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Voltage-dependent P/Q-type calcium channel subunit alpha-1A (Brain calcium channel I) (BI) (Calcium channel, L type, alpha-1 polypeptide isoform 4) (Voltage-gated calcium channel subunit alpha Cav2.1)

 CAC1A_MOUSE             Reviewed;        2368 AA.
P97445; Q2TPN3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
07-JUN-2017, entry version 165.
RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
AltName: Full=Brain calcium channel I;
Short=BI;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
Name=Cacna1a; Synonyms=Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a;
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].
STRAIN=Swiss Webster; TISSUE=Brain;
Richards K.S., Swensen A.M., Lipscombe D.;
"Molecular identity of P-type calcium current in Purkinje neurons.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-2212, AND VARIANT TG LEU-649.
STRAIN=DBA/2J;
PubMed=8929530; DOI=10.1016/S0092-8674(00)81381-1;
Fletcher C.F., Lutz C.M., O'Sullivan T.N., Shaughnessy J.D. Jr.,
Hawkes R., Frankel W.N., Copeland N.G., Jenkins N.A.;
"Absence epilepsy in tottering mutant mice is associated with calcium
channel defects.";
Cell 87:607-617(1996).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453;
SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND
SER-2071, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
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).
-!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
entry of calcium ions into excitable cells and are also involved
in a variety of calcium-dependent processes, including muscle
contraction, hormone or neurotransmitter release, gene expression,
cell motility, cell division and cell death. The isoform alpha-1A
gives rise to P and/or Q-type calcium currents. P/Q-type calcium
channels belong to the 'high-voltage activated' (HVA) group and
are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-
IVA (omega-Aga-IVA). They are however insensitive to
dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
{ECO:0000250|UniProtKB:O00555}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:O00555}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Brain specific; mainly found in the
cerebellum, olfactory bulb, cerebral cortex, hippocampus, and
inferior colliculus. In the hippocampus, expression occurs in
pyramidal and granule neurons, as well as in interneurons.
Purkinje cells contain predominantly P-type VSCC, the Q-type being
a prominent calcium current in cerebellar granule 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.
-!- DISEASE: Note=Defects in Cacna1a are the cause of a delayed-onset,
recessive neurological disorder seen in tottering (tg) mutants,
resulting in ataxia, motor seizures and behavioral absence
seizures resembling petit mal epilepsy (or absence epilepsy) in
humans. There are two more alleles, leaner (tg(lA)), that is
characterized by severe ataxia and frequent death past weaning,
but no motor seizures; and rolling Nagoya (tg(rol)), that presents
an intermediary phenotype, the ataxia being somewhat more severe
that with tg, but without motors seizures. Selective degeneration
of cerebellar Purkinje cells has been shown for all these types of
mutants. Selective degeneration of cerebellar Purkinje cells has
been shown for all these types of mutants.
{ECO:0000269|PubMed:8929530}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
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EMBL; AY714490; AAW56205.1; -; mRNA.
EMBL; U76716; AAC52940.1; -; mRNA.
CCDS; CCDS52618.1; -.
RefSeq; NP_031604.3; NM_007578.3.
UniGene; Mm.334658; -.
ProteinModelPortal; P97445; -.
BioGrid; 198430; 4.
IntAct; P97445; 1.
MINT; MINT-4997013; -.
STRING; 10090.ENSMUSP00000112436; -.
iPTMnet; P97445; -.
PhosphoSitePlus; P97445; -.
EPD; P97445; -.
MaxQB; P97445; -.
PaxDb; P97445; -.
PeptideAtlas; P97445; -.
PRIDE; P97445; -.
Ensembl; ENSMUST00000121390; ENSMUSP00000112436; ENSMUSG00000034656.
GeneID; 12286; -.
KEGG; mmu:12286; -.
UCSC; uc009mmn.2; mouse.
CTD; 773; -.
MGI; MGI:109482; Cacna1a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; P97445; -.
KO; K04344; -.
OMA; EKDCRGK; -.
OrthoDB; EOG091G0TKO; -.
PhylomeDB; P97445; -.
TreeFam; TF312805; -.
Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-MMU-422356; Regulation of insulin secretion.
ChiTaRS; Cacna1a; mouse.
PRO; PR:P97445; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000034656; -.
ExpressionAtlas; P97445; baseline and differential.
Genevisible; P97445; MM.
GO; GO:0042995; C:cell projection; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019905; F:syntaxin binding; ISO:MGI.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
GO; GO:0017156; P:calcium ion regulated exocytosis; IMP:MGI.
GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:MGI.
GO; GO:0008219; P:cell death; ISO:MGI.
GO; GO:0016049; P:cell growth; IMP:MGI.
GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:MGI.
GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
GO; GO:0021679; P:cerebellar molecular layer development; IMP:MGI.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
GO; GO:0021590; P:cerebellum maturation; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0051899; P:membrane depolarization; IMP:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; IMP:MGI.
GO; GO:0032353; P:negative regulation of hormone biosynthetic process; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0050877; P:neurological system process; IMP:MGI.
GO; GO:0050905; P:neuromuscular process; IMP:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
GO; GO:0043113; P:receptor clustering; IMP:MGI.
GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; IMP:MGI.
GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IDA:MGI.
GO; GO:0010817; P:regulation of hormone levels; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0001505; P:regulation of neurotransmitter levels; IMP:MGI.
GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IMP:MGI.
GO; GO:0048265; P:response to pain; IMP:MGI.
GO; GO:0060024; P:rhythmic synaptic transmission; IMP:MGI.
GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
GO; GO:0007416; P:synapse assembly; IMP:MGI.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
GO; GO:0021750; P:vestibular nucleus development; IMP:MGI.
InterPro; IPR005448; CACNA1A.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF249; PTHR10037:SF249; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01632; PQVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Calcium; Calcium channel; Calcium transport; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
CHAIN 1 2368 Voltage-dependent P/Q-type calcium
channel subunit alpha-1A.
/FTId=PRO_0000053917.
TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.
TRANSMEM 101 119 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 120 138 Extracellular. {ECO:0000255}.
TRANSMEM 139 156 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 157 168 Cytoplasmic. {ECO:0000255}.
TRANSMEM 169 184 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 185 192 Extracellular. {ECO:0000255}.
TRANSMEM 193 211 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 212 230 Cytoplasmic. {ECO:0000255}.
