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Protein

Voltage-dependent calcium channel gamma-3 subunit

Gene

Cacng3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.2 Publications

GO - Molecular functioni

GO - Biological processi

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-399719. Trafficking of AMPA receptors.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5576893. Phase 2 - plateau phase.
R-RNO-5576894. Phase 1 - inactivation of fast Na+ channels.
R-RNO-5682910. LGI-ADAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent calcium channel gamma-3 subunit
Alternative name(s):
Neuronal voltage-gated calcium channel gamma-3 subunit
Transmembrane AMPAR regulatory protein gamma-3
Short name:
TARP gamma-3
Gene namesi
Name:Cacng3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi628803. Cacng3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821HelicalSequence analysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence analysisAdd
BLAST
Transmembranei135 – 15521HelicalSequence analysisAdd
BLAST
Transmembranei181 – 20121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Voltage-dependent calcium channel gamma-3 subunitPRO_0000164677Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8VHX0.
PRIDEiQ8VHX0.

PTM databases

iPTMnetiQ8VHX0.
PhosphoSiteiQ8VHX0.

Expressioni

Gene expression databases

GenevisibleiQ8VHX0. RN.

Interactioni

Subunit structurei

The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG4, CACNG5; CACNG7 and CACNG8.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016632.

Structurei

3D structure databases

ProteinModelPortaliQ8VHX0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFNQ. Eukaryota.
ENOG4110ISU. LUCA.
GeneTreeiENSGT00550000074547.
HOGENOMiHOG000233440.
HOVERGENiHBG003682.
InParanoidiQ8VHX0.
KOiK04868.
OMAiLNSERDH.
OrthoDBiEOG7TQV1Q.
PhylomeDBiQ8VHX0.
TreeFamiTF327980.

Family and domain databases

InterProiIPR004031. PMP22/EMP/MP20/Claudin.
IPR008368. VDCC_gsu.
[Graphical view]
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01792. VDCCGAMMA.

Sequencei

Sequence statusi: Complete.

Q8VHX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRMCDRGIQM LITTVGAFAA FSLMTIAVGT DYWLYSRGVC RTKSTSDNET
60 70 80 90 100
SRKNEEVMTH SGLWRTCCLE GAFRGVCKKI DHFPEDADYE QDTAEYLLRA
110 120 130 140 150
VRASSVFPIL SVTLLFFGGL CVAASEFHRS RHSVILSAGI FFVSAGLSNI
160 170 180 190 200
IGIIVYISAN AGDPGQRDSK KSYSYGWSFY FGAFSFIIAE IVGVVAVHIY
210 220 230 240 250
IEKHQQLRAR SHSELLKKST FARLPPYRYR FRRRSSSRST EPRSRDLSPI
260 270 280 290 300
SKGFHTIPST DISMFTLSRD PSKLTMGTLL NSDRDHAFLQ FHNSTPKEFK
310
ESLHNNPANR RTTPV
Length:315
Mass (Da):35,516
Last modified:March 1, 2002 - v1
Checksum:iFB4EA036C494B6AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361340 mRNA. Translation: AAL50035.1.
RefSeqiNP_542422.1. NM_080691.1.
UniGeneiRn.212756.

Genome annotation databases

EnsembliENSRNOT00000016632; ENSRNOP00000016632; ENSRNOG00000012362.
GeneIDi140724.
KEGGirno:140724.
UCSCiRGD:628803. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361340 mRNA. Translation: AAL50035.1.
RefSeqiNP_542422.1. NM_080691.1.
UniGeneiRn.212756.

3D structure databases

ProteinModelPortaliQ8VHX0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016632.

PTM databases

iPTMnetiQ8VHX0.
PhosphoSiteiQ8VHX0.

Proteomic databases

PaxDbiQ8VHX0.
PRIDEiQ8VHX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016632; ENSRNOP00000016632; ENSRNOG00000012362.
GeneIDi140724.
KEGGirno:140724.
UCSCiRGD:628803. rat.

Organism-specific databases

CTDi10368.
RGDi628803. Cacng3.

Phylogenomic databases

eggNOGiENOG410IFNQ. Eukaryota.
ENOG4110ISU. LUCA.
GeneTreeiENSGT00550000074547.
HOGENOMiHOG000233440.
HOVERGENiHBG003682.
InParanoidiQ8VHX0.
KOiK04868.
OMAiLNSERDH.
OrthoDBiEOG7TQV1Q.
PhylomeDBiQ8VHX0.
TreeFamiTF327980.

Enzyme and pathway databases

ReactomeiR-RNO-399719. Trafficking of AMPA receptors.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5576893. Phase 2 - plateau phase.
R-RNO-5576894. Phase 1 - inactivation of fast Na+ channels.
R-RNO-5682910. LGI-ADAM interactions.

Miscellaneous databases

PROiQ8VHX0.

Gene expression databases

GenevisibleiQ8VHX0. RN.

Family and domain databases

InterProiIPR004031. PMP22/EMP/MP20/Claudin.
IPR008368. VDCC_gsu.
[Graphical view]
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01792. VDCCGAMMA.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Calcium channel gamma subunits provide insights into the evolution of this gene family."
    Chu P.-J., Robertson H.M., Best P.M.
    Gene 280:37-48(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "TARP subtypes differentially and dose-dependently control synaptic AMPA receptor gating."
    Milstein A.D., Zhou W., Karimzadegan S., Bredt D.S., Nicoll R.A.
    Neuron 55:905-918(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5."
    Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
    Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors."
    Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.
    Science 323:1313-1319(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "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-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCCG3_RAT
AccessioniPrimary (citable) accession number: Q8VHX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 98 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

Complete proteome, Reference proteome

Documents

  1. 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.