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Voltage-dependent calcium channel subunit alpha-2/delta-4 (Voltage-gated calcium channel subunit alpha-2/delta-4) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-4; Voltage-dependent calcium channel subunit delta-4]

 CA2D4_HUMAN             Reviewed;        1137 AA.
Q7Z3S7; Q7Z3S8; Q86XZ5; Q8IZS9;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
05-DEC-2018, entry version 120.
RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-4;
AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-4;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit alpha-2-4;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit delta-4;
Flags: Precursor;
Name=CACNA2D4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4; 5 AND 6), FUNCTION, TISSUE
SPECIFICITY, LACK OF GABAPENTIN-BINDING, INTERACTION WITH CACNA1C AND
CACNB3, AND VARIANT VAL-327.
PubMed=12181424; DOI=10.1124/mol.62.3.485;
Qin N., Yagel S., Momplaisir M.-L., Codd E.E., D'Andrea M.R.;
"Molecular cloning and characterization of the human voltage-gated
calcium channel alpha(2)delta-4 subunit.";
Mol. Pharmacol. 62:485-496(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
VAL-327.
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INVOLVEMENT IN RCD4.
PubMed=17033974; DOI=10.1086/508944;
Wycisk K.A., Zeitz C., Feil S., Wittmer M., Forster U., Neidhardt J.,
Wissinger B., Zrenner E., Wilke R., Kohl S., Berger W.;
"Mutation in the auxiliary calcium-channel subunit CACNA2D4 causes
autosomal recessive cone dystrophy.";
Am. J. Hum. Genet. 79:973-977(2006).
-!- FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium
channels regulates calcium current density and
activation/inactivation kinetics of the calcium channel.
{ECO:0000269|PubMed:12181424}.
-!- SUBUNIT: Dimer formed of alpha-2-2 and delta-2 chains; disulfide-
linked. Voltage-dependent calcium channels are multisubunit
complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta
(CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio
(Probable). Interacts with CACNA1C and CACNB3.
{ECO:0000269|PubMed:12181424, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Alpha2delta-4a;
IsoId=Q7Z3S7-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z3S7-2; Sequence=VSP_028070;
Note=No experimental confirmation available. May be due to an
intron retention.;
Name=4; Synonyms=Alpha2delta-4b;
IsoId=Q7Z3S7-4; Sequence=VSP_028069;
Name=5; Synonyms=Alpha2delta-4c;
IsoId=Q7Z3S7-5; Sequence=VSP_028071;
Name=6; Synonyms=Alpha2delta-4d;
IsoId=Q7Z3S7-6; Sequence=VSP_028069, VSP_028071;
Name=7;
IsoId=Q7Z3S7-7; Sequence=VSP_044107, VSP_044108, VSP_044109,
VSP_044110;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Predominantly expressed in certain types of
endocrine cells. Present in the Paneth cells of the small
intestine. Also present in the erythroblasts in the fetal liver,
in the cells of the zona reticularis of the adrenal gland and in
the basophils of the pituitary. Present at low level in some brain
regions such as the cerebellum (at protein level).
{ECO:0000269|PubMed:12181424}.
-!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent
metal cations and is required to promote trafficking of the alpha-
1 (CACNA1) subunit to the plasma membrane by an integrin-like
switch. {ECO:0000250}.
-!- PTM: May be proteolytically processed into subunits alpha-2-4 and
delta-4 that are disulfide-linked. It is however unclear whether
such cleavage really takes place in vivo and has a functional role
(By similarity). {ECO:0000250}.
-!- DISEASE: Retinal cone dystrophy 4 (RCD4) [MIM:610478]:
Characterized by minimal symptoms except for slowly progressive
reduction in visual acuity. {ECO:0000269|PubMed:17033974}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: In contrast to CACNA2D1 and CACNA2D2, it does not
bind gabapentin, an antiepileptic drug.
-!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH48288.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
Sequence=AAN06672.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF516695; AAN06672.1; ALT_INIT; mRNA.
EMBL; BX537436; CAD97678.1; -; mRNA.
