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Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1]

 CA2D1_HUMAN             Reviewed;        1103 AA.
P54289; Q17R45; Q9UD80; Q9UD81; Q9UD82;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 3.
10-OCT-2018, entry version 180.
RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-1;
AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-1;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit alpha-2-1;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit delta-1;
Flags: Precursor;
Name=CACNA2D1; Synonyms=CACNL2A, CCHL2A, MHS3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=1309651; DOI=10.1016/0896-6273(92)90109-Q;
Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G.,
Ellis S.B., Harpold M.M.;
"Structure and functional expression of alpha 1, alpha 2, and beta
subunits of a novel human neuronal calcium channel subtype.";
Neuron 8:71-84(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 528-648 (ISOFORMS 1; 2; 3; 4 AND 5),
TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
TISSUE=Neuroblastoma;
PubMed=8107964; DOI=10.1016/0028-3908(93)90004-M;
Brust P.F., Simerson S., McCue A.F., Deal C.R., Schoonmaker S.,
Williams M.E., Velicelebi G., Johnson E.C., Harpold M.M., Ellis S.B.;
"Human neuronal voltage-dependent calcium channels: studies on subunit
structure and role in channel assembly.";
Neuropharmacology 32:1089-1102(1993).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136; ASN-324 AND ASN-675.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348; ASN-475 AND ASN-824.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[7]
INTERCHAIN DISULFIDE BOND, AND SUBUNIT.
PubMed=22054663; DOI=10.1016/j.ceca.2011.10.002;
Calderon-Rivera A., Andrade A., Hernandez-Hernandez O.,
Gonzalez-Ramirez R., Sandoval A., Rivera M., Gomora J.C., Felix R.;
"Identification of a disulfide bridge essential for structure and
function of the voltage-gated Ca(2+) channel alpha(2)delta-1 auxiliary
subunit.";
Cell Calcium 51:22-30(2012).
-!- FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium
channels regulates calcium current density and
activation/inactivation kinetics of the calcium channel. Plays an
important role in excitation-contraction coupling (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Dimer formed of alpha-2-1 and delta-1 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 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Alpha-2a;
IsoId=P54289-1; Sequence=Displayed;
Name=2; Synonyms=Alpha-2b;
IsoId=P54289-2; Sequence=VSP_038348, VSP_038350;
Name=3; Synonyms=Alpha-2c;
IsoId=P54289-3; Sequence=VSP_038349, VSP_038350;
Name=4; Synonyms=Alpha-2d;
IsoId=P54289-4; Sequence=VSP_038349;
Name=5; Synonyms=Alpha-2e;
IsoId=P54289-5; Sequence=VSP_038348;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle.
Isoform 2 is expressed in the central nervous system. Isoform 2,
isoform 4 and isoform 5 are expressed in neuroblastoma cells.
Isoform 3, isoform 4 and isoform 5 are expressed in the aorta.
{ECO:0000269|PubMed:1309651, ECO:0000269|PubMed:8107964}.
-!- 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: Proteolytically processed into subunits alpha-2-1 and delta-1
that are disulfide-linked. {ECO:0000250}.
-!- MISCELLANEOUS: Binds gabapentin, an antiepileptic drug.
-!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
family. {ECO:0000305}.
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EMBL; M76559; AAA51903.1; -; mRNA.
EMBL; CH471091; EAW76990.1; -; Genomic_DNA.
EMBL; BC117468; AAI17469.1; -; mRNA.
EMBL; BC117470; AAI17471.1; -; mRNA.
CCDS; CCDS5598.1; -. [P54289-2]
PIR; JH0565; JH0565.
RefSeq; NP_000713.2; NM_000722.3. [P54289-2]
RefSeq; XP_005250627.1; XM_005250570.2. [P54289-1]
RefSeq; XP_005250629.1; XM_005250572.2. [P54289-3]
RefSeq; XP_005250630.1; XM_005250573.2. [P54289-5]
RefSeq; XP_005250631.1; XM_005250574.2. [P54289-4]
UniGene; Hs.282151; -.
UniGene; Hs.592625; -.
UniGene; Hs.743228; -.
ProteinModelPortal; P54289; -.
SMR; P54289; -.
BioGrid; 107235; 50.
ComplexPortal; CPX-3192; Skeletal muscle VGCC complex.
