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CCG4_MOUSE
ID   CCG4_MOUSE              Reviewed;         327 AA.
AC   Q9JJV4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Voltage-dependent calcium channel gamma-4 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-4 subunit;
DE   AltName: Full=Transmembrane AMPAR regulatory protein gamma-4;
DE            Short=TARP gamma-4;
GN   Name=Cacng4;
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   TISSUE=Brain;
RX   PubMed=10734232; DOI=10.1016/s0014-5793(00)01306-5;
RA   Klugbauer N., Dai S., Specht V., Lacinova L., Marais E., Bohn G.,
RA   Hofmann F.;
RT   "A family of gamma-like calcium channel subunits.";
RL   FEBS Lett. 470:189-197(2000).
RN   [2]
RP   SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX   PubMed=11389205; DOI=10.1111/j.1469-7793.2001.0467a.x;
RA   Green P.J., Warre R., Hayes P.D., McNaughton N.C., Medhurst A.D.,
RA   Pangalos M., Duckworth D.M., Randall A.D.;
RT   "Kinetic modification of the alpha(1I) subunit-mediated T-type Ca(2+)
RT   channel by a human neuronal Ca(2+) channel gamma subunit.";
RL   J. Physiol. (Lond.) 533:467-478(2001).
RN   [3]
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP   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).
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), including GRIA1 and GRIA4. Promotes their targeting to the
CC       cell membrane and synapses and modulates their gating properties by
CC       slowing their rates of activation, deactivation and desensitization and
CC       by mediating their resensitization (PubMed:17880894).
CC       {ECO:0000250|UniProtKB:Q9UBN1, ECO:0000269|PubMed:17880894}.
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). Interacts with GRIA1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8VHW9, ECO:0000250|UniProtKB:Q9UBN1}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389205};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:11389205}.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ272045; CAB86386.1; -; mRNA.
DR   CCDS; CCDS25571.1; -.
DR   RefSeq; NP_062304.1; NM_019431.2.
DR   AlphaFoldDB; Q9JJV4; -.
DR   SMR; Q9JJV4; -.
DR   STRING; 10090.ENSMUSP00000021066; -.
DR   GlyGen; Q9JJV4; 2 sites.
DR   iPTMnet; Q9JJV4; -.
DR   PhosphoSitePlus; Q9JJV4; -.
DR   PaxDb; Q9JJV4; -.
DR   PRIDE; Q9JJV4; -.
DR   ProteomicsDB; 265608; -.
DR   ABCD; Q9JJV4; 1 sequenced antibody.
DR   Antibodypedia; 19199; 174 antibodies from 28 providers.
DR   DNASU; 54377; -.
DR   Ensembl; ENSMUST00000021066; ENSMUSP00000021066; ENSMUSG00000020723.
DR   GeneID; 54377; -.
DR   KEGG; mmu:54377; -.
DR   UCSC; uc007maz.1; mouse.
DR   CTD; 27092; -.
DR   MGI; MGI:1859167; Cacng4.
DR   VEuPathDB; HostDB:ENSMUSG00000020723; -.
DR   eggNOG; ENOG502QPQH; Eukaryota.
DR   GeneTree; ENSGT01050000244893; -.
DR   HOGENOM; CLU_053704_0_1_1; -.
DR   InParanoid; Q9JJV4; -.
DR   OMA; MGLPMGD; -.
DR   OrthoDB; 1117127at2759; -.
DR   PhylomeDB; Q9JJV4; -.
DR   TreeFam; TF327980; -.
DR   Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
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   BioGRID-ORCS; 54377; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Cacng4; mouse.
DR   PRO; PR:Q9JJV4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9JJV4; protein.
DR   Bgee; ENSMUSG00000020723; Expressed in cortical plate and 147 other tissues.
DR   ExpressionAtlas; Q9JJV4; baseline and differential.
DR   Genevisible; Q9JJV4; MM.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
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; 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; IMP:UniProtKB.
DR   GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
DR   GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IGI:MGI.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR005423; VDCC_g4su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   PANTHER; PTHR12107:SF7; PTHR12107:SF7; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01603; VDCCGAMMA4.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..327
FT                   /note="Voltage-dependent calcium channel gamma-4 subunit"
FT                   /id="PRO_0000164679"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          235..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   327 AA;  36535 MW;  6BFB38B546FBCA86 CRC64;
     MVRCDRGLQM LLTTAGAFAA FSLMAIAIGT DYWLYSSAHI CNGTNLTMDD GPPPRRARGD
     LTHSGLWRVC CIEGIYRGHC FRINHFPEDN DYDHDSSEYL LRIVRASSVF PILSTILLLL
     GGLCIGAGRI YSRKNNIVLS AGILFVAAGL SNIIGIIVYI SSNTGDPSDK RDEDKKNHYN
     YGWSFYFGAL SFIVAETVGV LAVNIYIEKN KELRFKTKRE FLKASSSSPY ARMPSYRYRR
     RRSRSSSRST EASPSRDASP VGLKITGAIP MGELSMYTLS REPLKVTTAA SYSPDQDAGF
     LQMHDFFQQD LKEGFHVSML NRRTTPV
 
 
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