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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}.
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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
 
 
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