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Protein

Voltage-dependent L-type calcium channel subunit beta-3

Gene

Cacnb3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.

GO - Molecular functioni

  • protein kinase binding Source: RGD
  • voltage-gated calcium channel activity Source: RGD

GO - Biological processi

  • calcium ion transport Source: RGD
  • T cell receptor signaling pathway 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

Enzyme and pathway databases

ReactomeiR-RNO-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
R-RNO-422356. Regulation of insulin secretion.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5576893. Phase 2 - plateau phase.
R-RNO-5576894. Phase 1 - inactivation of fast Na+ channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit beta-3
Short name:
CAB3
Alternative name(s):
Calcium channel voltage-dependent subunit beta 3
Gene namesi
Name:Cacnb3
Synonyms:Cacnlb3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi2248. Cacnb3.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • voltage-gated calcium channel complex Source: RGD
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3137269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Voltage-dependent L-type calcium channel subunit beta-3PRO_0000144059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521PhosphoserineCombined sources
Modified residuei393 – 3931PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP54287.
PRIDEiP54287.

PTM databases

iPTMnetiP54287.
PhosphoSiteiP54287.

Expressioni

Gene expression databases

GenevisibleiP54287. RN.

Interactioni

Subunit structurei

The L-type calcium channel is composed of four subunits: alpha-1, alpha-2, beta and gamma. Interacts with CACNA2D4. Interacts with FASLG (By similarity). Interacts with CBARP; prevents the interaction of CACNB3 with the alpha subunit CACNA1C thereby negatively regulating the activity of the corresponding calcium channel.By similarity1 Publication

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi247336. 2 interactions.
DIPiDIP-59370N.
IntActiP54287. 1 interaction.
MINTiMINT-8407486.
STRINGi10116.ENSRNOP00000017490.

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 385Combined sources
Helixi40 – 5516Combined sources
Beta strandi62 – 687Combined sources
Helixi72 – 743Combined sources
Beta strandi92 – 987Combined sources
Beta strandi100 – 11011Combined sources
Beta strandi116 – 1194Combined sources
Helixi121 – 13111Combined sources
Turni136 – 1383Combined sources
Beta strandi170 – 1745Combined sources
Beta strandi180 – 1834Combined sources
Helixi191 – 20717Combined sources
Turni208 – 2103Combined sources
Beta strandi211 – 2177Combined sources
Helixi221 – 2233Combined sources
Turni226 – 2283Combined sources
Helixi231 – 2399Combined sources
Helixi240 – 2423Combined sources
Helixi247 – 26216Combined sources
Beta strandi266 – 2716Combined sources
Helixi277 – 2793Combined sources
Turni280 – 2823Combined sources
Beta strandi288 – 2925Combined sources
Helixi297 – 3059Combined sources
Helixi309 – 3124Combined sources
Helixi315 – 32612Combined sources
Helixi330 – 3323Combined sources
Beta strandi334 – 3374Combined sources
Helixi342 – 36019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYTX-ray2.60A/B16-366[»]
1VYUX-ray2.30A/B16-366[»]
ProteinModelPortaliP54287.
SMRiP54287. Positions 1-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54287.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 12062SH3Add
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG3812. Eukaryota.
ENOG410XRDI. LUCA.
GeneTreeiENSGT00390000002740.
HOGENOMiHOG000230979.
HOVERGENiHBG050765.
InParanoidiP54287.
KOiK04864.
OMAiNERNWQR.
OrthoDBiEOG7966G4.
PhylomeDBiP54287.
TreeFamiTF316195.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
IPR008079. VDCC_L_b3su.
IPR000584. VDCC_L_bsu.
[Graphical view]
PANTHERiPTHR11824. PTHR11824. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF12052. VGCC_beta4Aa_N. 1 hit.
[Graphical view]
PRINTSiPR01626. LCACHANNELB.
PR01696. LCACHANNELB3.
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P54287-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ
60 70 80 90 100
QLERAKHKPV AFAVRTNVSY CGVLDEECPV QGSGVNFEAK DFLHIKEKYS
110 120 130 140 150
NDWWIGRLVK EGGDIAFIPS PQRLESIRLK QEQKARRSGN PSSLSDIGNR
160 170 180 190 200
RSPPPSLAKQ KQKQAEHVPP YDVVPSMRPV VLVGPSLKGY EVTDMMQKAL
210 220 230 240 250
FDFLKHRFDG RISITRVTAD LSLAKRSVLN NPGKRTIIER SSARSSIAEV
260 270 280 290 300
QSEIERIFEL AKSLQLVVLD ADTINHPAQL AKTSLAPIIV FVKVSSPKVL
310 320 330 340 350
QRLIRSRGKS QMKHLTVQMM AYDKLVQCPP ESFDVILDEN QLDDACEHLA
360 370 380 390 400
EYLEVYWRAT HHPAPGPGML GPPSAIPGLQ NQQLLGERGE EHSPLERDSL
410 420 430 440 450
MPSDEASESS RQAWTGSSQR SSRHLEEDYA DAYQDLYQPH RQHTSGLPSA
460 470 480
NGHDPQDRLL AQDSEHDHND RNWQRNRPWP KDSY
Length:484
Mass (Da):54,564
Last modified:October 1, 1996 - v1
Checksum:i18815828E9C5C9CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88751 mRNA. Translation: AAA18486.1.
PIRiA46608.
RefSeqiNP_036960.1. NM_012828.2.
UniGeneiRn.2808.

