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   24-JAN-2024, entry version 127.
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.ENSMUSP00000113819; -.
DR   BindingDB; Q68EF4; -.
DR   ChEMBL; CHEMBL4105794; -.
DR   GlyConnect; 2509; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q68EF4; 3 sites, 2 glycans.
DR   GlyGen; Q68EF4; 4 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q68EF4; -.
DR   PhosphoSitePlus; Q68EF4; -.
DR   PaxDb; 10090-ENSMUSP00000112578; -.
DR   PeptideAtlas; Q68EF4; -.
DR   ProteomicsDB; 271303; -. [Q68EF4-1]
DR   ProteomicsDB; 271304; -. [Q68EF4-2]
DR   DNASU; 268934; -.
DR   GeneID; 268934; -.
DR   KEGG; mmu:268934; -.
DR   AGR; MGI:1351341; -.
DR   CTD; 2914; -.
DR   MGI; MGI:1351341; Grm4.
DR   eggNOG; KOG1056; Eukaryota.
DR   InParanoid; Q68EF4; -.
DR   OrthoDB; 5388627at2759; -.
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 80 CRISPR screens.
DR   ChiTaRS; Grm4; mouse.
DR   PRO; PR:Q68EF4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q68EF4; Protein.
DR   GO; GO:0150048; C:cerebellar granule cell to Purkinje cell synapse; IDA:SynGO.
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:0043005; C:neuron projection; IDA:BHF-UCL.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
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:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd15452; 7tmC_mGluR4; 1.
DR   CDD; cd06376; PBP1_mGluR_groupIII; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 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   PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR24060:SF23; METABOTROPIC GLUTAMATE RECEPTOR 4; 1.
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; Periplasmic binding protein-like I; 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
//