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CCG3_RAT
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   03-AUG-2022, entry version 132.
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   AlphaFoldDB; Q8VHX0; -.
DR   SMR; Q8VHX0; -.
DR   CORUM; Q8VHX0; -.
DR   STRING; 10116.ENSRNOP00000016632; -.
DR   iPTMnet; Q8VHX0; -.
DR   PhosphoSitePlus; Q8VHX0; -.
DR   PaxDb; Q8VHX0; -.
DR   PRIDE; Q8VHX0; -.
DR   Ensembl; ENSRNOT00000016632; ENSRNOP00000016632; ENSRNOG00000012362.
DR   GeneID; 140724; -.
DR   KEGG; rno:140724; -.
DR   UCSC; RGD:628803; rat.
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; NPREPGN; -.
DR   OrthoDB; 1117127at2759; -.
DR   PhylomeDB; Q8VHX0; -.
DR   TreeFam; TF327980; -.
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 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:0099061; C:integral component of postsynaptic density membrane; 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: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: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   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Ion channel; Ion transport;
KW   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"
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
 
 
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