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