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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_RABIT             Reviewed;        1106 AA.
P13806;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
20-JUN-2018, entry version 130.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2458626; DOI=10.1126/science.2458626;
Ellis S.B., Williams M.E., Ways N.R., Brenner R., Sharp A.H.,
Leung A.T., Campbell K.P., McKenna E., Koch W.J., Hui A., Schwartz A.,
Harpold M.M.;
"Sequence and expression of mRNAs encoding the alpha 1 and alpha 2
subunits of a DHP-sensitive calcium channel.";
Science 241:1661-1664(1988).
[2]
PROTEIN SEQUENCE OF 27-47.
PubMed=2558713; DOI=10.1021/bi00445a044;
Hamilton S.L., Hawkes M.J., Brush K., Cook R., Chang R.J.,
Smilowitz H.M.;
"Subunit composition of the purified dihydropyridine binding protein
from skeletal muscle.";
Biochemistry 28:7820-7828(1989).
[3]
PROTEIN SEQUENCE OF 961-973.
PubMed=1847144;
Jay S.D., Sharp A.H., Kahl S.D., Vedvick T.S., Harpold M.M.,
Campbell K.P.;
"Structural characterization of the dihydropyridine-sensitive calcium
channel alpha 2-subunit and the associated delta peptides.";
J. Biol. Chem. 266:3287-3293(1991).
[4]
PROTEIN SEQUENCE OF 961-975; 992-1000 AND 1033-1050, PROTEOLYTIC
PROCESSING, AND SUBUNIT.
PubMed=2168391;
de Jongh K.S., Warner C., Catterall W.A.;
"Subunits of purified calcium channels. Alpha 2 and delta are encoded
by the same gene.";
J. Biol. Chem. 265:14738-14741(1990).
-!- 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.
-!- 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.
{ECO:0000269|PubMed:2168391}.
-!- INTERACTION:
P07293:CACNA1S; NbExp=3; IntAct=EBI-9683767, EBI-8613624;
-!- 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=P13806-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Skeletal muscle.
-!- 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:0000269|PubMed:2168391}.
-!- 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; M21948; AAA81562.1; -; mRNA.
PIR; S10579; CHRBA2.
RefSeq; NP_001075745.1; NM_001082276.1. [P13806-1]
UniGene; Ocu.2039; -.
PDB; 3JBR; EM; 4.20 A; F=1-39, F=56-661, F=956-1106.
PDB; 5GJV; EM; 3.60 A; F=1-1106.
PDB; 5GJW; EM; 3.90 A; F=1-1106.
PDBsum; 3JBR; -.
PDBsum; 5GJV; -.
PDBsum; 5GJW; -.
ProteinModelPortal; P13806; -.
SMR; P13806; -.
ComplexPortal; CPX-3189; Skeletal muscle VGCC complex.
DIP; DIP-61880N; -.
IntAct; P13806; 3.
STRING; 9986.ENSOCUP00000024431; -.
GeneID; 100009105; -.
KEGG; ocu:100009105; -.
CTD; 781; -.
eggNOG; KOG2353; Eukaryota.
eggNOG; ENOG410XPDX; LUCA.
HOGENOM; HOG000004860; -.
HOVERGEN; HBG057779; -.
InParanoid; P13806; -.
KO; K04858; -.
Proteomes; UP000001811; Unplaced.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:BHF-UCL.
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; 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;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
SIGNAL 1 26 {ECO:0000269|PubMed:2558713}.
CHAIN 27 1106 Voltage-dependent calcium channel subunit
alpha-2/delta-1.
/FTId=PRO_0000304636.
CHAIN 27 960 Voltage-dependent calcium channel subunit
alpha-2-1.
/FTId=PRO_0000005007.
CHAIN 961 1106 Voltage-dependent calcium channel subunit
delta-1.
/FTId=PRO_0000005008.
TOPO_DOM 27 1076 Extracellular. {ECO:0000255}.
TRANSMEM 1077 1097 Helical. {ECO:0000255}.
TOPO_DOM 1098 1106 Cytoplasmic. {ECO:0000255}.
DOMAIN 255 432 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 448 539 Cache.
MOTIF 261 265 MIDAS-like motif.
METAL 261 261 Divalent metal cation. {ECO:0000250}.
METAL 263 263 Divalent metal cation. {ECO:0000250}.
METAL 265 265 Divalent metal cation. {ECO:0000250}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000250|UniProtKB:P54290}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 784 784 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 891 891 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 406 1062 Interchain (between alpha-2-1 and delta-1
chains). {ECO:0000250}.
CONFLICT 45 45 D -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 1106 AA; 125043 MW; B00DE7F3C877B618 CRC64;
MAAGRPLAWT LTLWQAWLIL IGPSSEEPFP SAVTIKSWVD KMQEDLVTLA KTASGVHQLV
DIYEKYQDLY TVEPNNARQL VEIAARDIEK LLSNRSKALV RLALEAEKVQ AAHQWREDFA
SNEVVYYNAK DDLDPEKNDS EPGSQRIKPV FIDDANFRRQ VSYQHAAVHI PTDIYEGSTI
VLNELNWTSA LDDVFKKNRE EDPSLLWQVF GSATGLARYY PASPWVDNSR TPNKIDLYDV
RRRPWYIQGA ASPKDMLILV DVSGSVSGLT LKLIRTSVSE MLETLSDDDF VNVASFNSNA
QDVSCFQHLV QANVRNKKVL KDAVNNITAK GITDYKKGFS FAFEQLLNYN VSRANCNKII
MLFTDGGEER AQEIFAKYNK DKKVRVFTFS VGQHNYDRGP IQWMACENKG YYYEIPSIGA
IRINTQEYLD VLGRPMVLAG DKAKQVQWTN VYLDALELGL VITGTLPVFN ITGQFENKTN
LKNQLILGVM GVDVSLEDIK RLTPRFTLCP NGYYFAIDPN GYVLLHPNLQ PKPIGVGIPT
INLRKRRPNV QNPKSQEPVT LDFLDAELEN DIKVEIRNKM IDGESGEKTF RTLVKSQDER
YIDKGNRTYT WTPVNGTDYS SLALVLPTYS FYYIKAKIEE TITQARYSET LKPDNFEESG
YTFLAPRDYC SDLKPSDNNT EFLLNFNEFI DRKTPNNPSC NTDLINRVLL DAGFTNELVQ
NYWSKQKNIK GVKARFVVTD GGITRVYPKE AGENWQENPE TYEDSFYKRS LDNDNYVFTA
PYFNKSGPGA YESGIMVSKA VEIYIQGKLL KPAVVGIKID VNSWIENFTK TSIRDPCAGP
VCDCKRNSDV MDCVILDDGG FLLMANHDDY TNQIGRFFGE IDPSLMRHLV NISVYAFNKS
YDYQSVCEPG AAPKQGAGHR SAYVPSIADI LQIGWWATAA AWSILQQFLL SLTFPRLLEA
ADMEDDDFTA SMSKQSCITE QTQYFFDNDS KSFSGVLDCG NCSRIFHVEK LMNTNLIFIM
VESKGTCPCD TRLLIQAEQT SDGPDPCDMV KQPRYRKGPD VCFDNNVLED YTDCGGVSGL
NPSLWSIIGI QFVLLWLVSG SRHCLL


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