CCG8_RAT
ID CCG8_RAT Reviewed; 421 AA.
AC Q8VHW5;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 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-251 AND SER-254, AND
RP IDENTIFICATION BY 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 [7]
RP PALMITOYLATION.
RX PubMed=23687301; DOI=10.1074/jbc.m112.431676;
RA Oku S., Takahashi N., Fukata Y., Fukata M.;
RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10
RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to
RT Rab5-positive endosomes.";
RL J. Biol. Chem. 288:19816-19829(2013).
CC -!- FUNCTION: Regulates the activity of L-type calcium channels that
CC contain CACNA1C as pore-forming subunit (By similarity). Regulates the
CC trafficking and gating properties of AMPA-selective glutamate receptors
CC (AMPARs). Promotes their targeting to the cell membrane and synapses
CC and modulates their gating properties by slowing their rates of
CC 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:0000250|UniProtKB:Q8VHW2, ECO:0000269|PubMed:17880894,
CC ECO:0000269|PubMed:19234459}.
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 (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, CACNG2, CACNG3, CACNG4, CACNG5 and CACNG7.
CC Interacts with CNIH2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8VHW2}.
CC -!- INTERACTION:
CC Q8VHW5; P63329: Ppp3ca; NbExp=6; IntAct=EBI-9086576, EBI-7022944;
CC Q8VHW5; Q08209: PPP3CA; Xeno; NbExp=2; IntAct=EBI-9086576, EBI-352922;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VHW2};
CC Multi-pass membrane protein {ECO:0000305}. Postsynaptic density
CC membrane {ECO:0000250|UniProtKB:Q8VHW2}.
CC -!- PTM: Palmitoylated (PubMed:23687301). Probably palmitoylated by ZDHHC3
CC and ZDHHC7 (PubMed:23687301). {ECO:0000269|PubMed:23687301}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF361346; AAL50041.1; -; mRNA.
DR RefSeq; NP_542427.1; NM_080696.2.
DR PDB; 6QKC; EM; 4.10 A; I/J=2-417.
DR PDB; 6QKZ; EM; 6.30 A; I/J=2-417.
DR PDB; 7OCA; EM; 3.40 A; I/J=2-417.
DR PDB; 7OCD; EM; 3.50 A; I/J=2-417.
DR PDB; 7OCE; EM; 3.10 A; I/J=2-417.
DR PDB; 7OCF; EM; 3.60 A; I/J=2-417.
DR PDB; 7QHB; EM; 3.50 A; I/J=2-417.
DR PDB; 7QHH; EM; 3.60 A; I/J=2-417.
DR PDBsum; 6QKC; -.
DR PDBsum; 6QKZ; -.
DR PDBsum; 7OCA; -.
DR PDBsum; 7OCD; -.
DR PDBsum; 7OCE; -.
DR PDBsum; 7OCF; -.
DR PDBsum; 7QHB; -.
DR PDBsum; 7QHH; -.
DR AlphaFoldDB; Q8VHW5; -.
DR SMR; Q8VHW5; -.
DR BioGRID; 250845; 2.
DR CORUM; Q8VHW5; -.
DR IntAct; Q8VHW5; 8.
DR MINT; Q8VHW5; -.
DR STRING; 10116.ENSRNOP00000019300; -.
DR BindingDB; Q8VHW5; -.
DR ChEMBL; CHEMBL4523410; -.
DR iPTMnet; Q8VHW5; -.
DR PhosphoSitePlus; Q8VHW5; -.
DR SwissPalm; Q8VHW5; -.
DR PaxDb; Q8VHW5; -.
DR PRIDE; Q8VHW5; -.
DR ABCD; Q8VHW5; 1 sequenced antibody.
DR GeneID; 140729; -.
DR KEGG; rno:140729; -.
DR UCSC; RGD:628808; rat.
DR CTD; 59283; -.
DR RGD; 628808; Cacng8.
DR eggNOG; ENOG502QUEC; Eukaryota.
DR InParanoid; Q8VHW5; -.
DR OrthoDB; 1117127at2759; -.
DR PhylomeDB; Q8VHW5; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-RNO-5576893; Phase 2 - plateau phase.
DR Reactome; R-RNO-5682910; LGI-ADAM interactions.
DR PRO; PR:Q8VHW5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
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; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; 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:0030346; F:protein phosphatase 2B binding; IPI: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:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IBA:GO_Central.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; 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; 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; ISO:RGD.
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..421
FT /note="Voltage-dependent calcium channel gamma-8 subunit"
FT /id="PRO_0000164692"
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..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT HELIX 17..40
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 129..148
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 158..183
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:7OCD"
FT HELIX 203..239
FT /evidence="ECO:0007829|PDB:7OCE"
SQ SEQUENCE 421 AA; 43269 MW; 0FDB1461BDC780A9 CRC64;
MESLKRWNEE RGLWCEKGVQ VLLTTIGAFA 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 GLASAGGGGG GAGVGAYGGA AGAAGGGGTG SERDRGSSAG
FLTLHNAFPK EAASGVTVTV TGPPAAPAPA PPAPAAPAPG TLSKEAAASN TNTLNRKTTP
V
