CCG2_RAT
ID CCG2_RAT Reviewed; 323 AA.
AC Q71RJ2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Voltage-dependent calcium channel gamma-2 subunit;
DE AltName: Full=Neuronal voltage-gated calcium channel gamma-2 subunit;
DE AltName: Full=Stargazin {ECO:0000303|PubMed:27756895};
DE AltName: Full=Transmembrane AMPAR regulatory protein gamma-2;
DE Short=TARP gamma-2 {ECO:0000303|PubMed:27756895};
GN Name=Cacng2 {ECO:0000312|RGD:71095}; Synonyms=Stg {ECO:0000305};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034;
RA Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.;
RT "AMPA receptor subunit-specific regulation by a distinct family of type II
RT TARPs.";
RL Neuron 59:986-996(2008).
RN [5]
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 [6]
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 [7]
RP FUNCTION, 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 [8]
RP FUNCTION, AND INTERACTION WITH GRIA1.
RX PubMed=20805473; DOI=10.1073/pnas.1011706107;
RA Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W.,
RA Nicoll R.A.;
RT "Functional comparison of the effects of TARPs and cornichons on AMPA
RT receptor trafficking and gating.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, 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).
RN [10]
RP INTERACTION WITH DLG4; GRIA2 AND MPP2, AND SUBCELLULAR LOCATION.
RX PubMed=27756895; DOI=10.1038/srep35283;
RA Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
RT "MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
RT adhesion molecules to core components of the postsynaptic density.";
RL Sci. Rep. 6:35283-35283(2016).
CC -!- FUNCTION: Regulates the trafficking and gating properties of AMPA-
CC selective glutamate receptors (AMPARs). Promotes their targeting to the
CC cell membrane and synapses and modulates their gating properties by
CC slowing their rates of activation, deactivation and desensitization.
CC Does not show subunit-specific AMPA receptor regulation and regulates
CC all AMPAR subunits. Thought to stabilize the calcium channel in an
CC inactivated (closed) state. {ECO:0000269|PubMed:17880894,
CC ECO:0000269|PubMed:18817736, ECO:0000269|PubMed:19234459,
CC ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:20805473}.
CC -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC alpha-1, alpha-2/delta, beta and gamma. Interacts with the PDZ domains
CC of DLG4/PSD-95 and DLG1/SAP97 (PubMed:27756895). May interact with GOPC
CC (By similarity). Acts as an auxiliary subunit for AMPA-selective
CC glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2,
CC GRIA3, GRIA4, CNIH2, CNIH3, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8.
CC Interacts with GRIA1 and GRIA2 (PubMed:27756895). Interacts with MPP2
CC (PubMed:27756895). {ECO:0000250|UniProtKB:Q9Y698,
CC ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:20805473,
CC ECO:0000269|PubMed:27756895}.
CC -!- INTERACTION:
CC Q71RJ2; P31016: Dlg4; NbExp=2; IntAct=EBI-8538384, EBI-375655;
CC Q71RJ2; P19490: Gria1; NbExp=7; IntAct=EBI-8538384, EBI-371642;
CC Q71RJ2; P19491: Gria2; NbExp=2; IntAct=EBI-8538384, EBI-77718;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Synapse,
CC synaptosome {ECO:0000269|PubMed:27756895}.
CC -!- PTM: Phosphorylation of Thr-321 by PKA impairs interaction with DLG1
CC and DLG4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
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DR EMBL; AF361339; AAL50034.1; -; mRNA.
DR EMBL; CH473950; EDM15892.1; -; Genomic_DNA.
DR RefSeq; NP_445803.1; NM_053351.1.
DR PDB; 5KK2; EM; 7.30 A; E/F/G/H=1-323.
DR PDB; 5VOT; EM; 4.90 A; E/F/G/H=1-323.
DR PDB; 5VOU; EM; 6.40 A; E/F/G/H=1-323.
DR PDB; 5VOV; EM; 7.70 A; E/F/G/H=1-323.
