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

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Q9Z1L5 (CA2D3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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:

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

Gene names

Name:

Cacna2d3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1091 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Calcium channel Ion channel Voltage-gated channel
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated calcium channel activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

Potential

Chain

34 – 1091

1058

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

PRO_0000304649

Chain

34 – ?

Voltage-dependent calcium channel subunit alpha-2-3 Potential

PRO_0000304650

Chain

? – 1091

Voltage-dependent calcium channel subunit delta-3 Potential

PRO_0000304651

Regions

Topological domain

34 – 1007

974

Extracellular Potential

Transmembrane

1008 – 1030

Helical; Potential

Topological domain

1031 – 1091

Cytoplasmic Potential

Domain

256 – 438

183

VWFA

Domain

452 – 549

Cache

Motif

262 – 266

MIDAS-like motif

Sites

Metal binding

262

Divalent metal cation By similarity

Metal binding

264

Divalent metal cation By similarity

Metal binding

266

Divalent metal cation By similarity

Amino acid modifications

Glycosylation

166

N-linked (GlcNAc...) Potential

Glycosylation

309

N-linked (GlcNAc...) Potential

Glycosylation

553

N-linked (GlcNAc...) Potential

Glycosylation

632

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z1L5 [UniParc].

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

FASTA

1,091

122,778

        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

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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.
IPI	IPI00130253.
PIR	T30256.
RefSeq	NP_033915.1. NM_009785.1.
UniGene	Mm.386754.
3D structure databases
ProteinModelPortal	Q9Z1L5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z1L5. 1 interaction.
STRING	10090.ENSMUSP00000022567.
PTM databases
PhosphoSite	Q9Z1L5.
Proteomic databases
PaxDb	Q9Z1L5.
PRIDE	Q9Z1L5.
Protocols and materials databases
DNASU	12294.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022567; ENSMUSP00000022567; ENSMUSG00000021991.
GeneID	12294.
KEGG	mmu:12294.
UCSC	uc007sui.1. mouse.
Organism-specific databases
CTD	55799.
MGI	MGI:1338890. Cacna2d3.
Phylogenomic databases
eggNOG	NOG307080.
GeneTree	ENSGT00530000062904.
HOGENOM	HOG000010247.
HOVERGEN	HBG107124.
InParanoid	Q9Z1L5.
KO	K04860.
OMA	KTIPKYK.
OrthoDB	EOG479F69.
Gene expression databases
Bgee	Q9Z1L5.
Genevestigator	Q9Z1L5.
Family and domain databases
InterPro	IPR004010. Cache_domain. IPR013608. VWA_N. IPR002035. VWF_A. [Graphical view]
Pfam	PF02743. Cache_1. 1 hit. PF08399. VWA_N. 1 hit. [Graphical view]
SMART	SM00327. VWA. 1 hit. [Graphical view]
PROSITE	PS50234. VWFA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280792.
SOURCE	Search...

Entry information

Entry name

CA2D3_MOUSE

Accession

Primary (citable) accession number: Q9Z1L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents