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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_RABIT             Reviewed;        2424 AA.
P27884; P27883;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
30-AUG-2017, entry version 131.
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=CACH4, CACN3, CACNL1A4;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1849233; DOI=10.1038/350398a0;
Mori Y., Friedrich T., Kim M.-S., Mikami A., Nakai J., Ruth P.,
Bosse E., Hofmann F., Flockerzi V., Furuichi T., Mikoshiba K.,
Imoto K., Tanabe T., Numa S.;
"Primary structure and functional expression from complementary DNA of
a brain calcium channel.";
Nature 350:398-402(1991).
[2]
BETA-SUBUNIT BINDING DOMAIN, AND MUTAGENESIS OF GLU-386; LEU-389;
TYR-392 AND GLU-400.
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).
[3]
FUNCTION, AND MUTAGENESIS OF GLU-188 AND GLU-1658.
PubMed=11055992; DOI=10.1085/jgp.116.5.637;
Winterfield J.R., Swartz K.J.;
"A hot spot for the interaction of gating modifier toxins with
voltage-dependent ion channels.";
J. Gen. Physiol. 116:637-644(2000).
-!- 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:0000269|PubMed:11055992}.
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=BI-2; Synonyms=1A-2;
IsoId=P27884-1; Sequence=Displayed;
Name=BI-1; Synonyms=1A-1;
IsoId=P27884-2; Sequence=VSP_000879, VSP_000880;
Name=CBP101; Synonyms=CBP109;
IsoId=P27884-3; Sequence=VSP_000878;
Name=CBP103;
IsoId=P27884-4; Sequence=VSP_000877;
Name=CBP107;
IsoId=P27884-5; Sequence=VSP_000876;
-!- TISSUE SPECIFICITY: Brain specific. 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
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EMBL; X57477; CAA40715.1; -; mRNA.
EMBL; X57689; CAA40872.1; -; mRNA.
EMBL; X57476; CAA40714.1; -; mRNA.
EMBL; X57688; CAA40871.1; -; mRNA.
PIR; I46477; I46477.
PIR; I46480; I46480.
RefSeq; NP_001095163.1; NM_001101693.1. [P27884-2]
UniGene; Ocu.2123; -.
PDB; 3DVM; X-ray; 2.60 A; B=1963-1982.
PDBsum; 3DVM; -.
ProteinModelPortal; P27884; -.
SMR; P27884; -.
DIP; DIP-29591N; -.
PRIDE; P27884; -.
GeneID; 100009265; -.
KEGG; ocu:100009265; -.
CTD; 773; -.
HOVERGEN; HBG050763; -.
InParanoid; P27884; -.
KO; K04344; -.
EvolutionaryTrace; P27884; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IEA:GOC.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
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;
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 2424 Voltage-dependent P/Q-type calcium
channel subunit alpha-1A.
/FTId=PRO_0000053918.
TOPO_DOM 1 98 Cytoplasmic. {ECO:0000255}.
TRANSMEM 99 117 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 118 135 Extracellular. {ECO:0000255}.
TRANSMEM 136 155 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 156 167 Cytoplasmic. {ECO:0000255}.
TRANSMEM 168 185 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 186 190 Extracellular. {ECO:0000255}.
TRANSMEM 191 209 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 210 228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 229 248 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 249 335 Extracellular. {ECO:0000255}.
TRANSMEM 336 360 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 361 487 Cytoplasmic. {ECO:0000255}.
TRANSMEM 488 506 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 507 521 Extracellular. {ECO:0000255}.
TRANSMEM 522 541 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 542 549 Cytoplasmic. {ECO:0000255}.
TRANSMEM 550 568 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 569 578 Extracellular. {ECO:0000255}.
TRANSMEM 579 597 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 598 616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 617 636 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 637 689 Extracellular. {ECO:0000255}.
TRANSMEM 690 714 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 715 1253 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1254 1272 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1273 1288 Extracellular. {ECO:0000255}.