EMBL; BX537437; CAD97679.1; -; mRNA.
EMBL; AC005342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC048288; AAH48288.1; ALT_SEQ; mRNA.
CCDS; CCDS44785.1; -. [Q7Z3S7-1]
RefSeq; NP_758952.4; NM_172364.4. [Q7Z3S7-1]
UniGene; Hs.13768; -.
ProteinModelPortal; Q7Z3S7; -.
STRING; 9606.ENSP00000372169; -.
ChEMBL; CHEMBL2363032; -.
TCDB; 8.A.18.4.1; the ca(2+) channel auxiliary subunit Alpha2Delta types 1-4 (cca-Alpha2Delta) family.
iPTMnet; Q7Z3S7; -.
PhosphoSitePlus; Q7Z3S7; -.
BioMuta; CACNA2D4; -.
DMDM; 296434419; -.
PaxDb; Q7Z3S7; -.
PeptideAtlas; Q7Z3S7; -.
PRIDE; Q7Z3S7; -.
ProteomicsDB; 69073; -.
ProteomicsDB; 69074; -. [Q7Z3S7-2]
ProteomicsDB; 69076; -. [Q7Z3S7-4]
ProteomicsDB; 69077; -. [Q7Z3S7-5]
ProteomicsDB; 69078; -. [Q7Z3S7-6]
DNASU; 93589; -.
Ensembl; ENST00000382722; ENSP00000372169; ENSG00000151062. [Q7Z3S7-1]
Ensembl; ENST00000545595; ENSP00000442329; ENSG00000151062. [Q7Z3S7-7]
Ensembl; ENST00000585708; ENSP00000467697; ENSG00000151062. [Q7Z3S7-6]
Ensembl; ENST00000586184; ENSP00000465060; ENSG00000151062. [Q7Z3S7-5]
Ensembl; ENST00000588077; ENSP00000468530; ENSG00000151062. [Q7Z3S7-4]
Ensembl; ENST00000642910; ENSP00000494565; ENSG00000284953. [Q7Z3S7-6]
Ensembl; ENST00000644981; ENSP00000494395; ENSG00000284953. [Q7Z3S7-5]
Ensembl; ENST00000645018; ENSP00000495256; ENSG00000284953. [Q7Z3S7-1]
Ensembl; ENST00000645225; ENSP00000493490; ENSG00000284953. [Q7Z3S7-4]
Ensembl; ENST00000646498; ENSP00000494913; ENSG00000284953. [Q7Z3S7-7]
GeneID; 93589; -.
KEGG; hsa:93589; -.
UCSC; uc058jsm.1; human. [Q7Z3S7-1]
CTD; 93589; -.
DisGeNET; 93589; -.
EuPathDB; HostDB:ENSG00000151062.14; -.
GeneCards; CACNA2D4; -.
H-InvDB; HIX0010321; -.
H-InvDB; HIX0171624; -.
HGNC; HGNC:20202; CACNA2D4.
HPA; HPA031952; -.
MalaCards; CACNA2D4; -.
MIM; 608171; gene.
MIM; 610478; phenotype.
neXtProt; NX_Q7Z3S7; -.
OpenTargets; ENSG00000151062; -.
Orphanet; 1872; Cone rod dystrophy.
Orphanet; 215; Congenital stationary night blindness.
PharmGKB; PA130546913; -.
eggNOG; KOG2353; Eukaryota.
eggNOG; ENOG410XPDX; LUCA.
GeneTree; ENSGT00940000155997; -.
HOGENOM; HOG000010247; -.
HOVERGEN; HBG107124; -.
InParanoid; Q7Z3S7; -.
KO; K04861; -.
OMA; ANEWTYC; -.
OrthoDB; EOG091G00UY; -.
PhylomeDB; Q7Z3S7; -.
TreeFam; TF315824; -.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
ChiTaRS; CACNA2D4; human.
GenomeRNAi; 93589; -.
PRO; PR:Q7Z3S7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000151062; Expressed in 115 organ(s), highest expression level in blood.
