ID CCG3_RAT Reviewed; 315 AA.
AC Q8VHX0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 140.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=11738816; DOI=10.1016/s0378-1119(01)00738-7;
RA Chu P.-J., Robertson H.M., Best P.M.;
RT "Calcium channel gamma subunits provide insights into the evolution of this
RT gene family.";
RL Gene 280:37-48(2001).
RN [2]
RP FUNCTION.
RX PubMed=17880894; DOI=10.1016/j.neuron.2007.08.022;
RA Milstein A.D., Zhou W., Karimzadegan S., Bredt D.S., Nicoll R.A.;
RT "TARP subtypes differentially and dose-dependently control synaptic AMPA
RT receptor gating.";
RL Neuron 55:905-918(2007).
RN [3]
RP FUNCTION.
RX PubMed=19234459; DOI=10.1038/nn.2266;
RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.;
RT "Selective regulation of long-form calcium-permeable AMPA receptors by an
RT atypical TARP, gamma-5.";
RL Nat. Neurosci. 12:277-285(2009).
RN [4]
RP ERRATUM OF PUBMED:19234459.
RX DOI=10.1038/nn0609-808c;
RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.;
RL Nat. Neurosci. 12:808-808(2009).
RN [5]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19265014; DOI=10.1126/science.1167852;
RA Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B.,
RA Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.;
RT "Functional proteomics identify cornichon proteins as auxiliary subunits of
RT AMPA receptors.";
RL Science 323:1313-1319(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates the trafficking to the somatodendritic compartment
CC and gating properties of AMPA-selective glutamate receptors (AMPARs).
CC Promotes their targeting to the cell membrane and synapses and
CC modulates their gating properties by slowing their rates of activation,
CC deactivation and desensitization. Does not show subunit-specific AMPA
CC receptor regulation and regulates all AMPAR subunits. Thought to
CC stabilize the calcium channel in an inactivated (closed) state.
CC {ECO:0000269|PubMed:17880894, ECO:0000269|PubMed:19234459}.
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 (PubMed:19265014). 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JJV5, ECO:0000269|PubMed:19265014}.
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:0000250|UniProtKB:Q9JJV5}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
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DR EMBL; AF361340; AAL50035.1; -; mRNA.
DR RefSeq; NP_542422.1; NM_080691.1.
DR PDB; 7TNJ; EM; 4.02 A; A/B/C/D=5-207.
DR PDB; 7TNK; EM; 4.50 A; A/B/C/D=5-207.
DR PDB; 7TNL; EM; 3.59 A; A/B/C/D=5-207.
DR PDB; 7TNM; EM; 4.74 A; A/B/C/D=5-207.
DR PDB; 7TNP; EM; 3.96 A; A/B/C/D=5-207.
DR PDB; 8C1P; EM; 2.90 A; E/F/G/H=2-315.
DR PDB; 8C1Q; EM; 2.82 A; E/F/G/H=2-315.
DR PDB; 8C2H; EM; 2.64 A; E/F/G/H=2-315.
DR PDB; 8C2I; EM; 2.70 A; E/F/G/H=2-315.
DR PDB; 8P3T; EM; 3.39 A; E/F/G/H=2-315.
DR PDB; 8P3U; EM; 3.77 A; E/F/G/H=2-315.
DR PDB; 8P3V; EM; 3.53 A; E/F/G/H=2-315.
DR PDB; 8P3W; EM; 3.53 A; E/F/G/H=2-315.
DR PDBsum; 7TNJ; -.
DR PDBsum; 7TNK; -.
DR PDBsum; 7TNL; -.
DR PDBsum; 7TNM; -.
DR PDBsum; 7TNP; -.
DR PDBsum; 8C1P; -.
DR PDBsum; 8C1Q; -.
DR PDBsum; 8C2H; -.
DR PDBsum; 8C2I; -.
DR PDBsum; 8P3T; -.
DR PDBsum; 8P3U; -.
DR PDBsum; 8P3V; -.
DR PDBsum; 8P3W; -.
DR AlphaFoldDB; Q8VHX0; -.
DR EMDB; EMD-16379; -.
DR EMDB; EMD-16380; -.
DR EMDB; EMD-16390; -.
DR EMDB; EMD-16391; -.
DR EMDB; EMD-17394; -.
DR EMDB; EMD-17395; -.
DR EMDB; EMD-17396; -.
DR EMDB; EMD-17397; -.
DR SMR; Q8VHX0; -.
DR CORUM; Q8VHX0; -.
DR STRING; 10116.ENSRNOP00000016632; -.
DR iPTMnet; Q8VHX0; -.
DR PhosphoSitePlus; Q8VHX0; -.
DR PaxDb; 10116-ENSRNOP00000016632; -.
DR Ensembl; ENSRNOT00000016632.4; ENSRNOP00000016632.1; ENSRNOG00000012362.4.
DR Ensembl; ENSRNOT00055014238; ENSRNOP00055011429; ENSRNOG00055008418.
DR Ensembl; ENSRNOT00060052336; ENSRNOP00060043557; ENSRNOG00060030131.
DR Ensembl; ENSRNOT00065021407; ENSRNOP00065016565; ENSRNOG00065013062.
DR GeneID; 140724; -.
DR KEGG; rno:140724; -.
DR UCSC; RGD:628803; rat.
DR AGR; RGD:628803; -.
DR CTD; 10368; -.
DR RGD; 628803; Cacng3.
DR eggNOG; ENOG502QVF5; Eukaryota.
DR GeneTree; ENSGT01050000244893; -.
DR HOGENOM; CLU_053704_0_1_1; -.
DR InParanoid; Q8VHX0; -.
DR OMA; QIHNSIP; -.
DR OrthoDB; 2957055at2759; -.
DR PhylomeDB; Q8VHX0; -.
DR TreeFam; TF327980; -.
DR Reactome; R-RNO-399719; Trafficking of AMPA receptors.
DR Reactome; R-RNO-5682910; LGI-ADAM interactions.
DR PRO; PR:Q8VHX0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012362; Expressed in frontal cortex and 3 other cell types or tissues.
DR Genevisible; Q8VHX0; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR GO; GO:0016247; F:channel regulator activity; IBA:GO_Central.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IDA:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
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; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA: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.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Ion channel;
KW Ion transport; 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_0000164677"
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:0007744|PubMed:22673903"
FT HELIX 6..29
FT /evidence="ECO:0007829|PDB:8C2H"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:8C2H"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:8C2H"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:8C2H"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:8C2H"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:8C2H"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:8C2H"
FT HELIX 106..127
FT /evidence="ECO:0007829|PDB:8C2H"
FT HELIX 133..160
FT /evidence="ECO:0007829|PDB:8C2H"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:8C2H"
FT HELIX 177..206
FT /evidence="ECO:0007829|PDB:8C2H"
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
//
