CCG4_RAT
ID CCG4_RAT Reviewed; 327 AA.
AC Q8VHW9;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 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, SUBCELLULAR LOCATION, AND SUBUNIT.
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, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, 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 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, PubMed:19234459).
CC {ECO:0000250|UniProtKB:Q9UBN1, 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) (PubMed:17880894, PubMed:19234459).
CC Interacts with GRIA1 (PubMed:17880894). {ECO:0000250|UniProtKB:Q9UBN1,
CC ECO:0000269|PubMed:17880894, ECO:0000269|PubMed:19234459}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17880894};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in heart left ventricle.
CC {ECO:0000269|PubMed:21127204}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
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DR EMBL; AF361341; AAL50036.1; -; mRNA.
DR RefSeq; NP_542423.1; NM_080692.1.
DR AlphaFoldDB; Q8VHW9; -.
DR SMR; Q8VHW9; -.
DR CORUM; Q8VHW9; -.
DR STRING; 10116.ENSRNOP00000004383; -.
DR GlyGen; Q8VHW9; 2 sites.
DR iPTMnet; Q8VHW9; -.
DR PhosphoSitePlus; Q8VHW9; -.
DR PaxDb; Q8VHW9; -.
DR PRIDE; Q8VHW9; -.
DR ABCD; Q8VHW9; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000004383; ENSRNOP00000004383; ENSRNOG00000003262.
DR GeneID; 140725; -.
DR KEGG; rno:140725; -.
DR UCSC; RGD:628804; rat.
DR CTD; 27092; -.
DR RGD; 628804; Cacng4.
DR eggNOG; ENOG502QPQH; Eukaryota.
DR GeneTree; ENSGT01050000244893; -.
DR HOGENOM; CLU_053704_0_1_1; -.
DR InParanoid; Q8VHW9; -.
DR OMA; MGLPMGD; -.
DR OrthoDB; 1117127at2759; -.
DR PhylomeDB; Q8VHW9; -.
DR TreeFam; TF327980; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
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:Q8VHW9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003262; Expressed in frontal cortex and 9 other tissues.
DR Genevisible; Q8VHW9; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0009986; C:cell surface; 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; IDA:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; 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: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:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IDA:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
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_0000164680"
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 226..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 36523 MW; 7205476FD8823AD6 CRC64;
MVRCDRGLQM LLTTAGAFAA FSLMAIAIGT DYWLYSSAHI CNGTNLTMDD GPPPRRARGD
LTHSGLWRVC CIEGIYKGHC FRINHFPEDN DYDHDSSEYL LRIVRASSVF PILSTILLLL
GGLCIGAGRI YSRKNNIVLS AGILFVAAGL SNIIGIIVYI SSNTGDPSDK RDEDKKNHYN
YGWSFYFGAL SFIVAETVGV LAVNIYIEKN KELRFKTKRE FLKASSSSPY SRMPSYRYRR
RRSRSSSRST EASPSRDASP VGLKITGAIP MGELSMYTLS REPLKVTTAA SYSPDQDAGF
LQMHDFFQQD LKEGFHVSML NRRTTPV