ComplexPortal; CPX-3195; Cardiac muscle VGCC complex.
IntAct; P54289; 9.
STRING; 9606.ENSP00000349320; -.
BindingDB; P54289; -.
ChEMBL; CHEMBL1919; -.
DrugBank; DB00381; Amlodipine.
DrugBank; DB04838; Cyclandelate.
DrugBank; DB01023; Felodipine.
DrugBank; DB00996; Gabapentin.
DrugBank; DB00308; Ibutilide.
DrugBank; DB00270; Isradipine.
DrugBank; DB00653; Magnesium Sulfate.
DrugBank; DB00622; Nicardipine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB06712; Nilvadipine.
DrugBank; DB00401; Nisoldipine.
DrugBank; DB01054; Nitrendipine.
DrugBank; DB00421; Spironolactone.
DrugBank; DB04922; XP13512.
TCDB; 8.A.18.1.1; the ca(2+) channel auxiliary subunit Alpha2Delta types 1-4 (cca-Alpha2Delta) family.
GlyConnect; 1895; -.
iPTMnet; P54289; -.
PhosphoSitePlus; P54289; -.
SwissPalm; P54289; -.
BioMuta; CACNA2D1; -.
DMDM; 262527579; -.
EPD; P54289; -.
MaxQB; P54289; -.
PaxDb; P54289; -.
PeptideAtlas; P54289; -.
PRIDE; P54289; -.
ProteomicsDB; 56675; -.
ProteomicsDB; 56676; -. [P54289-2]
ProteomicsDB; 56677; -. [P54289-3]
ProteomicsDB; 56678; -. [P54289-4]
ProteomicsDB; 56679; -. [P54289-5]
Ensembl; ENST00000356253; ENSP00000348589; ENSG00000153956. [P54289-1]
Ensembl; ENST00000356860; ENSP00000349320; ENSG00000153956. [P54289-2]
GeneID; 781; -.
KEGG; hsa:781; -.
UCSC; uc003uhr.2; human. [P54289-1]
CTD; 781; -.
DisGeNET; 781; -.
EuPathDB; HostDB:ENSG00000153956.15; -.
GeneCards; CACNA2D1; -.
HGNC; HGNC:1399; CACNA2D1.
HPA; HPA008213; -.
HPA; HPA008621; -.
MalaCards; CACNA2D1; -.
MIM; 114204; gene.
neXtProt; NX_P54289; -.
OpenTargets; ENSG00000153956; -.
Orphanet; 130; Brugada syndrome.
Orphanet; 51083; Familial short QT syndrome.
PharmGKB; PA86; -.
eggNOG; KOG2353; Eukaryota.
eggNOG; ENOG410XPDX; LUCA.
GeneTree; ENSGT00530000062904; -.
HOVERGEN; HBG057779; -.
InParanoid; P54289; -.
KO; K04858; -.
OMA; SGVLDCG; -.
OrthoDB; EOG091G00UY; -.
PhylomeDB; P54289; -.
TreeFam; TF315824; -.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
ChiTaRS; CACNA2D1; human.
GeneWiki; CACNA2D1; -.
GenomeRNAi; 781; -.
PRO; PR:P54289; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000153956; Expressed in 204 organ(s), highest expression level in biceps brachii.
CleanEx; HS_CACNA2D1; -.
ExpressionAtlas; P54289; baseline and differential.
Genevisible; P54289; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
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:BHF-UCL.
GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:BHF-UCL.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; IMP:BHF-UCL.
GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IGI:ARUK-UCL.
GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISS:BHF-UCL.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
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; PF00092; VWA; 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; Phosphoprotein; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1103 Voltage-dependent calcium channel subunit
alpha-2/delta-1.
/FTId=PRO_0000304633.
CHAIN 25 956 Voltage-dependent calcium channel subunit
alpha-2-1. {ECO:0000250}.
/FTId=PRO_0000005001.
CHAIN 957 1103 Voltage-dependent calcium channel subunit
delta-1. {ECO:0000250}.
/FTId=PRO_0000005002.
TOPO_DOM 25 1073 Extracellular. {ECO:0000255}.
TRANSMEM 1074 1094 Helical. {ECO:0000255}.
TOPO_DOM 1095 1103 Cytoplasmic. {ECO:0000255}.
DOMAIN 253 430 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 446 556 Cache.
