ID   CCG3_MOUSE              Reviewed;         315 AA.
AC   Q9JJV5; A6H6R5;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Voltage-dependent calcium channel gamma-3 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-3 subunit;
DE   AltName: Full=Transmembrane AMPAR regulatory protein gamma-3;
DE            Short=TARP gamma-3;
GN   Name=Cacng3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10734232; DOI=10.1016/s0014-5793(00)01306-5;
RA   Klugbauer N., Dai S., Specht V., Lacinova L., Marais E., Bohn G.,
RA   Hofmann F.;
RT   "A family of gamma-like calcium channel subunits.";
RL   FEBS Lett. 470:189-197(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH AP4M1 AND GRIA1, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF 227-TYR--THR-240.
RX   PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
RA   Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
RA   Yuzaki M.;
RT   "Accumulation of AMPA receptors in autophagosomes in neuronal axons lacking
RT   adaptor protein AP-4.";
RL   Neuron 57:730-745(2008).
CC   -!- FUNCTION: Regulates the trafficking to the somatodendritic compartment
CC       and gating properties of AMPA-selective glutamate receptors (AMPARs)
CC       (PubMed:18341993). Promotes their targeting to the cell membrane and
CC       synapses and modulates their gating properties by slowing their rates
CC       of activation, deactivation and desensitization. Does not show subunit-
CC       specific AMPA receptor regulation and regulates all AMPAR subunits.
CC       Thought to stabilize the calcium channel in an inactivated (closed)
CC       state (By similarity). {ECO:0000250|UniProtKB:Q8VHX0,
CC       ECO:0000269|PubMed:18341993}.
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma. Acts as an auxiliary subunit
CC       for AMPA-selective glutamate receptors (AMPARs). Found in a complex
CC       with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG4, CACNG5,
CC       CACNG7 and CACNG8 (By similarity). Interacts with AP4M1 and GRIA1;
CC       associates GRIA1 with the adaptor protein complex 4 (AP-4) to target
CC       GRIA1 to the somatodendritic compartment of neurons (PubMed:18341993).
CC       {ECO:0000250|UniProtKB:Q8VHX0, ECO:0000269|PubMed:18341993}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=Displays a somatodendritic localization and
CC       is excluded from axons in neurons. {ECO:0000269|PubMed:18341993}.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ272044; CAB86385.1; -; mRNA.
DR   EMBL; CH466531; EDL17281.1; -; Genomic_DNA.
DR   EMBL; BC138673; AAI38674.1; -; mRNA.
DR   EMBL; BC145971; AAI45972.1; -; mRNA.
DR   CCDS; CCDS21816.1; -.
DR   RefSeq; NP_062303.2; NM_019430.2.
DR   AlphaFoldDB; Q9JJV5; -.
DR   SMR; Q9JJV5; -.
DR   BioGRID; 207630; 3.
DR   IntAct; Q9JJV5; 1.
DR   MINT; Q9JJV5; -.
DR   STRING; 10090.ENSMUSP00000081664; -.
DR   GlyGen; Q9JJV5; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9JJV5; -.
DR   PhosphoSitePlus; Q9JJV5; -.
DR   SwissPalm; Q9JJV5; -.
DR   PaxDb; 10090-ENSMUSP00000081664; -.
DR   PeptideAtlas; Q9JJV5; -.
DR   ProteomicsDB; 265607; -.
DR   Antibodypedia; 26064; 270 antibodies from 28 providers.
DR   DNASU; 54376; -.
DR   Ensembl; ENSMUST00000084615.10; ENSMUSP00000081664.3; ENSMUSG00000066189.10.
DR   GeneID; 54376; -.
DR   KEGG; mmu:54376; -.
DR   UCSC; uc009jov.3; mouse.
DR   AGR; MGI:1859165; -.
DR   CTD; 10368; -.
DR   MGI; MGI:1859165; Cacng3.
DR   VEuPathDB; HostDB:ENSMUSG00000066189; -.
DR   eggNOG; ENOG502QVF5; Eukaryota.
DR   GeneTree; ENSGT01050000244893; -.
DR   HOGENOM; CLU_053704_0_1_1; -.
DR   InParanoid; Q9JJV5; -.
DR   OMA; QIHNSIP; -.
DR   OrthoDB; 2957055at2759; -.
DR   PhylomeDB; Q9JJV5; -.
DR   TreeFam; TF327980; -.
DR   Reactome; R-MMU-399719; Trafficking of AMPA receptors.
DR   Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR   BioGRID-ORCS; 54376; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q9JJV5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JJV5; Protein.
DR   Bgee; ENSMUSG00000066189; Expressed in superior frontal gyrus and 57 other cell types or tissues.
DR   ExpressionAtlas; Q9JJV5; baseline and differential.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR   GO; GO:0016247; F:channel regulator activity; IBA:GO_Central.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0099590; P:neurotransmitter receptor internalization; IBA:GO_Central.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IBA:GO_Central.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR   GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IMP:UniProtKB.
DR   GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:UniProtKB.
DR   GO; GO:0019226; P:transmission of nerve impulse; IBA:GO_Central.
DR   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008368; VDCC_gsu.
DR   PANTHER; PTHR12107; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA SUBUNIT; 1.
DR   PANTHER; PTHR12107:SF5; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA-3 SUBUNIT; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   Genevisible; Q9JJV5; MM.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..315
FT                   /note="Voltage-dependent calcium channel gamma-3 subunit"
FT                   /id="PRO_0000164676"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          232..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VHX0"
FT   MUTAGEN         227..240
FT                   /note="YRYRFRRRSSSRST->ARARARRRAAARAA: Decreased
FT                   interaction with AP4M1. Has no effect on interaction with
FT                   GRIA1. Dominant negative mutant which alters AMPARs
FT                   localization to the somatodendritic compartment."
FT                   /evidence="ECO:0000269|PubMed:18341993"
FT   CONFLICT        61
FT                   /note="S -> F (in Ref. 1; CAB86385)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   315 AA;  35516 MW;  FB4EA036C494B6AD CRC64;
     MRMCDRGIQM LITTVGAFAA FSLMTIAVGT DYWLYSRGVC RTKSTSDNET SRKNEEVMTH
     SGLWRTCCLE GAFRGVCKKI DHFPEDADYE QDTAEYLLRA VRASSVFPIL SVTLLFFGGL
     CVAASEFHRS RHSVILSAGI FFVSAGLSNI IGIIVYISAN AGDPGQRDSK KSYSYGWSFY
     FGAFSFIIAE IVGVVAVHIY IEKHQQLRAR SHSELLKKST FARLPPYRYR FRRRSSSRST
     EPRSRDLSPI SKGFHTIPST DISMFTLSRD PSKLTMGTLL NSDRDHAFLQ FHNSTPKEFK
     ESLHNNPANR RTTPV
//