CleanEx; HS_CACNA2D4; -.
ExpressionAtlas; Q7Z3S7; baseline and differential.
Genevisible; Q7Z3S7; HS.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013680; VDCC_a2/dsu.
InterPro; IPR013608; VWA_N.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF08473; VGCC_alpha2; 1.
Pfam; PF13768; VWA_3; 1.
Pfam; PF08399; VWA_N; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50234; VWFA; 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; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1137 Voltage-dependent calcium channel subunit
alpha-2/delta-4.
/FTId=PRO_0000304655.
CHAIN 20 991 Voltage-dependent calcium channel subunit
alpha-2-4. {ECO:0000255}.
/FTId=PRO_0000304656.
CHAIN 992 1137 Voltage-dependent calcium channel subunit
delta-4. {ECO:0000255}.
/FTId=PRO_0000304657.
TOPO_DOM 20 1115 Extracellular. {ECO:0000255}.
TRANSMEM 1116 1136 Helical. {ECO:0000255}.
TOPO_DOM 1137 1137 Cytoplasmic. {ECO:0000255}.
DOMAIN 291 473 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 487 580 Cache.
MOTIF 297 301 MIDAS-like motif.
METAL 297 297 Divalent metal cation. {ECO:0000250}.
METAL 299 299 Divalent metal cation. {ECO:0000250}.
METAL 301 301 Divalent metal cation. {ECO:0000250}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 664 664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 447 1097 Interchain (between alpha-2-4 and delta-4
chains). {ECO:0000250}.
VAR_SEQ 1 855 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044107.
VAR_SEQ 1 76 MVCGCSALLPLPNPRPTMPATPNFLANPSSSSRWIPLQPMP
VAWAFVQKTSALLWLLLLGTSLSPAWGQAKIPLET -> MA
VALGTRRRDR (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:12181424}.
/FTId=VSP_028069.
VAR_SEQ 872 886 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044108.
VAR_SEQ 908 911 TGRF -> SDYV (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044109.
VAR_SEQ 912 1137 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044110.
VAR_SEQ 975 1137 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_028070.
VAR_SEQ 1104 1137 ENAQDCGGASDTSASPPLLLLPVCAWGLLPQLLR -> VRV
EADRGWAGFSSPNPLCLGLCPCRQEHIGMPMNTPVPVLLGG
NIRVYAL (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:12181424}.
/FTId=VSP_028071.
VARIANT 327 327 I -> V (in dbSNP:rs10735005).
{ECO:0000269|PubMed:12181424,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_035049.
VARIANT 863 863 R -> H (in dbSNP:rs36077411).
/FTId=VAR_035050.
VARIANT 869 869 T -> M (in dbSNP:rs35331095).
/FTId=VAR_035051.
CONFLICT 368 368 K -> N (in Ref. 2; CAD97678).
{ECO:0000305}.
CONFLICT 650 650 V -> A (in Ref. 1; AAN06672).
{ECO:0000305}.
CONFLICT 710 710 T -> A (in Ref. 2; CAD97679).
{ECO:0000305}.
CONFLICT 879 879 C -> Y (in Ref. 1; AAN06672).
{ECO:0000305}.
CONFLICT 1034 1034 G -> E (in Ref. 2; CAD97679).
{ECO:0000305}.
