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Protein

Voltage-dependent calcium channel subunit alpha-2/delta-3

Gene

Cacna2d3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi262 – 2621Divalent metal cationBy similarity
Metal bindingi264 – 2641Divalent metal cationBy similarity
Metal bindingi266 – 2661Divalent metal cationBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. voltage-gated calcium channel activity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent calcium channel subunit alpha-2/delta-3
Alternative name(s):
Voltage-gated calcium channel subunit alpha-2/delta-3
Cleaved into the following 2 chains:
Gene namesi
Name:Cacna2d3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1338890. Cacna2d3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 1007974ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1069 – 108921HelicalSequence AnalysisAdd
BLAST
Topological domaini1090 – 10912CytoplasmicSequence Analysis

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 1091Voltage-dependent calcium channel subunit delta-3Sequence AnalysisPRO_0000304651
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 10911058Voltage-dependent calcium channel subunit alpha-2/delta-3PRO_0000304649Add
BLAST
Chaini34 – ?Voltage-dependent calcium channel subunit alpha-2-3Sequence AnalysisPRO_0000304650

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi412 ↔ 1055Interchain (between alpha-2-3 and delta-3 chains)By similarity
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence Analysis
Modified residuei924 – 9241PhosphotyrosineBy similarity

Post-translational modificationi

N-glycosylated.1 Publication
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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Z1L5.
PaxDbiQ9Z1L5.
PRIDEiQ9Z1L5.

PTM databases

PhosphoSiteiQ9Z1L5.

Expressioni

Tissue specificityi

Brain-specific. Predominantly expressed in the caudate putamen, entorhinal complex, hippocampus and cortex.2 Publications

Gene expression databases

BgeeiQ9Z1L5.
GenevestigatoriQ9Z1L5.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ9Z1L5. 1 interaction.
STRINGi10090.ENSMUSP00000022567.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1L5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini256 – 438183VWFAPROSITE-ProRule annotationAdd
BLAST
Domaini452 – 54998CacheAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi262 – 2665MIDAS-like motif

Domaini

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.By similarity

Sequence similaritiesi

Contains 1 cache domain.Curated
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307080.
GeneTreeiENSGT00530000062904.
HOGENOMiHOG000010247.
HOVERGENiHBG107124.
InParanoidiQ9Z1L5.
KOiK04860.
OMAiSHNESLK.
OrthoDBiEOG7NSB1G.
PhylomeDBiQ9Z1L5.
TreeFamiTF315824.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR004010. Cache_domain.
IPR013608. VWA_N.
IPR002035. VWF_A.
[Graphical view]
PfamiPF02743. Cache_1. 1 hit.
PF08399. VWA_N. 1 hit.
[Graphical view]
SMARTiSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z1L5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGPGSLCCA SRGASALLAT ALLYAALGDV VRSEQQIPLS VVKLWASAFG
60 70 80 90 100
GEIKSIAAKY SGSQLLQKKY KEYEKDVAIE EIDGLQLVKK LAKIMEEMFH
110 120 130 140 150
KKSEAVRRLV EAAEEAHLKH EFDADLQYEY FNAVLINERD KDGNFLELGK
160 170 180 190 200
EFILAPNDHF NNLPVNISLS DVQVPTNMYN KDPAIVNGVY WSESLNKVFV
210 220 230 240 250
DNFDRDPSLI WQYFGSAKGF FRQYPGIKWE PDENGVIAFD CRNRKWYIQA
260 270 280 290 300
ATSPKDVVIL VDVSGSMKGL RLTIAKQTVS SILDTLGDDD FFNIITYNEE
310 320 330 340 350
LHYVEPCLNG TLVQADRTNK EHFREHLDKL FAKGIGMLDI ALNEAFNILS
360 370 380 390 400
DFNHTGQGSI CSQAIMLITD GAVDTYDTIF AKYNWPDRKV RIFTYLIGRE
410 420 430 440 450
AAFADNLKWM ACANKGFFTQ ISTLADVQEN VMEYLHVLSR PKVIDQEHDV
460 470 480 490 500
VWTEAYIDST LPQAQKLADD QGLVLMTTVA MPVFSKQNET RSKGILLGVV
510 520 530 540 550
GTDVPVKELL KTIPKYKLGI HGYAFAITNN GYILTHPELR PLYEEGKKRR
560 570 580 590 600
KPNYSSVDLS EVEWEDRDDV LRNAMVNRKT GKFSMEVKKT VDKGKRVLVM
610 620 630 640 650
TNDYYYTDIK GTPFSLGVAL SRGHGKYFFR GNVTIEEGLH DLEHPDVSLA
660 670 680 690 700
DEWSYCNTDL HPEHRHLSQL EAIKLYLKGK EPLLQCDKEL IQEVLFDAVV
710 720 730 740 750
SAPIEAYWTS LALNKSENSD KGVEVAFLGT RTGLSRINLF VGAEQLTNQD
760 770 780 790 800
FLKAGDKENI FNADHFPLWY RRAAEQIAGS FVYSIPFSTG TVNKSNVVTA
810 820 830 840 850
STSIQLLDER KSPVVAAVGI QMKLEFFQRK FWTASRQCAS LDGKCSISCD
860 870 880 890 900
DETVNCYLID NNGFILVSED YTQTGDFFGE VEGAVMNKLL TMGSFKRITL
910 920 930 940 950
YDYQAMCRAN KESSDSAHGL LDPYKAFLSA AKWIMTELVL FLVEFNLCSW
960 970 980 990 1000
WHSDMTAKAQ KLKQTLEPCD TEYPAFVSER TIKETTGNIA CEDCSKSFVI
1010 1020 1030 1040 1050
QQIPSSNLFM VVVDSSCLCE SVAPITMAPI EIRYNESLKC ERLKAQKIRR
1060 1070 1080 1090
RPESCHGFHP EENARECGGA SSLQAQAALL LLPLVSSLFS R
Length:1,091
Mass (Da):122,778
Last modified:May 1, 1999 - v1
Checksum:i7AEE2BDA10077A0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010949 mRNA. Translation: CAA09423.1.
PIRiT30256.
RefSeqiNP_033915.1. NM_009785.1.
UniGeneiMm.386754.

