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CCG7_RAT
ID   CCG7_RAT                Reviewed;         275 AA.
AC   P62957; Q8VBX3; Q8WXS6; Q9BXT1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Voltage-dependent calcium channel gamma-7 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-7 subunit;
DE   AltName: Full=Transmembrane AMPAR regulatory protein gamma-7;
DE            Short=TARP gamma-7;
GN   Name=Cacng7;
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], AND TISSUE SPECIFICITY.
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=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   [3]
RP   FUNCTION, AND SUBUNIT.
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   TISSUE SPECIFICITY.
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).
RN   [7]
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).
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 (PubMed:18817736, PubMed:19234459). Shows specificity
CC       only for GRIA1 and GRIA2 (By similarity).
CC       {ECO:0000250|UniProtKB:P62955, ECO:0000269|PubMed:18817736,
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), such as GRIA1 and GRIA2 (PubMed:19234459,
CC       PubMed:19265014). {ECO:0000250|UniProtKB:P62955,
CC       ECO:0000269|PubMed:19234459, ECO:0000269|PubMed:19265014}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung and testis.
CC       {ECO:0000269|PubMed:11738816}.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF361345; AAL50040.1; -; mRNA.
DR   RefSeq; NP_542426.1; NM_080695.1.
DR   RefSeq; XP_006228075.1; XM_006228013.3.
DR   AlphaFoldDB; P62957; -.
DR   SMR; P62957; -.
DR   CORUM; P62957; -.
DR   STRING; 10116.ENSRNOP00000019683; -.
DR   iPTMnet; P62957; -.
DR   PhosphoSitePlus; P62957; -.
DR   PaxDb; P62957; -.
DR   Ensembl; ENSRNOT00000089944; ENSRNOP00000069074; ENSRNOG00000056257.
DR   GeneID; 140728; -.
DR   KEGG; rno:140728; -.
DR   UCSC; RGD:628807; rat.
DR   CTD; 59284; -.
DR   RGD; 628807; Cacng7.
DR   eggNOG; ENOG502QTQ7; Eukaryota.
DR   GeneTree; ENSGT01050000244961; -.
DR   HOGENOM; CLU_053704_1_1_1; -.
DR   InParanoid; P62957; -.
DR   OMA; RPRMSNC; -.
DR   OrthoDB; 1093662at2759; -.
DR   PhylomeDB; P62957; -.
DR   TreeFam; TF327980; -.
DR   Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-RNO-5576893; Phase 2 - plateau phase.
DR   PRO; PR:P62957; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000056257; Expressed in cerebellum and 12 other tissues.
DR   Genevisible; P62957; RN.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR   GO; GO:0044300; C:cerebellar mossy fiber; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005769; C:early endosome; 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:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
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: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:1903861; P:positive regulation of dendrite extension; IMP: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:0043488; P:regulation of mRNA stability; IMP:RGD.
DR   GO; GO:0019226; P:transmission of nerve impulse; IBA:GO_Central.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008371; VDCC_g7su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   PANTHER; PTHR12107:SF12; PTHR12107:SF12; 1.
DR   Pfam; PF13903; Claudin_2; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01795; VDCCGAMMA7.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..275
FT                   /note="Voltage-dependent calcium channel gamma-7 subunit"
FT                   /id="PRO_0000164689"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62956"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62956"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62956"
SQ   SEQUENCE   275 AA;  31003 MW;  43CC82B9FA6A5C73 CRC64;
     MSHCSSRALT LLSSVFGACG LLLVGIAVST DYWLYMEEGT VLPQNQTTEV KMALHAGLWR
     VCFFAGREKG RCVASEYFLE PEINLVTENT ENILKTVRTA TPFPMVSLFL VFTAFVISNI
     GHIRPQRTIL AFVSGIFFIL SGLSLVVGLV LYISSINDEV MNRPSSSEQY FHYRYGWSFA
     FAASSFLLKE GAGVMSVYLF TKRYAEEEMY RPHPAFYRPR LSDCSDYSGQ FLQPEAWRRG
     RSPSDISSDV SIQMTQNYPP AIKYPDHLHI STSPC
 
 
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