Genome annotation databases

EnsembliENSRNOT00000081206; ENSRNOP00000073026; ENSRNOG00000054274.
GeneIDi25297.
KEGGirno:25297.
UCSCiRGD:2248. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88751 mRNA. Translation: AAA18486.1.
PIRiA46608.
RefSeqiNP_036960.1. NM_012828.2.
UniGeneiRn.2808.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYTX-ray2.60A/B16-366[»]
1VYUX-ray2.30A/B16-366[»]
ProteinModelPortaliP54287.
SMRiP54287. Positions 1-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247336. 2 interactions.
DIPiDIP-59370N.
IntActiP54287. 1 interaction.
MINTiMINT-8407486.
STRINGi10116.ENSRNOP00000017490.

Chemistry

ChEMBLiCHEMBL3137269.

PTM databases

iPTMnetiP54287.
PhosphoSiteiP54287.

Proteomic databases

PaxDbiP54287.
PRIDEiP54287.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000081206; ENSRNOP00000073026; ENSRNOG00000054274.
GeneIDi25297.
KEGGirno:25297.
UCSCiRGD:2248. rat.

Organism-specific databases

CTDi784.
RGDi2248. Cacnb3.

Phylogenomic databases

eggNOGiKOG3812. Eukaryota.
ENOG410XRDI. LUCA.
GeneTreeiENSGT00390000002740.
HOGENOMiHOG000230979.
HOVERGENiHBG050765.
InParanoidiP54287.
KOiK04864.
OMAiNERNWQR.
OrthoDBiEOG7966G4.
PhylomeDBiP54287.
TreeFamiTF316195.

Enzyme and pathway databases

ReactomeiR-RNO-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
R-RNO-422356. Regulation of insulin secretion.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5576893. Phase 2 - plateau phase.
R-RNO-5576894. Phase 1 - inactivation of fast Na+ channels.

Miscellaneous databases

EvolutionaryTraceiP54287.
NextBioi606063.
PROiP54287.

Gene expression databases

GenevisibleiP54287. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
IPR008079. VDCC_L_b3su.
IPR000584. VDCC_L_bsu.
[Graphical view]
PANTHERiPTHR11824. PTHR11824. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF12052. VGCC_beta4Aa_N. 1 hit.
[Graphical view]
PRINTSiPR01626. LCACHANNELB.
PR01696. LCACHANNELB3.
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a third calcium channel beta subunit."
    Castellano A., Wei X., Birnbaumer L., Perez-Reyes E.
    J. Biol. Chem. 268:3450-3455(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: INTERACTION WITH CBARP AND CACNA1C.

Entry informationi

Entry nameiCACB3_RAT
AccessioniPrimary (citable) accession number: P54287
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.