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Q9Z1L5 (CA2D3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent calcium channel subunit alpha-2/delta-3
Alternative name(s):
Voltage-gated calcium channel subunit alpha-2/delta-3
Gene names
Name:Cacna2d3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1091 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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). Ref.1 Ref.2

Subunit structure

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.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Brain-specific. Predominantly expressed in the caudate putamen, entorhinal complex, hippocampus and cortex. Ref.1 Ref.3

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 By similarity.

Post-translational modification

N-glycosylated. Ref.4

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.

Miscellaneous

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

Sequence similarities

Belongs to the calcium channel subunit alpha-2/delta family.

Contains 1 cache domain.

Contains 1 VWFA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 10911058Voltage-dependent calcium channel subunit alpha-2/delta-3
PRO_0000304649
Chain34 – ?Voltage-dependent calcium channel subunit alpha-2-3 PotentialPRO_0000304650
Chain? – 1091Voltage-dependent calcium channel subunit delta-3 PotentialPRO_0000304651

Regions

Topological domain34 – 1007974Extracellular Potential
Transmembrane1069 – 108921Helical; Potential
Topological domain1090 – 10912Cytoplasmic Potential
Domain256 – 438183VWFA
Domain452 – 54998Cache
Motif262 – 2665MIDAS-like motif

Sites

Metal binding2621Divalent metal cation By similarity
Metal binding2641Divalent metal cation By similarity
Metal binding2661Divalent metal cation By similarity

Amino acid modifications

Modified residue9241Phosphotyrosine By similarity
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential
Disulfide bond412 ↔ 1055Interchain (between alpha-2-3 and delta-3 chains) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z1L5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7AEE2BDA10077A0A

FASTA1,091122,778
        10         20         30         40         50         60 
MAGPGSLCCA SRGASALLAT ALLYAALGDV VRSEQQIPLS VVKLWASAFG GEIKSIAAKY 

        70         80         90        100        110        120 
SGSQLLQKKY KEYEKDVAIE EIDGLQLVKK LAKIMEEMFH KKSEAVRRLV EAAEEAHLKH 

       130        140        150        160        170        180 
EFDADLQYEY FNAVLINERD KDGNFLELGK EFILAPNDHF NNLPVNISLS DVQVPTNMYN 

       190        200        210        220        230        240 
KDPAIVNGVY WSESLNKVFV DNFDRDPSLI WQYFGSAKGF FRQYPGIKWE PDENGVIAFD 

       250        260        270        280        290        300 
CRNRKWYIQA ATSPKDVVIL VDVSGSMKGL RLTIAKQTVS SILDTLGDDD FFNIITYNEE 

       310        320        330        340        350        360 
LHYVEPCLNG TLVQADRTNK EHFREHLDKL FAKGIGMLDI ALNEAFNILS DFNHTGQGSI 

       370        380        390        400        410        420 
CSQAIMLITD GAVDTYDTIF AKYNWPDRKV RIFTYLIGRE AAFADNLKWM ACANKGFFTQ 

       430        440        450        460        470        480 
ISTLADVQEN VMEYLHVLSR PKVIDQEHDV VWTEAYIDST LPQAQKLADD QGLVLMTTVA 

       490        500        510        520        530        540 
MPVFSKQNET RSKGILLGVV GTDVPVKELL KTIPKYKLGI HGYAFAITNN GYILTHPELR 

       550        560        570        580        590        600 
PLYEEGKKRR KPNYSSVDLS EVEWEDRDDV LRNAMVNRKT GKFSMEVKKT VDKGKRVLVM 

       610        620        630        640        650        660 
TNDYYYTDIK GTPFSLGVAL SRGHGKYFFR GNVTIEEGLH DLEHPDVSLA DEWSYCNTDL 

       670        680        690        700        710        720 
HPEHRHLSQL EAIKLYLKGK EPLLQCDKEL IQEVLFDAVV SAPIEAYWTS LALNKSENSD 

       730        740        750        760        770        780 
KGVEVAFLGT RTGLSRINLF VGAEQLTNQD FLKAGDKENI FNADHFPLWY RRAAEQIAGS 

       790        800        810        820        830        840 
FVYSIPFSTG TVNKSNVVTA STSIQLLDER KSPVVAAVGI QMKLEFFQRK FWTASRQCAS 

       850        860        870        880        890        900 
LDGKCSISCD DETVNCYLID NNGFILVSED YTQTGDFFGE VEGAVMNKLL TMGSFKRITL 

       910        920        930        940        950        960 
YDYQAMCRAN KESSDSAHGL LDPYKAFLSA AKWIMTELVL FLVEFNLCSW WHSDMTAKAQ 

       970        980        990       1000       1010       1020 
KLKQTLEPCD TEYPAFVSER TIKETTGNIA CEDCSKSFVI QQIPSSNLFM VVVDSSCLCE 

      1030       1040       1050       1060       1070       1080 
SVAPITMAPI EIRYNESLKC ERLKAQKIRR RPESCHGFHP EENARECGGA SSLQAQAALL 

      1090 
LLPLVSSLFS R 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ010949 mRNA. Translation: CAA09423.1.
PIRT30256.
RefSeqNP_033915.1. NM_009785.1.
UniGeneMm.386754.

3D structure databases

ProteinModelPortalQ9Z1L5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z1L5. 1 interaction.
STRING10090.ENSMUSP00000022567.

PTM databases

PhosphoSiteQ9Z1L5.

Proteomic databases

MaxQBQ9Z1L5.
PaxDbQ9Z1L5.
PRIDEQ9Z1L5.

Protocols and materials databases

DNASU12294.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022567; ENSMUSP00000022567; ENSMUSG00000021991.
GeneID12294.
KEGGmmu:12294.
UCSCuc007sui.1. mouse.

Organism-specific databases

CTD55799.
MGIMGI:1338890. Cacna2d3.

Phylogenomic databases

eggNOGNOG307080.
GeneTreeENSGT00530000062904.
HOGENOMHOG000010247.
HOVERGENHBG107124.
InParanoidQ9Z1L5.
KOK04860.
OMAKHEFDAD.
OrthoDBEOG7NSB1G.
PhylomeDBQ9Z1L5.
TreeFamTF315824.

Gene expression databases

BgeeQ9Z1L5.
GenevestigatorQ9Z1L5.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR004010. Cache_domain.
IPR013608. VWA_N.
IPR002035. VWF_A.
[Graphical view]
PfamPF02743. Cache_1. 1 hit.
PF08399. VWA_N. 1 hit.
[Graphical view]
SMARTSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
PROSITEPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280792.
PROQ9Z1L5.
SOURCESearch...

Entry information

Entry nameCA2D3_MOUSE
AccessionPrimary (citable) accession number: Q9Z1L5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot