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Protein

Voltage-dependent calcium channel subunit alpha-2/delta-1

Gene

CACNA2D1

Organism
Oryctolagus cuniculus (Rabbit)
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. Plays an important role in excitation-contraction coupling.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi261 – 2611Divalent metal cationBy similarity
Metal bindingi263 – 2631Divalent metal cationBy similarity
Metal bindingi265 – 2651Divalent metal cationBy similarity

GO - Molecular functioni

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-1
Alternative name(s):
Voltage-gated calcium channel subunit alpha-2/delta-1
Cleaved into the following 2 chains:
Gene namesi
Name:CACNA2D1
Synonyms:CACNL2A, CCHL2A
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 10761050ExtracellularSequence analysisAdd
BLAST
Transmembranei1077 – 109721HelicalSequence analysisAdd
BLAST
Topological domaini1098 – 11069CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 11061080Voltage-dependent calcium channel subunit alpha-2/delta-1PRO_0000304636Add
BLAST
Chaini27 – 960934Voltage-dependent calcium channel subunit alpha-2-1PRO_0000005007Add
BLAST
Chaini961 – 1106146Voltage-dependent calcium channel subunit delta-1PRO_0000005008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Modified residuei121 – 1211PhosphoserineBy similarity
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi406 ↔ 1062Interchain (between alpha-2-1 and delta-1 chains)By similarity
Glycosylationi615 – 6151N-linked (GlcNAc...)Sequence analysis
Glycosylationi784 – 7841N-linked (GlcNAc...)Sequence analysis
Glycosylationi891 – 8911N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Proteolytically processed into subunits alpha-2-1 and delta-1 that are disulfide-linked.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Skeletal muscle.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

IntActiP13806. 1 interaction.
STRINGi9986.ENSOCUP00000024431.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JBRelectron microscopy4.20F1-39[»]
F56-661[»]
F956-1106[»]
ProteinModelPortaliP13806.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 432178VWFAPROSITE-ProRule annotationAdd
BLAST
Domaini448 – 53992CacheAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi261 – 2655MIDAS-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

eggNOGiKOG2353. Eukaryota.
ENOG410XPDX. LUCA.
HOGENOMiHOG000004860.
HOVERGENiHBG057779.
InParanoidiP13806.
KOiK04858.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR013680. VDCC_a2/dsu.
IPR013608. VWA_N.
IPR002035. VWF_A.
[Graphical view]
PfamiPF08473. VGCC_alpha2. 1 hit.
PF00092. VWA. 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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: 2 isoforms are produced.

Isoform 1 (identifier: P13806-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAGRPLAWT LTLWQAWLIL IGPSSEEPFP SAVTIKSWVD KMQEDLVTLA
60 70 80 90 100
KTASGVHQLV DIYEKYQDLY TVEPNNARQL VEIAARDIEK LLSNRSKALV
110 120 130 140 150
RLALEAEKVQ AAHQWREDFA SNEVVYYNAK DDLDPEKNDS EPGSQRIKPV
160 170 180 190 200
FIDDANFRRQ VSYQHAAVHI PTDIYEGSTI VLNELNWTSA LDDVFKKNRE
210 220 230 240 250
EDPSLLWQVF GSATGLARYY PASPWVDNSR TPNKIDLYDV RRRPWYIQGA
260 270 280 290 300
ASPKDMLILV DVSGSVSGLT LKLIRTSVSE MLETLSDDDF VNVASFNSNA
310 320 330 340 350
QDVSCFQHLV QANVRNKKVL KDAVNNITAK GITDYKKGFS FAFEQLLNYN
360 370 380 390 400
VSRANCNKII MLFTDGGEER AQEIFAKYNK DKKVRVFTFS VGQHNYDRGP
410 420 430 440 450
IQWMACENKG YYYEIPSIGA IRINTQEYLD VLGRPMVLAG DKAKQVQWTN
460 470 480 490 500
VYLDALELGL VITGTLPVFN ITGQFENKTN LKNQLILGVM GVDVSLEDIK
510 520 530 540 550
RLTPRFTLCP NGYYFAIDPN GYVLLHPNLQ PKPIGVGIPT INLRKRRPNV
560 570 580 590 600
QNPKSQEPVT LDFLDAELEN DIKVEIRNKM IDGESGEKTF RTLVKSQDER
610 620 630 640 650
YIDKGNRTYT WTPVNGTDYS SLALVLPTYS FYYIKAKIEE TITQARYSET
660 670 680 690 700
LKPDNFEESG YTFLAPRDYC SDLKPSDNNT EFLLNFNEFI DRKTPNNPSC
710 720 730 740 750
NTDLINRVLL DAGFTNELVQ NYWSKQKNIK GVKARFVVTD GGITRVYPKE
760 770 780 790 800
AGENWQENPE TYEDSFYKRS LDNDNYVFTA PYFNKSGPGA YESGIMVSKA
810 820 830 840 850
VEIYIQGKLL KPAVVGIKID VNSWIENFTK TSIRDPCAGP VCDCKRNSDV
860 870 880 890 900
MDCVILDDGG FLLMANHDDY TNQIGRFFGE IDPSLMRHLV NISVYAFNKS
910 920 930 940 950
YDYQSVCEPG AAPKQGAGHR SAYVPSIADI LQIGWWATAA AWSILQQFLL
960 970 980 990 1000
SLTFPRLLEA ADMEDDDFTA SMSKQSCITE QTQYFFDNDS KSFSGVLDCG
1010 1020 1030 1040 1050
NCSRIFHVEK LMNTNLIFIM VESKGTCPCD TRLLIQAEQT SDGPDPCDMV
1060 1070 1080 1090 1100
KQPRYRKGPD VCFDNNVLED YTDCGGVSGL NPSLWSIIGI QFVLLWLVSG

