GRM4_RAT
ID GRM4_RAT Reviewed; 912 AA.
AC P31423;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Metabotropic glutamate receptor 4;
DE Short=mGluR4;
DE Flags: Precursor;
GN Name=Grm4; Synonyms=Gprc1d, Mglur4;
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 TISSUE=Brain;
RX PubMed=1309649; DOI=10.1016/0896-6273(92)90118-w;
RA Tanabe Y., Masu M., Ishii T., Shigemoto R., Nakanishi S.;
RT "A family of metabotropic glutamate receptors.";
RL Neuron 8:169-179(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8338667; DOI=10.1016/0896-6273(93)90269-w;
RA O'Hara P.J., Sheppard P.O., Thoegersen H., Venezia D., Haldeman B.A.,
RA McGrane V., Houamed K.M., Thomsen C., Gilbert T.L., Mulvihill E.R.;
RT "The ligand-binding domain in metabotropic glutamate receptors is related
RT to bacterial periplasmic binding proteins.";
RL Neuron 11:41-52(1993).
RN [3]
RP PROTEIN SEQUENCE OF 347-357 AND 686-692, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH PICK1.
RX PubMed=11122333; DOI=10.1046/j.1460-9568.2000.01309.x;
RA El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H.;
RT "Interaction of the C-terminal tail region of the metabotropic glutamate
RT receptor 7 with the protein kinase C substrate PICK1.";
RL Eur. J. Neurosci. 12:4215-4221(2000).
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 -!- SUBUNIT: Interacts with PICK1. {ECO:0000269|PubMed:11122333}.
CC -!- INTERACTION:
CC P31423; O08599-1: Stxbp1; Xeno; NbExp=2; IntAct=EBI-7974891, EBI-15809216;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Is widely distributed in the CNS. Predominant
CC expression is seen in the granule cells of the cerebellum.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; M92077; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M90518; AAA93190.1; -; mRNA.
DR PIR; JH0563; JH0563.
DR RefSeq; NP_073157.1; NM_022666.1.
DR AlphaFoldDB; P31423; -.
DR SMR; P31423; -.
DR BioGRID; 246582; 5.
DR DIP; DIP-41144N; -.
DR IntAct; P31423; 5.
DR MINT; P31423; -.
DR STRING; 10116.ENSRNOP00000060812; -.
DR BindingDB; P31423; -.
DR ChEMBL; CHEMBL2787; -.
DR DrugCentral; P31423; -.
DR GuidetoPHARMACOLOGY; 292; -.
DR GlyGen; P31423; 5 sites.
DR iPTMnet; P31423; -.
DR PhosphoSitePlus; P31423; -.
DR SwissPalm; P31423; -.
DR PaxDb; P31423; -.
DR PRIDE; P31423; -.
DR Ensembl; ENSRNOT00000093633; ENSRNOP00000082873; ENSRNOG00000000487.
DR GeneID; 24417; -.
DR KEGG; rno:24417; -.
DR UCSC; RGD:2745; rat.
DR CTD; 2914; -.
DR RGD; 2745; Grm4.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR InParanoid; P31423; -.
DR OrthoDB; 483746at2759; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR PRO; PR:P31423; -.
DR Proteomes; UP000002494; Chromosome 20.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:UniProtKB.
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; IPI:RGD.
DR GO; GO:0005516; F:calmodulin binding; IPI:RGD.
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:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; TAS:UniProtKB.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; TAS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; TAS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; NAS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; TAS:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; TAS:UniProtKB.
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 Cell membrane; Direct protein sequencing; 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_0000012931"
FT TOPO_DOM 33..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..610
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..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..656
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..675
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..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..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..772
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..808
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..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 CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
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 CONFLICT 124
FT /note="Q -> R (in Ref. 2; AAA93190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 912 AA; 101819 MW; 336430EF19B4B577 CRC64;
MSGKGGWAWW WARLPLCLLL SLYAPWVPSS LGKPKGHPHM NSIRIDGDIT LGGLFPVHGR
GSEGKACGEL KKEKGIHRLE AMLFALDRIN NDPDLLPNIT LGARILDTCS RDTHALEQSL
TFVQALIEKD GTEVRCGSGG PPIITKPERV VGVIGASGSS VSIMVANILR LFKIPQISYA
STAPDLSDNS RYDFFSRVVP SDTYQAQAMV DIVRALKWNY VSTLASEGSY GESGVEAFIQ
KSRENGGVCI AQSVKIPREP KTGEFDKIIK RLLETSNARG IIIFANEDDI RRVLEAARRA
NQTGHFFWMG SDSWGSKSAP VLRLEEVAEG AVTILPKRMS VRGFDRYFSS RTLDNNRRNI
WFAEFWEDNF HCKLSRHALK KGSHIKKCTN RERIGQDSAY EQEGKVQFVI DAVYAMGHAL
HAMHRDLCPG RVGLCPRMDP VDGTQLLKYI RNVNFSGIAG NPVTFNENGD APGRYDIYQY
QLRNGSAEYK VIGSWTDHLH LRIERMQWPG SGQQLPRSIC SLPCQPGERK KTVKGMACCW
HCEPCTGYQY QVDRYTCKTC PYDMRPTENR TSCQPIPIVK LEWDSPWAVL PLFLAVVGIA
ATLFVVVTFV RYNDTPIVKA SGRELSYVLL AGIFLCYATT FLMIAEPDLG TCSLRRIFLG
LGMSISYAAL LTKTNRIYRI FEQGKRSVSA PRFISPASQL AITFILISLQ LLGICVWFVV
DPSHSVVDFQ DQRTLDPRFA RGVLKCDISD LSLICLLGYS MLLMVTCTVY AIKTRGVPET
FNEAKPIGFT MYTTCIVWLA FIPIFFGTSQ SADKLYIQTT TLTVSVSLSA SVSLGMLYMP
KVYIILFHPE QNVPKRKRSL KAVVTAATMS NKFTQKGNFR PNGEAKSELC ENLETPALAT
KQTYVTYTNH AI