Genome annotation databases

EnsembliENSMUST00000022567; ENSMUSP00000022567; ENSMUSG00000021991.
GeneIDi12294.
KEGGimmu:12294.
UCSCiuc007sui.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010949 mRNA. Translation: CAA09423.1.
PIRiT30256.
RefSeqiNP_033915.1. NM_009785.1.
UniGeneiMm.386754.

3D structure databases

ProteinModelPortaliQ9Z1L5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z1L5. 1 interaction.
STRINGi10090.ENSMUSP00000022567.

PTM databases

PhosphoSiteiQ9Z1L5.

Proteomic databases

MaxQBiQ9Z1L5.
PaxDbiQ9Z1L5.
PRIDEiQ9Z1L5.

Protocols and materials databases

DNASUi12294.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022567; ENSMUSP00000022567; ENSMUSG00000021991.
GeneIDi12294.
KEGGimmu:12294.
UCSCiuc007sui.1. mouse.

Organism-specific databases

CTDi55799.
MGIiMGI:1338890. Cacna2d3.

Phylogenomic databases

eggNOGiNOG307080.
GeneTreeiENSGT00530000062904.
HOGENOMiHOG000010247.
HOVERGENiHBG107124.
InParanoidiQ9Z1L5.
KOiK04860.
OMAiSHNESLK.
OrthoDBiEOG7NSB1G.
PhylomeDBiQ9Z1L5.
TreeFamiTF315824.

Miscellaneous databases

ChiTaRSiCacna2d3. mouse.
NextBioi280792.
PROiQ9Z1L5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1L5.
GenevestigatoriQ9Z1L5.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR004010. Cache_domain.
IPR013608. VWA_N.
IPR002035. VWF_A.
[Graphical view]
PfamiPF02743. Cache_1. 1 hit.
PF08399. VWA_N. 1 hit.
[Graphical view]
SMARTiSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular diversity of the calcium channel alpha2delta subunit."
    Klugbauer N., Lacinova L., Marais E., Hobom M., Hofmann F.
    J. Neurosci. 19:684-691(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Absence of modulation of the expressed calcium channel alpha1G subunit by alpha2delta subunits."
    Lacinova L., Klugbauer N., Hofmann F.
    J. Physiol. (Lond.) 516:639-645(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Tissue-specific expression and gabapentin-binding properties of calcium channel alpha2delta subunit subtypes."
    Gong H.C., Hang J., Kohler W., Li L., Su T.-Z.
    J. Membr. Biol. 184:35-43(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Calcium channel alpha(2)delta subunits-structure and Gabapentin binding."
    Marais E., Klugbauer N., Hofmann F.
    Mol. Pharmacol. 59:1243-1248(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION, PROTEOLYTIC PROCESSING, LACK OF GABAPENTIN-BINDING.

Entry informationi

Entry nameiCA2D3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to CACNA2D1 and CACNA2D2, it does not bind gabapentin, an antiepileptic drug.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.