDNVLSAM MALFTVSTFE GWPALLYKAI DSNGENVGPV YNYRVEISIF FIIYIIIVAF
FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK ARPLRRYIPK NPYQYKFWYV
VNSSPFEYMM FVLIMLNTLC LAMQHYEQSK MFNDAMDILN MVFTGVFTVE MVLKVIAFKP
KGYFSDAWNT FDSLIVIGSI IDVALSEADN SEESNRISIT FFRLFRVMRL VKLLSRGEGI
RTLLWTFIKS FQALPYVALL IAMLFFIYAV IGMQMFGKVA MRDNNQINRN NNFQTFPQAV
LLLFRCATGE AWQEIMLACL PGKLCDPDSD YNPGEEYTCG SNFAIVYFIS FYMLCAFLII
NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWSEYDPEA KGRIKHLDVV TLLRRIQPPL
GFGKLCPHRV ACKRLVAMNM PLNSDGTVMF NATLFALVRT ALKIKTEGNL EQANEELRAV
IKKIWKKTSM KLLDQVVPPA GDDEVTVGKF YATFLIQDYF RKFKKRKEQG LVGKYPAKNT
TIALQAGLRT LHDIGPEIRR AISCDLQDDE PEDSKPEEED VFKRNGALLG NYVNHVNSDR
RESLQQTNTT HRPLHVQRPS IPPASDTEKP LFPPAGNSVC HNHHNHNSIG KQVPTSTNAN
LNNANMSKAA HGKRPSIGDL EHVSENGHYS YKHDRELQRR SSIKRTRYYE TYIRSESGDE
QLPTIFREDP EIHGYFRDPR CFGEQEYFSS EECCEDDSSP TWSRQNYSYY NRYPGSSMDF
ERPRGYHHPQ GFLEDDDSPI GYDSRRSPRR RLLPPTPPSH RRSSFNFECL RRQNSQDDVL
PSPALPHRAA LPLHLMQQQI MAVAGLDSSK AQKYSPSHST RSWATPPATP PYRDWTPCYT
PLIQVDRSES MDQVNGSLPS LHRSSWYTDE PDISYRTFTP ASLTVPSSFR NKNSDKQRSA
DSLVEAVLIS EGLGRYARDP KFVSATKHEI ADACDLTIDE MESAASTLLN GSVCPRANGD
MGPISHRQDY ELQDFGPGYS DEEPDPGREE EDLADEMICI TTL


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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
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
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-
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
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
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
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
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
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
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
EIAAB05027 Cacna1f,Mouse,Mus musculus,Voltage-dependent L-type calcium channel subunit alpha-1F,Voltage-gated calcium channel subunit alpha Cav1.4


 

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