TRANSMEM 1289 1308 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1309 1320 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1321 1339 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1340 1350 Extracellular. {ECO:0000255}.
TRANSMEM 1351 1369 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1370 1388 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1389 1408 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1409 1495 Extracellular. {ECO:0000255}.
TRANSMEM 1496 1520 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1521 1575 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1576 1604 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1605 1609 Extracellular. {ECO:0000255}.
TRANSMEM 1610 1629 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1630 1637 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1638 1656 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1657 1665 Extracellular. {ECO:0000255}.
TRANSMEM 1666 1684 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1685 1703 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1704 1723 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1724 1795 Extracellular. {ECO:0000255}.
TRANSMEM 1796 1820 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1821 2424 Cytoplasmic. {ECO:0000255}.
REPEAT 85 363 I.
REPEAT 473 717 II.
REPEAT 1240 1523 III.
REPEAT 1560 1823 IV.
CA_BIND 1849 1860 {ECO:0000250}.
REGION 383 400 Binding to the beta subunit.
COMPBIAS 13 18 Poly-Gly.
COMPBIAS 727 732 Poly-Glu.
COMPBIAS 1004 1010 Poly-Gly.
COMPBIAS 1012 1017 Poly-Arg.
COMPBIAS 2219 2227 Poly-His.
COMPBIAS 2242 2246 Poly-Arg.
COMPBIAS 2288 2297 Poly-Arg.
COMPBIAS 2298 2301 Poly-Gly.
COMPBIAS 2372 2377 Poly-Pro.
COMPBIAS 2411 2416 Poly-Gly.
SITE 318 318 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 668 668 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1469 1469 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1658 1658 Binds to omega-Aga-IVA.
SITE 1765 1765 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 409 409 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1104 1104 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1831 1831 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1993 1993 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2054 2054 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2072 2072 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2084 2084 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2086 2086 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
MOD_RES 2127 2127 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2148 2148 Phosphoserine.
{ECO:0000250|UniProtKB:P54282}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1665 1665 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 772 1120 Missing (in isoform CBP103).
{ECO:0000305}.
/FTId=VSP_000877.
VAR_SEQ 772 1051 Missing (in isoform CBP107).
{ECO:0000305}.
/FTId=VSP_000876.
VAR_SEQ 1857 1884 LYRDMYAMLRHMPPPLGLGKNCPARVAY -> HYKDMYSLL
RVISPPLGLGKKCPHRVAC (in isoform CBP101).
{ECO:0000305}.
/FTId=VSP_000878.
VAR_SEQ 2230 2273 RGPGRVSPGVSARRRRRGPVARVRPARAPALAHARARARAP
ARL -> PAAADKERYGPQDRPDHGHGRARARDQRWSRSPS
EGREHTTHRQ (in isoform BI-1).
{ECO:0000305}.
/FTId=VSP_000879.
VAR_SEQ 2274 2424 Missing (in isoform BI-1). {ECO:0000305}.
/FTId=VSP_000880.
VARIANT 419 419 Missing (in isoform CBP315).
VARIANT 877 877 A -> T (in isoform CBS).
VARIANT 1104 1104 S -> N (in isoform CBS).
MUTAGEN 188 188 E->K: No change in inhibition by omega-
Aga-IVA. {ECO:0000269|PubMed:11055992}.
MUTAGEN 386 386 E->S: Reduced beta-subunit interaction.
{ECO:0000269|PubMed:7509046}.
MUTAGEN 389 389 L->H: Reduced beta-subunit interaction.
{ECO:0000269|PubMed:7509046}.
MUTAGEN 392 392 Y->S: Reduced beta-subunit interaction.
{ECO:0000269|PubMed:7509046}.
MUTAGEN 400 400 E->A: No effect on beta-subunit
interaction.
{ECO:0000269|PubMed:7509046}.