SEQUENCE 1137 AA; 127938 MW; BF7FD169E1AF34F7 CRC64;
MVCGCSALLP LPNPRPTMPA TPNFLANPSS SSRWIPLQPM PVAWAFVQKT SALLWLLLLG
TSLSPAWGQA KIPLETVKLW ADTFGGDLYN TVTKYSGSLL LQKKYKDVES SLKIEEVDGL
ELVRKFSEDM ENMLRRKVEA VQNLVEAAEE ADLNHEFNES LVFDYYNSVL INERDEKGNF
VELGAEFLLE SNAHFSNLPV NTSISSVQLP TNVYNKDPDI LNGVYMSEAL NAVFVENFQR
DPTLTWQYFG SATGFFRIYP GIKWTPDENG VITFDCRNRG WYIQAATSPK DIVILVDVSG
SMKGLRMTIA KHTITTILDT LGENDFINII AYNDYVHYIE PCFKGILVQA DRDNREHFKL
LVEELMVKGV GVVDQALREA FQILKQFQEA KQGSLCNQAI MLISDGAVED YEPVFEKYNW
PDCKVRVFTY LIGREVSFAD RMKWIACNNK GYYTQISTLA DTQENVMEYL HVLSRPMVIN
HDHDIIWTEA YMDSKLLSSQ AQSLTLLTTV AMPVFSKKNE TRSHGILLGV VGSDVALREL
MKLAPRYKLG VHGYAFLNTN NGYILSHPDL RPLYREGKKL KPKPNYNSVD LSEVEWEDQA
ESLRTAMINR ETGTLSMDVK VPMDKGKRVL FLTNDYFFTD ISDTPFSLGV VLSRGHGEYI
LLGNTSVEEG LHDLLHPDLA LAGDWIYCIT DIDPDHRKLS QLEAMIRFLT RKDPDLECDE
ELVREVLFDA VVTAPMEAYW TALALNMSEE SEHVVDMAFL GTRAGLLRSS LFVGSEKVSD
RKFLTPEDEA SVFTLDRFPL WYRQASEHPA GSFVFNLRWA EGPESAGEPM VVTASTAVAV
TVDKRTAIAA AAGVQMKLEF LQRKFWAATR QCSTVDGPCT QSCEDSDLDC FVIDNNGFIL
ISKRSRETGR FLGEVDGAVL TQLLSMGVFS QVTMYDYQAM CKPSSHHHSA AQPLVSPISA
FLTATRWLLQ ELVLFLLEWS VWGSWYDRGA EAKSVFHHSH KHKKQDPLQP CDTEYPVFVY
QPAIREANGI VECGPCQKVF VVQQIPNSNL LLLVTDPTCD CSIFPPVLQE ATEVKYNASV
KCDRMRSQKL RRRPDSCHAF HPEENAQDCG GASDTSASPP LLLLPVCAWG LLPQLLR


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E1344c ELISA kit CACNA1A,CHCACHA1A,Chicken,Gallus gallus,Voltage-dependent P_Q-type calcium channel subunit alpha-1A,Voltage-gated calcium channel subunit alpha Cav2.1 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
U1344c CLIA CACNA1A,CHCACHA1A,Chicken,Gallus gallus,Voltage-dependent P_Q-type calcium channel subunit alpha-1A,Voltage-gated calcium channel subunit alpha Cav2.1 96T
EIAAB04958 CACNA2D1,CACNL2A,CCHL2A,Oryctolagus cuniculus,Rabbit,Voltage-dependent calcium channel subunit alpha-2_delta-1,Voltage-gated calcium channel subunit alpha-2_delta-1
EIAAB04963 Cacna2d2,Kiaa0558,Mouse,Mus musculus,Protein ducky,Voltage-dependent calcium channel subunit alpha-2_delta-2,Voltage-gated calcium channel subunit alpha-2_delta-2
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
EIAAB04962 CACNA2D2,Homo sapiens,Human,KIAA0558,Voltage-dependent calcium channel subunit alpha-2_delta-2,Voltage-gated calcium channel subunit alpha-2_delta-2
EIAAB05011 CACNA1B,CHCACHA1B,Chicken,Gallus gallus,Voltage-dependent N-type calcium channel subunit alpha-1B,Voltage-gated calcium channel subunit alpha Cav2.2
EIAAB05017 CACNA1C,CHCACHA1C,Chicken,Gallus gallus,Voltage-dependent L-type calcium channel subunit alpha-1C,Voltage-gated calcium channel subunit alpha Cav1.2
EIAAB04960 Cacna2d1,Cacnl2a,Cchl2a,Rat,Rattus norvegicus,Voltage-dependent calcium channel subunit alpha-2_delta-1,Voltage-gated calcium channel subunit alpha-2_delta-1


 

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