TRANSMEM 231 250 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 251 337 Extracellular. {ECO:0000255}.
TRANSMEM 338 362 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 363 489 Cytoplasmic. {ECO:0000255}.
TRANSMEM 490 509 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 510 523 Extracellular. {ECO:0000255}.
TRANSMEM 524 543 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 544 551 Cytoplasmic. {ECO:0000255}.
TRANSMEM 552 570 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 571 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 599 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 600 618 Cytoplasmic. {ECO:0000255}.
TRANSMEM 619 638 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 639 691 Extracellular. {ECO:0000255}.
TRANSMEM 692 716 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 717 1190 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1191 1214 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1215 1231 Extracellular. {ECO:0000255}.
TRANSMEM 1232 1251 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1252 1258 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1259 1282 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1283 1293 Extracellular. {ECO:0000255}.
TRANSMEM 1294 1311 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1312 1330 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1331 1350 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1351 1437 Extracellular. {ECO:0000255}.
TRANSMEM 1438 1462 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1463 1518 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1519 1537 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1538 1551 Extracellular. {ECO:0000255}.
TRANSMEM 1552 1573 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1574 1580 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1581 1600 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1601 1607 Extracellular. {ECO:0000255}.
TRANSMEM 1608 1626 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1627 1645 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1646 1665 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1666 1737 Extracellular. {ECO:0000255}.
TRANSMEM 1738 1763 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1764 2368 Cytoplasmic. {ECO:0000255}.
REPEAT 65 365 I.
REPEAT 475 719 II.
REPEAT 1182 1465 III.
REPEAT 1502 1765 IV.
CA_BIND 1791 1802 {ECO:0000250}.
REGION 385 402 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 729 734 Poly-Glu.
COMPBIAS 1155 1158 Poly-Glu.
SITE 320 320 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 670 670 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1411 1411 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1600 1600 Binds to omega-Aga-IVA. {ECO:0000250}.
SITE 1707 1707 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 411 411 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 792 792 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1051 1051 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1935 1935 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1998 1998 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2016 2016 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2028 2028 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2030 2030 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2071 2071 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2091 2091 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1607 1607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 649 649 P -> L (in tg).
{ECO:0000269|PubMed:8929530}.
CONFLICT 79 79 S -> P (in Ref. 2; AAC52940).
{ECO:0000305}.
CONFLICT 82 82 L -> F (in Ref. 2; AAC52940).
{ECO:0000305}.
CONFLICT 884 884 P -> L (in Ref. 2; AAC52940).
{ECO:0000305}.
CONFLICT 888 888 E -> D (in Ref. 1; AAW56205).
{ECO:0000305}.
CONFLICT 1083 1083 N -> D (in Ref. 2; AAC52940).
{ECO:0000305}.
CONFLICT 1349 1349 L -> F (in Ref. 2; AAC52940).
{ECO:0000305}.
CONFLICT 1373 1373 L -> F (in Ref. 2; AAC52940).
{ECO:0000305}.
CONFLICT 2161 2161 P -> PH (in Ref. 1; AAW56205).
{ECO:0000305}.
SEQUENCE 2368 AA; 267647 MW; E7B573BA005E5CB1 CRC64;
MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART
MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE
QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL
TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL
IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV
LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD
GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF
YIRRMVKTQA FYWTVLSLVA LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM
YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI
MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA
NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR
TSEMRKQNLL ASREALYGDA AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR
APEALRPTAR PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA
DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE
GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP NLSTTRPIQQ DLGRQDLPLA
EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN
PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN
ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF
RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC
VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV
KARDREWKKY EFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI
FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF
SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI
KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED
EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF
YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI
AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS
KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AHEGGMKESP
SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT
RAASMPRLPA ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR
PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS PSEGREHTTH RQGSSSVSGS
PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA
PRWPAHAPEG PRPRGADYTE PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY
YAGHGAPRPR TARRGAHDAY SESEDDWC


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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
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
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
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
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
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
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
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
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
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
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
E1344Rb ELISA kit 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 subuni 96T
E1344m ELISA kit 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 su 96T
E1344c ELISA CACNA1A,CHCACHA1A,Chicken,Gallus gallus,Voltage-dependent P_Q-type calcium channel subunit alpha-1A,Voltage-gated calcium channel subunit alpha Cav2.1 96T


 

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