CCG8_MOUSE
ID CCG8_MOUSE Reviewed; 423 AA.
AC Q8VHW2;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Voltage-dependent calcium channel gamma-8 subunit;
DE AltName: Full=Neuronal voltage-gated calcium channel gamma-8 subunit;
DE AltName: Full=Transmembrane AMPAR regulatory protein gamma-8;
DE Short=TARP gamma-8;
GN Name=Cacng8;
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 STRAIN=BALB/cJ;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CNIH2.
RX PubMed=21172611; DOI=10.1016/j.neuron.2010.11.026;
RA Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H.,
RA Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.;
RT "Hippocampal AMPA receptor gating controlled by both TARP and cornichon
RT proteins.";
RL Neuron 68:1082-1096(2010).
RN [4]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CACNA1C, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21127204; DOI=10.1096/fj.10-172353;
RA Yang L., Katchman A., Morrow J.P., Doshi D., Marx S.O.;
RT "Cardiac L-type calcium channel (Cav1.2) associates with gamma subunits.";
RL FASEB J. 25:928-936(2011).
CC -!- FUNCTION: Regulates the activity of L-type calcium channels that
CC contain CACNA1C as pore-forming subunit (PubMed:21127204). Regulates
CC the trafficking and gating properties of AMPA-selective glutamate
CC receptors (AMPARs). 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 and by mediating their
CC resensitization. Does not show subunit-specific AMPA receptor
CC regulation and regulates all AMPAR subunits. Thought to stabilize the
CC calcium channel in an inactivated (closed) state.
CC {ECO:0000269|PubMed:21127204, ECO:0000269|PubMed:21172611}.
CC -!- SUBUNIT: Interacts with CACNA1C. Identified in a complex with the L-
CC type calcium channel subunits CACNA1C, CACNA2D1 and either CACNB1 or
CC CACNB2 (PubMed:21127204). Acts as an auxiliary subunit for AMPA-
CC selective glutamate receptors (AMPARs). Found in a complex with GRIA1,
CC GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5 and
CC CACNG7. Interacts with CNIH2. {ECO:0000269|PubMed:21127204,
CC ECO:0000269|PubMed:21172611}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21127204,
CC ECO:0000305|PubMed:21172611}; Multi-pass membrane protein
CC {ECO:0000250}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:21172611}.
CC -!- PTM: Palmitoylated. Probably palmitoylated by ZDHHC3 and ZDHHC7.
CC {ECO:0000250|UniProtKB:Q8VHW5}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
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DR EMBL; AF361350; AAL50045.1; -; mRNA.
DR CCDS; CCDS57471.1; -.
DR PDB; 7LDD; EM; 3.40 A; G/H=1-423.
DR PDB; 7LDE; EM; 3.90 A; G/H=1-423.
DR PDB; 7LEP; EM; 3.25 A; G/H=19-233.
DR PDBsum; 7LDD; -.
DR PDBsum; 7LDE; -.
DR PDBsum; 7LEP; -.
DR AlphaFoldDB; Q8VHW2; -.
DR SMR; Q8VHW2; -.
DR IntAct; Q8VHW2; 1.
DR STRING; 10090.ENSMUSP00000138618; -.
DR iPTMnet; Q8VHW2; -.
DR PhosphoSitePlus; Q8VHW2; -.
DR SwissPalm; Q8VHW2; -.
DR MaxQB; Q8VHW2; -.
DR PaxDb; Q8VHW2; -.
DR PRIDE; Q8VHW2; -.
DR ProteomicsDB; 265721; -.
DR ABCD; Q8VHW2; 1 sequenced antibody.
DR UCSC; uc029wda.2; mouse.
DR MGI; MGI:1932376; Cacng8.
DR eggNOG; ENOG502QUEC; Eukaryota.
DR InParanoid; Q8VHW2; -.
DR PhylomeDB; Q8VHW2; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR ChiTaRS; Cacng8; mouse.
DR PRO; PR:Q8VHW2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VHW2; protein.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0005246; F:calcium channel regulator activity; 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:0030346; F:protein phosphatase 2B 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:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IBA:GO_Central.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; ISO:MGI.
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:2000311; P:regulation of AMPA receptor activity; IDA:UniProtKB.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR GO; GO:0019226; P:transmission of nerve impulse; IBA:GO_Central.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR008372; VDCC_g8su.
DR InterPro; IPR008368; VDCC_gsu.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01796; VDCCGAMMA8.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..423
FT /note="Voltage-dependent calcium channel gamma-8 subunit"
FT /id="PRO_0000164691"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 271..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 129..149
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 157..183
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 204..231
FT /evidence="ECO:0007829|PDB:7LEP"
SQ SEQUENCE 423 AA; 43453 MW; D3AD13E18F9EB02D CRC64;
MESLKRWNEE RGLWCEKGVQ VLLTTIGAFS AFGLMTIAIS TDYWLYTRAL ICNTTNLTAG
DDGPPHRGGS GSSEKKDPGG LTHSGLWRIC CLEGLKRGVC VKINHFPEDT DYDHDSAEYL
LRVVRASSIF PILSAILLLL GGVCVAASRV YKSKRNIILG AGILFVAAGL SNIIGVIVYI
SANAGEPGPK RDEEKKNHYS YGWSFYFGGL SFILAEVIGV LAVNIYIERS REAHCQSRSD
LLKAGGGAGG SGGSGPSAIL RLPSYRFRYR RRSRSSSRGS SEASPSRDAS PGGPGGPGFA
STDISMYTLS RDPSKGSVAA GLASAGGGGS GAGVGAYGGA AGAAGGGGAG SERDRGSSAG
FLTLHNAFPK EAASGVTVTV TGPPAAPAPA PAPPAPAAPA PGTLSKEAAA SNTNTLNRKT
TPV