MOTIF 259 263 MIDAS-like motif.
METAL 259 259 Divalent metal cation. {ECO:0000250}.
METAL 261 261 Divalent metal cation. {ECO:0000250}.
METAL 263 263 Divalent metal cation. {ECO:0000250}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000250|UniProtKB:P54290}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 604 604 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 675 675 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 781 781 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 824 824 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 888 888 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 895 895 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 985 985 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 998 998 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 404 1059 Interchain (between alpha-2-1 and delta-1
chains).
VAR_SEQ 531 554 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:8107964}.
/FTId=VSP_038349.
VAR_SEQ 531 549 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:1309651,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8107964}.
/FTId=VSP_038348.
VAR_SEQ 644 644 Y -> SKKGKMKD (in isoform 2 and isoform
3). {ECO:0000303|PubMed:1309651,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8107964}.
/FTId=VSP_038350.
VARIANT 1019 1019 E -> D (in dbSNP:rs9886043).
/FTId=VAR_053960.
VARIANT 1057 1057 D -> A (in dbSNP:rs35131433).
/FTId=VAR_035047.
CONFLICT 99 99 R -> S (in Ref. 1; AAA51903).
{ECO:0000305}.
CONFLICT 386 386 T -> R (in Ref. 1; AAA51903).
{ECO:0000305}.
CONFLICT 395 395 D -> E (in Ref. 1; AAA51903).
{ECO:0000305}.
CONFLICT 635 635 L -> I (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
SEQUENCE 1103 AA; 124568 MW; 0749685DE9DB0700 CRC64;
MAAGCLLALT LTLFQSLLIG PSSEEPFPSA VTIKSWVDKM QEDLVTLAKT ASGVNQLVDI
YEKYQDLYTV EPNNARQLVE IAARDIEKLL SNRSKALVRL ALEAEKVQAA HQWREDFASN
EVVYYNAKDD LDPEKNDSEP GSQRIKPVFI EDANFGRQIS YQHAAVHIPT DIYEGSTIVL
NELNWTSALD EVFKKNREED PSLLWQVFGS ATGLARYYPA SPWVDNSRTP NKIDLYDVRR
RPWYIQGAAS PKDMLILVDV SGSVSGLTLK LIRTSVSEML ETLSDDDFVN VASFNSNAQD
VSCFQHLVQA NVRNKKVLKD AVNNITAKGI TDYKKGFSFA FEQLLNYNVS RANCNKIIML
FTDGGEERAQ EIFNKYNKDK KVRVFTFSVG QHNYDRGPIQ WMACENKGYY YEIPSIGAIR
INTQEYLDVL GRPMVLAGDK AKQVQWTNVY LDALELGLVI TGTLPVFNIT GQFENKTNLK
NQLILGVMGV DVSLEDIKRL TPRFTLCPNG YYFAIDPNGY VLLHPNLQPK PIGVGIPTIN
LRKRRPNIQN PKSQEPVTLD FLDAELENDI KVEIRNKMID GESGEKTFRT LVKSQDERYI
DKGNRTYTWT PVNGTDYSLA LVLPTYSFYY IKAKLEETIT QARYSETLKP DNFEESGYTF
IAPRDYCNDL KISDNNTEFL LNFNEFIDRK TPNNPSCNAD LINRVLLDAG FTNELVQNYW
SKQKNIKGVK ARFVVTDGGI TRVYPKEAGE NWQENPETYE DSFYKRSLDN DNYVFTAPYF
NKSGPGAYES GIMVSKAVEI YIQGKLLKPA VVGIKIDVNS WIENFTKTSI RDPCAGPVCD
CKRNSDVMDC VILDDGGFLL MANHDDYTNQ IGRFFGEIDP SLMRHLVNIS VYAFNKSYDY
QSVCEPGAAP KQGAGHRSAY VPSVADILQI GWWATAAAWS ILQQFLLSLT FPRLLEAVEM
EDDDFTASLS KQSCITEQTQ YFFDNDSKSF SGVLDCGNCS RIFHGEKLMN TNLIFIMVES
KGTCPCDTRL LIQAEQTSDG PNPCDMVKQP RYRKGPDVCF DNNVLEDYTD CGGVSGLNPS
LWYIIGIQFL LLWLVSGSTH RLL


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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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