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Voltage-dependent calcium channel subunit alpha-2/delta-3 (Voltage-gated calcium channel subunit alpha-2/delta-3) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-3; Voltage-dependent calcium channel subunit delta-3]

 CA2D3_RAT               Reviewed;        1085 AA.
Q8CFG5;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-NOV-2018, entry version 96.
RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-3;
AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-3;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit alpha-2-3;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit delta-3;
Flags: Precursor;
Name=Cacna2d3;
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], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=Sprague-Dawley; TISSUE=Heart atrium;
PubMed=12606261; DOI=10.1016/S0022-2828(02)00313-9;
Chu P.-J., Best P.M.;
"Molecular cloning of calcium channel alpha(2)delta-subunits from rat
atria and the differential regulation of their expression by IGF-1.";
J. Mol. Cell. Cardiol. 35:207-215(2003).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-918, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
-!- FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium
channels regulates calcium current density and
activation/inactivation kinetics of the calcium channel. Acts as a
regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type
(CACNA1B), L-type (CACNA1C OR CACNA1D) but not T-type (CACNA1G)
(By similarity). {ECO:0000250}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: In heart, it is expressed in atrium but not in
ventricle. {ECO:0000269|PubMed:12606261}.
-!- INDUCTION: By IGF1. {ECO:0000269|PubMed:12606261}.
-!- 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: N-glycosylated. {ECO:0000250}.
-!- PTM: May be proteolytically processed into subunits alpha-2-3 and
delta-3 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}.
-!- MISCELLANEOUS: In contrast to CACNA2D1 and CACNA2D2, it does not
bind gabapentin, an antiepileptic drug. {ECO:0000250}.
-!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
family. {ECO:0000305}.
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EMBL; AF486278; AAO14654.1; -; mRNA.
RefSeq; NP_783185.1; NM_175595.2.
UniGene; Rn.229510; -.
ProteinModelPortal; Q8CFG5; -.
STRING; 10116.ENSRNOP00000042602; -.
iPTMnet; Q8CFG5; -.
PhosphoSitePlus; Q8CFG5; -.
PaxDb; Q8CFG5; -.
PRIDE; Q8CFG5; -.
GeneID; 306243; -.
KEGG; rno:306243; -.
UCSC; RGD:631361; rat.
CTD; 55799; -.
RGD; 631361; Cacna2d3.
eggNOG; KOG2353; Eukaryota.
eggNOG; ENOG410XPDX; LUCA.
HOGENOM; HOG000010247; -.
HOVERGEN; HBG107124; -.
InParanoid; Q8CFG5; -.
KO; K04860; -.
PhylomeDB; Q8CFG5; -.
PRO; PR:Q8CFG5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
GO; GO:0005246; F:calcium channel regulator activity; TAS:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0006816; P:calcium ion transport; IDA:RGD.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEP:RGD.
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;
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 33 {ECO:0000255}.
CHAIN 34 1085 Voltage-dependent calcium channel subunit
alpha-2/delta-3.
/FTId=PRO_0000304652.
CHAIN 34 ? Voltage-dependent calcium channel subunit
alpha-2-3. {ECO:0000255}.
/FTId=PRO_0000304653.
CHAIN ? 1085 Voltage-dependent calcium channel subunit
delta-3. {ECO:0000255}.
/FTId=PRO_0000304654.
TOPO_DOM 34 1062 Extracellular. {ECO:0000255}.
TRANSMEM 1063 1083 Helical. {ECO:0000255}.
TOPO_DOM 1084 1085 Cytoplasmic. {ECO:0000255}.
DOMAIN 256 438 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 452 543 Cache.
MOTIF 262 266 MIDAS-like motif.
METAL 262 262 Divalent metal cation. {ECO:0000250}.
METAL 264 264 Divalent metal cation. {ECO:0000250}.
METAL 266 266 Divalent metal cation. {ECO:0000250}.
MOD_RES 918 918 Phosphotyrosine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 547 547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 626 626 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 412 1049 Interchain (between alpha-2-3 and delta-3
chains). {ECO:0000250}.
SEQUENCE 1085 AA; 122204 MW; 9584F533E318002A CRC64;
MAGPGSLCCA SRGASALLAT ALLYAALGDV VRSEQQIPLS VVKLWASAFG GEIKSIAAKY
SGSQLLQKKY KEYEKDVAIE EIDGLQLVKK LAKNMEEMFH KKSEAVRRLV EAAEEAHLKH
EFDADLQYEY FNAVLINERD KDGNFLELGK EFILAPNDHF NNLPVNISLS DVQVPTNMYN
KDPAIVNGVY WSESLNKVFV DNFDRDPSLI WQYFGSAKGF FRQYPGIKWE PDENGVIAFD
CRNRKWYIQA ATSPKDVVIL VDVSGSMKGL RLTIAKQTVS SILDTLGDDD FFNIITYNEE
LHYVEPCLNG TLVQADRTNK EHFREHLDKL FAKGIGMLDI ALNEAFNVLS DFNHTGQGSI
CSQAIMLITD GAVDTYDTIF AKYNWPERKV RIFTYLIGRE AAFADNLKWM ACANKGFFTQ
ISTLADVQEN VMEYLHVLSR PKVIDQEHDV VWTEAYIDST LADDQGLVLM TTVAMPVFSK
QNETRSKGIL LGVVGTDVPV KELLKTIPKY KLGIHGYAFA ITNNGYILTH PELRPLYEEG
KKRRKPNYSS VDLSEVEWED RDDVLRNAMV NRKTGKFSME VKKTVDKGKR VLVMTNDYYY
TDIKGAPFSL GVALSRGHGK YFFRGNVTIE EGLHDLEHPD VSLADEWSYC NTDLHPEHRH
LSQLEAIKLY LKGKEPLLQC DKELIQEVLF DAVVSAPIEA YWTSLALNKS ENSDKGVEVA
FLGTRTGLSR INLFVGAEQL TNQDFLKARD KENIFNADHF PLWYRRAAEQ IPGSFVYSIP
FSTGTVNKSN VVTASTSIQL LDERKSPVVA AVGIQMKLEF FQRKFWTASR QCASLDGKCS
ISCDDETVNC YLIDNNGFIL VSEDYTQTGD FFGEVEGAVM NKLLTMGSFK RITLYDYQAM
CRANKESSDS AHGLLDPYKA FLSAAKWIVT ELVLFLVEFN LCSWWHSDMT AKAQKLKQTL
EPCDTEYPAF VSERTIKETT GNIACEDCSK SFVIQQIPSS NLFMVVVDSS CLCESVAPIT
MAPIEIRYNE SLKCERLKAQ KIRRRPESCH GFHPEENARE CGGASSLQAQ VALLLLPLVS
SLFSR


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