SRHCLL
Length:1,106
Mass (Da):125,043
Last modified:April 1, 1990 - v1
Checksum:iB00DE7F3C877B618
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451D → S AA sequence (PubMed:2558713).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21948 mRNA. Translation: AAA81562.1.
PIRiS10579. CHRBA2.
RefSeqiNP_001075745.1. NM_001082276.1. [P13806-1]
UniGeneiOcu.2039.

Genome annotation databases

GeneIDi100009105.
KEGGiocu:100009105.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21948 mRNA. Translation: AAA81562.1.
PIRiS10579. CHRBA2.
RefSeqiNP_001075745.1. NM_001082276.1. [P13806-1]
UniGeneiOcu.2039.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JBRelectron microscopy4.20F1-39[»]
F56-661[»]
F956-1106[»]
ProteinModelPortaliP13806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13806. 1 interaction.
STRINGi9986.ENSOCUP00000024431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009105.
KEGGiocu:100009105.

Organism-specific databases

CTDi781.

Phylogenomic databases

eggNOGiKOG2353. Eukaryota.
ENOG410XPDX. LUCA.
HOGENOMiHOG000004860.
HOVERGENiHBG057779.
InParanoidiP13806.
KOiK04858.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR013680. VDCC_a2/dsu.
IPR013608. VWA_N.
IPR002035. VWF_A.
[Graphical view]
PfamiPF08473. VGCC_alpha2. 1 hit.
PF00092. VWA. 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. "Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits of a DHP-sensitive calcium channel."
    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.
    Science 241:1661-1664(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Subunit composition of the purified dihydropyridine binding protein from skeletal muscle."
    Hamilton S.L., Hawkes M.J., Brush K., Cook R., Chang R.J., Smilowitz H.M.
    Biochemistry 28:7820-7828(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-47.
  3. "Structural characterization of the dihydropyridine-sensitive calcium channel alpha 2-subunit and the associated delta peptides."
    Jay S.D., Sharp A.H., Kahl S.D., Vedvick T.S., Harpold M.M., Campbell K.P.
    J. Biol. Chem. 266:3287-3293(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 961-973.
  4. "Subunits of purified calcium channels. Alpha 2 and delta are encoded by the same gene."
    de Jongh K.S., Warner C., Catterall W.A.
    J. Biol. Chem. 265:14738-14741(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 961-975; 992-1000 AND 1033-1050, PROTEOLYTIC PROCESSING, SUBUNIT.

Entry informationi

Entry nameiCA2D1_RABIT
AccessioniPrimary (citable) accession number: P13806
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds gabapentin, an antiepileptic drug.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.