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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_RAT               Reviewed;        1091 AA.
P54290;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
28-FEB-2018, entry version 143.
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;
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].
PubMed=1314383; DOI=10.1073/pnas.89.8.3251;
Kim H.L., Kim H., Lee P., King R.G., Chin H.;
"Rat brain expresses an alternatively spliced form of the
dihydropyridine-sensitive L-type calcium channel alpha 2 subunit.";
Proc. Natl. Acad. Sci. U.S.A. 89:3251-3255(1992).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-973, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24090084; DOI=10.1021/pr400783j;
Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
Graham M.E., Packer N.H., Cordwell S.J.;
"Site-specific glycan-peptide analysis for determination of N-
glycoproteome heterogeneity.";
J. Proteome Res. 12:5791-5800(2013).
-!- 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}.
-!- INTERACTION:
P35442:THBS2 (xeno); NbExp=2; IntAct=EBI-2466294, EBI-2466249;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=2 isoforms are produced.;
Name=1;
IsoId=P54290-1; Sequence=Displayed;
-!- 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.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M86621; AAA41088.1; -; mRNA.
PIR; A44147; A44147.
UniGene; Rn.1110; -.
UniGene; Rn.11276; -.
ProteinModelPortal; P54290; -.
SMR; P54290; -.
IntAct; P54290; 3.
STRING; 10116.ENSRNOP00000034572; -.
BindingDB; P54290; -.
ChEMBL; CHEMBL3420; -.
iPTMnet; P54290; -.
PhosphoSitePlus; P54290; -.
UniCarbKB; P54290; -.
PaxDb; P54290; -.
PRIDE; P54290; -.
RGD; 2247; Cacna2d1.
eggNOG; KOG2353; Eukaryota.
eggNOG; ENOG410XPDX; LUCA.
HOGENOM; HOG000004860; -.
HOVERGEN; HBG057779; -.
InParanoid; P54290; -.
PhylomeDB; P54290; -.
PRO; PR:P54290; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
GO; GO:0030315; C:T-tubule; ISO:RGD.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; ISO:RGD.
GO; GO:0060402; P:calcium ion transport into cytosol; IDA:BHF-UCL.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:RGD.
GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; IDA:BHF-UCL.
GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:RGD.
GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
GO; GO:0098903; P:regulation of membrane repolarization during action potential; IDA:BHF-UCL.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
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;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
SIGNAL 1 24 {ECO:0000250}.
CHAIN 25 1091 Voltage-dependent calcium channel subunit
alpha-2/delta-1.
/FTId=PRO_0000304635.
CHAIN 25 944 Voltage-dependent calcium channel subunit
alpha-2-1. {ECO:0000250}.
/FTId=PRO_0000005005.
CHAIN 945 1091 Voltage-dependent calcium channel subunit
delta-1. {ECO:0000250}.
/FTId=PRO_0000005006.
TOPO_DOM 25 1061 Extracellular. {ECO:0000255}.
TRANSMEM 1062 1082 Helical. {ECO:0000255}.
TOPO_DOM 1083 1091 Cytoplasmic. {ECO:0000255}.
DOMAIN 252 429 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 445 536 Cache.
MOTIF 258 262 MIDAS-like motif.
METAL 258 258 Divalent metal cation. {ECO:0000250}.
METAL 260 260 Divalent metal cation. {ECO:0000250}.
METAL 262 262 Divalent metal cation. {ECO:0000250}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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 323 323 N-linked (GlcNAc...) asparagine;
alternate. {ECO:0000255}.
CARBOHYD 323 323 N-linked (HexNAc...) asparagine;
alternate. {ECO:0000244|PubMed:24090084}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 593 593 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 769 769 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 876 876 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 973 973 N-linked (HexNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
DISULFID 403 1047 Interchain (between alpha-2-1 and delta-1
chains). {ECO:0000250}.
SEQUENCE 1091 AA; 123823 MW; 7054907D9D343B34 CRC64;
MAAGCLLALT LTLFQSWLIG PSSEEPFPSP VTIKSWVDKM QEDLVTLAKT ASGVTQLADI
YEKYQDLYTV EPNNARQLVE IAARDIEKLL SNRSKALVRL AMEAEKVQAA HQWREDFASN
EVVYYNAKDD LDPERNESES GSQRIKPVFI EDANFGRQIS YQHAAVHIPT DIYEGSTIVL
NELNWTSALD EVFKRNRDED PTLLWQVFAA DRLARYYPAS PWVDNSRTPN KIDLYDVRRR
PWYIQGAASP KDMLILVDVS GSVSGLTLKL IRTSVSEMLE TLSDDDFVNV ASFNSNAQDV
SCFQHLVQAN VRNKKVLKDA VNNITAKGIT DYKKGFTFAF EQLLNYNVSR ANCNKIIMLF
TDGGEERAQE IFAKYNKDKK VRVFTFSVGQ HNYDRGPIQW MACENKGYYY EIPSIGAIRI
NTQEYLDVLG RPMVLAGDKA KQVQWTNVYL DALELGLVIT GTLPVFNVTG QSENKTNLKN
QLILGVMGVD VSLEDIKRLT PRFTLCPNGY YFAIDPNGYV LLHPNLQPKN PKSQEPVTLD
FLDAELENDI KVEIRNKMID GESGEKTFRT LVKSQDERYI DKGNRTYTWT PVNGTDYRYL
ALVLPTYSFY YIKAKIEETI TQARSKKGKM KDSETLKPDN FEESGYTFIA PREYCNDLKP
SDNNTEFLLN FNEFIDRKTP NNPSCNTDLI NRILLDAGFT NELVQNYWSK QKNIKGVKAR
FVVTDGGITR VYPKEAGENW QENPETYEDS FYKRSLDNDN YVFTAPYFNK SGPGAYESGI
MVSKAVELYI QGKLLKPAVV GIKIDVNSWI ENFTKTSIRD PCAGPVCDCK RNSDVMDCVI
LDDGGFLLMA NHDDYTNQIG RFFGEIDPRM MRHLVNISLY AFNKSYDYQS VCDPGAAPKQ
GAGHRSAYVP SITDILQIGW WATAAAWSIL QQLLLSLTFP RLLEAVEMEE DDFTASLSKQ
SCITEQTQYF FKNDTKSFSG LLDCGNCSRI FHVEKLMNTN LVFIMVESKG TCPCDTRLLM
QAEQTSDGPD PCDMVKQPRY RKGPDVCFDN NVLEDYTDCG GVSGLNPSLW SIFGLQFILL
WLVSGSRHYL W


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