GRM4_MOUSE
ID GRM4_MOUSE Reviewed; 912 AA.
AC Q68EF4; Q80UC2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Metabotropic glutamate receptor 4;
DE Short=mGluR4;
DE Flags: Precursor;
GN Name=Grm4; Synonyms=Gprc1d, Mglur4;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-642.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [3]
RP IDENTIFICATION BY 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: G-protein coupled receptor for glutamate. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors. Signaling inhibits adenylate cyclase activity
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PICK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68EF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68EF4-2; Sequence=VSP_028517, VSP_028518;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; BC072635; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC080284; AAH80284.1; -; mRNA.
DR EMBL; AY255558; AAO85070.1; -; mRNA.
DR CCDS; CCDS28563.1; -. [Q68EF4-2]
DR CCDS; CCDS70775.1; -. [Q68EF4-1]
DR RefSeq; NP_001013403.1; NM_001013385.2.
DR AlphaFoldDB; Q68EF4; -.
DR SMR; Q68EF4; -.
DR BioGRID; 234582; 4.
DR DIP; DIP-49002N; -.
DR IntAct; Q68EF4; 2.
DR STRING; 10090.ENSMUSP00000112578; -.
DR BindingDB; Q68EF4; -.
DR ChEMBL; CHEMBL4105794; -.
DR GlyConnect; 2509; 2 N-Linked glycans (1 site).
DR GlyGen; Q68EF4; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q68EF4; -.
DR PhosphoSitePlus; Q68EF4; -.
DR PaxDb; Q68EF4; -.
DR PeptideAtlas; Q68EF4; -.
DR PRIDE; Q68EF4; -.
DR ProteomicsDB; 271303; -. [Q68EF4-1]
DR ProteomicsDB; 271304; -. [Q68EF4-2]
DR DNASU; 268934; -.
DR GeneID; 268934; -.
DR KEGG; mmu:268934; -.
DR CTD; 2914; -.
DR MGI; MGI:1351341; Grm4.
DR eggNOG; KOG1056; Eukaryota.
DR InParanoid; Q68EF4; -.
DR PhylomeDB; Q68EF4; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR BioGRID-ORCS; 268934; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Grm4; mouse.
DR PRO; PR:Q68EF4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q68EF4; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; TAS:MGI.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR001786; GPCR_3_mGluR4.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01054; MTABOTROPC4R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..912
FT /note="Metabotropic glutamate receptor 4"
FT /id="PRO_0000306852"
FT TOPO_DOM 33..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..671
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 180..182
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT /evidence="ECO:0000250"
FT DISULFID 249..538
FT /evidence="ECO:0000250"
FT DISULFID 372..388
FT /evidence="ECO:0000250"
FT DISULFID 428..435
FT /evidence="ECO:0000250"
FT DISULFID 520..539
FT /evidence="ECO:0000250"
FT DISULFID 524..542
FT /evidence="ECO:0000250"
FT DISULFID 545..557
FT /evidence="ECO:0000250"
FT DISULFID 560..573
FT /evidence="ECO:0000250"
FT VAR_SEQ 815..832
FT /note="LYIQTTTLTVSVSLSASV -> VTSEALPVEFSPPLLAHN (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028517"
FT VAR_SEQ 833..912
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028518"
FT CONFLICT 713
FT /note="C -> G (in Ref. 1; AAH80284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 912 AA; 101824 MW; 5D73C6423CF4E38C CRC64;
MSGKGGWAWW WARLPLCLLL SLYGSWVPSS LGKPKGHPHM NSIRIDGDIT LGGLFPVHGR
GSEGKACGEL KKEKGIHRLE AMLFALDRIN NDPDLLPNIT LGARILDTCS RDTHALEQSL
TFVQALIEKD GTEVRCGSGG PPIITKPERV VGVIGASGSS VSIMVANILR LFKIPQISYA
STAPDLSDNS RYDFFSRVVP SDTYQAQAMV DIVRALKWNY VSTLASEGSY GESGVEAFIQ
KSRENGGVCI AQSVKIPREP KTGEFDKIIK RLLETSNARA IIIFANEDDI RRVLEAARRA
NQTGHFFWMG SDSWGSKSAP VLRLEEVAEG AVTILPKRTS VRGFDRYFSS RTLDNNRRNI
WFAEFWEDNF HCKLSRHALK KGSHIKKCTN RERIGQDSAY EQEGKVQFVI DAVYAMGHAL
HAMHRDLCPG RVGLCPRMDP VDGTQLLKYI RNVNFSGIAG NPVTFNENGD APGRYDIYQY
QRRNGSAEYK VIGSWTDHLH LRIERMQWPG SGQQLPRSIC SLPCQPGERK KTVKGMACCW
HCEPCTGYQY QVDRYTCKTC PYDMRPTENR TSCQPIPIVK LEWDSPWAVL PLFLAVVGIA
ATLFVVVTFV RYNDTPIVKA SGRELSYVLL AGIFLCYATT FLMIAEPDLG TCSLRRIFLG
LGMSISYAAL LTKTNRIYRI FEQGKRSVSA PRFISPASQL AITFVLISLQ LLCICVWFVV
DPSHSVVDFQ DQRTLDPRFA RGVLKCDISD LSLICLLGYS MLLMVTCTVY AIKTRGVPET
FNEAKPIGFT MYTTCIVWLA FIPIFFGTSQ SADKLYIQTT TLTVSVSLSA SVSLGMLYMP
KVYIILFHPE QNVPKRKRSL KAVVTAATMS NKFTQKGNFR PNGEAKSELC ENLEAPALAT
KQTYVTYTNH AI