MUTAGEN 1658 1658 E->K: Loss of inhibition by omega-Aga-
IVA. {ECO:0000269|PubMed:11055992}.
HELIX 1963 1979 {ECO:0000244|PDB:3DVM}.
SEQUENCE 2424 AA; 273231 MW; F7CC4D0AB4B45604 CRC64;
MARFGDEMPA RYGGGGAGAA AGVVVGAAGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA
LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH
LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG
ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF
AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTRCQPY WEGPNNGITQ
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS
GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD VEQRHPFDGA
LRRATIKKSK TDLLHPEEAE DQLADIASVG SPFARASIKS AKLENSSFFH KKERRMRFYI
RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG
LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT
VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA
QELTKDEQEE EEAVNQKLAL QKAKEVAEVS PLSAANMSIA MKEQQKNQKP AKSVWEQRTS
EMRKQNLLAS REALYSEMDP EERWKASYAR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR
VAEPTVDQRL GQQRAEDFLR KQARHHDRAR DPSAHAAAGL DARRPWAGSQ EAELSREGPY
GRESDHQARE GGLEPPGFWE GEAERGKAGD PHRRHAHRQG VGGSGGSRSG SPRTGTADGE
PRRHRVHRRP GEDGPDDKAE RRGRHREGSR PARSGEGEAE GPDGGGGGGG ERRRRHRHGP
PPAYDPDARR DDRERRHRRR KDTQGSGVPV SGPNLSTTRP IQQDLSRQEP PLAEDMDNLK
NSRLATAEPV SPHENLSHAG LPQSPAKMGS STDPAGPTPA TAANPQNSTA SRRTPNNPGN
PSNPGPPKTP ENSLIVTNPS TAQTNSAKTA RKPDHTTVEI PPACPPPLNH TVVQVNKNAN
PDPLPKKEDE KKEEVDEGPG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL NLRYFEMCIL
MVIAMSSIAL AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE MVIKMIDLGL VLHQGAYFRD
LWNILDFIVV SGALVAFAFT GNSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV
NSLKNVFNIL IVYMLFMFIF AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA
RDREWKKYEF HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY
VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA KPLTRHMPQN
KQSFQYRMWQ FVVSPPFEYT IMAMIALNTI VLMMKFYGAS VAYDNALKVF NIVFTSLFSL
ECLLKVLAFG ILNYFRDAWN IFDFVTVLGS ITDILVTEFG NNFINLSFLR LFRAARLIKL
LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIGIDM EDEDSDEDEF
QITEHNNFRT FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTPE CGNEFAYFYF
VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP AAWGRMLYRD
MYAMLRHMPP PLGLGKNCPA RVAYKRLLRM DLPVADDNTV HFNSTLMALI RTALDIKIAK
GGADKQQMDA ELRKEMMAIW PNLSQKTLDL LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA
KKLQAMREEQ NRTPLMFQRM EPPPDEGGAG QNALPSTQLD PAGGLMAHED GLKDSPSWVT
QRAQEMFQKT GTWSPERAPP ADMADSQPKP QSVEMREMSQ DGYSDSEHCL PMEGQARAAS
MPRLPAENQR RRGRPRGSDL STICDTSPMK RSASVLGPKA SRRLDDYSLE RVPPEENQRH
HPRRRERAHR TSERSLGRYT DVDTGLGTDL SMTTQSGDLP SREREQERGR PKDRKHRPHH
HHHHHHHPGR GPGRVSPGVS ARRRRRGPVA RVRPARAPAL AHARARARAP ARLLPELRLR
RARRPRPRQR RRPRRRRGGG GRALRRAPGP REPLAQDSPG RGPSVCLARA ARPAGPQRLL
PGPRTGQAPR ARLPQKPARS VQRERRGLVL SPPPPPPGEL APRAHPARTP RPGPGDSRSR
RGGRRWTASA GKGGGGPRAS APSP


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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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