DR PDB; 6NJL; EM; 6.70 A; F/H=1-323.
DR PDB; 6NJM; EM; 6.50 A; F/H=1-323.
DR PDB; 6NJN; EM; 6.50 A; F/H=1-323.
DR PDBsum; 5KK2; -.
DR PDBsum; 5VOT; -.
DR PDBsum; 5VOU; -.
DR PDBsum; 5VOV; -.
DR PDBsum; 6NJL; -.
DR PDBsum; 6NJM; -.
DR PDBsum; 6NJN; -.
DR AlphaFoldDB; Q71RJ2; -.
DR SMR; Q71RJ2; -.
DR CORUM; Q71RJ2; -.
DR DIP; DIP-41720N; -.
DR IntAct; Q71RJ2; 7.
DR MINT; Q71RJ2; -.
DR STRING; 10116.ENSRNOP00000008414; -.
DR ChEMBL; CHEMBL4523358; -.
DR GlyGen; Q71RJ2; 1 site.
DR iPTMnet; Q71RJ2; -.
DR PhosphoSitePlus; Q71RJ2; -.
DR SwissPalm; Q71RJ2; -.
DR PaxDb; Q71RJ2; -.
DR PRIDE; Q71RJ2; -.
DR ABCD; Q71RJ2; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000106728; ENSRNOP00000085982; ENSRNOG00000065511.
DR GeneID; 84347; -.
DR KEGG; rno:84347; -.
DR UCSC; RGD:71095; rat.
DR CTD; 10369; -.
DR RGD; 71095; Cacng2.
DR eggNOG; ENOG502QSNI; Eukaryota.
DR GeneTree; ENSGT01050000244893; -.
DR HOGENOM; CLU_053704_0_1_1; -.
DR InParanoid; Q71RJ2; -.
DR OMA; CIQKESK; -.
DR PhylomeDB; Q71RJ2; -.
DR TreeFam; TF327980; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-RNO-5682910; LGI-ADAM interactions.
DR PRO; PR:Q71RJ2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000006226; Expressed in cerebellum and 2 other tissues.
DR Genevisible; Q71RJ2; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005246; F:calcium channel regulator activity; NAS:RGD.
DR GO; GO:0016247; F:channel regulator activity; IBA:GO_Central.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0060082; P:eye blink reflex; IEP:RGD.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR GO; GO:0060081; P:membrane hyperpolarization; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0099590; P:neurotransmitter receptor internalization; ISO:RGD.
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; ISO:RGD.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; IDA:RGD.
DR GO; GO:1904510; P:positive regulation of protein localization to basolateral plasma membrane; IDA:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; ISO:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; IDA:RGD.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR005422; VDCC_g2su.
DR InterPro; IPR008368; VDCC_gsu.
DR PANTHER; PTHR12107:SF1; PTHR12107:SF1; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01602; VDCCGAMMA2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Synapse; Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..323
FT /note="Voltage-dependent calcium channel gamma-2 subunit"
FT /id="PRO_0000408973"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 233..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 271
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88602"
FT MOD_RES 321
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O88602"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 323 AA; 35895 MW; AA9D475606A0FBA4 CRC64;
MGLFDRGVQM LLTTVGAFAA FSLMTIAVGT DYWLYSRGVC KTKSVSENET SKKNEEVMTH
SGLWRTCCLE GNFKGLCKQI DHFPEDADYE ADTAEYFLRA VRASSIFPIL SVILLFMGGL
CIAASEFYKT RHNIILSAGI FFVSAGLSNI IGIIVYISAN AGDPSKSDSK KNSYSYGWSF
YFGALSFIIA EMVGVLAVHM FIDRHKQLRA TARATDYLQA SAITRIPSYR YRYQRRSRSS
SRSTEPSHSR DASPVGVKGF NTLPSTEISM YTLSRDPLKA ATTPTATYNS DRDNSFLQVH
NCIQKDSKDS LHANTANRRT TPV
