ID GRM2_RAT Reviewed; 872 AA.
AC P31421;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 24-JAN-2024, entry version 179.
DE RecName: Full=Metabotropic glutamate receptor 2;
DE Short=mGluR2;
DE Flags: Precursor;
GN Name=Grm2; Synonyms=Gprc1b, Mglur2;
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 INTERACTION WITH TAMALIN.
RX PubMed=11850456; DOI=10.1523/jneurosci.22-04-01280.2002;
RA Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y.,
RA Nakanishi S.;
RT "Tamalin, a PDZ domain-containing protein, links a protein complex
RT formation of group 1 metabotropic glutamate receptors and the guanine
RT nucleotide exchange factor cytohesins.";
RL J. Neurosci. 22:1280-1289(2002).
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 May mediate suppression of neurotransmission or may be involved in
CC synaptogenesis or synaptic stabilization.
CC -!- SUBUNIT: Interacts with HTR2A (By similarity). Interacts with TAMALIN.
CC {ECO:0000250, ECO:0000269|PubMed:11850456}.
CC -!- INTERACTION:
CC P31421; P14842: Htr2a; NbExp=3; IntAct=EBI-7090147, EBI-7090176;
CC P31421; Q96S59: RANBP9; Xeno; NbExp=4; IntAct=EBI-7090147, EBI-636085;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Synapse {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Is widely distributed in the CNS and prominent
CC expression is seen in Golgi cells of the cerebellum and some particular
CC neuronal cells in other brain regions.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; M92075; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JH0561; JH0561.
DR RefSeq; NP_001099181.1; NM_001105711.1.
DR RefSeq; XP_017450945.1; XM_017595456.1.
DR RefSeq; XP_017450946.1; XM_017595457.1.
DR AlphaFoldDB; P31421; -.
DR SMR; P31421; -.
DR BioGRID; 246580; 3.
DR DIP; DIP-41937N; -.
DR IntAct; P31421; 2.
DR MINT; P31421; -.
DR STRING; 10116.ENSRNOP00000017607; -.
DR BindingDB; P31421; -.
DR ChEMBL; CHEMBL2851; -.
DR DrugCentral; P31421; -.
DR GuidetoPHARMACOLOGY; 290; -.
DR GlyCosmos; P31421; 5 sites, No reported glycans.
DR GlyGen; P31421; 5 sites.
DR iPTMnet; P31421; -.
DR PhosphoSitePlus; P31421; -.
DR PaxDb; 10116-ENSRNOP00000017607; -.
DR Ensembl; ENSRNOT00000017607.4; ENSRNOP00000017607.2; ENSRNOG00000013171.4.
DR Ensembl; ENSRNOT00055020073; ENSRNOP00055016160; ENSRNOG00055011818.
DR Ensembl; ENSRNOT00060030031; ENSRNOP00060024237; ENSRNOG00060017564.
DR Ensembl; ENSRNOT00065013122; ENSRNOP00065009696; ENSRNOG00065008268.
DR GeneID; 24415; -.
DR KEGG; rno:24415; -.
DR UCSC; RGD:2743; rat.
DR AGR; RGD:2743; -.
DR CTD; 2912; -.
DR RGD; 2743; Grm2.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; P31421; -.
DR OMA; IPWATPS; -.
DR OrthoDB; 5388627at2759; -.
DR PhylomeDB; P31421; -.
DR TreeFam; TF313240; -.
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:P31421; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000013171; Expressed in frontal cortex and 3 other cell types or tissues.
DR Genevisible; P31421; RN.
DR GO; GO:0097449; C:astrocyte projection; IDA:ARUK-UCL.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IMP:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:ARUK-UCL.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0014047; P:glutamate secretion; IDA:UniProtKB.
DR GO; GO:0090461; P:intracellular glutamate homeostasis; ISO:RGD.
DR GO; GO:0060292; P:long-term synaptic depression; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:ARUK-UCL.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0014048; P:regulation of glutamate secretion; IMP:RGD.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; NAS:UniProtKB.
DR GO; GO:2001023; P:regulation of response to drug; IMP:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0042220; P:response to cocaine; IMP:RGD.
DR CDD; cd15447; 7tmC_mGluR2; 1.
DR CDD; cd06375; PBP1_mGluR_groupII; 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; IPR001458; GPCR_3_mGluR2.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR24060:SF147; METABOTROPIC GLUTAMATE RECEPTOR 2; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01052; MTABOTROPC2R.
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 Cell membrane; Cell projection; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..872
FT /note="Metabotropic glutamate receptor 2"
FT /id="PRO_0000012926"
FT TOPO_DOM 19..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..590
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..655
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..725
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..747
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..783
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..793
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..819
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 677..685
FT /note="Important for interaction with HTR2A"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 166..168
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..92
FT /evidence="ECO:0000250"
FT DISULFID 234..518
FT /evidence="ECO:0000250"
FT DISULFID 355..362
FT /evidence="ECO:0000250"
FT DISULFID 400..407
FT /evidence="ECO:0000250"
FT DISULFID 500..519
FT /evidence="ECO:0000250"
FT DISULFID 504..522
FT /evidence="ECO:0000250"
FT DISULFID 525..537
FT /evidence="ECO:0000250"
FT DISULFID 540..553
FT /evidence="ECO:0000250"
SQ SEQUENCE 872 AA; 95774 MW; 1E74CABD6AD4BED9 CRC64;
MESLLGFLAL LLLWGAVAEG PAKKVLTLEG DLVLGGLFPV HQKGGPAEEC GPVNEHRGIQ
RLEAMLFALD RINRDPHLLP GVRLGAHILD SCSKDTHALE QALDFVRASL SRGADGSRHI
CPDGSYATHS DAPTAVTGVI GGSYSDVSIQ VANLLRLFQI PQISYASTSA KLSDKSRYDY
FARTVPPDFF QAKAMAEILR FFNWTYVSTV ASEGDYGETG IEAFELEARA RNICVATSEK
VGRAMSRAAF EGVVRALLQK PSARVAVLFT RSEDARELLA ATQRLNASFT WVASDGWGAL
ESVVAGSERA AEGAITIELA SYPISDFASY FQSLDPWNNS RNPWFREFWE ERFHCSFRQR
DCAAHSLRAV PFEQESKIMF VVNAVYAMAH ALHNMHRALC PNTTHLCDAM RPVNGRRLYK
DFVLNVKFDA PFRPADTDDE VRFDRFGDGI GRYNIFTYLR AGSGRYRYQK VGYWAEGLTL
DTSFIPWASP SAGPLPASRC SEPCLQNEVK SVQPGEVCCW LCIPCQPYEY RLDEFTCADC
GLGYWPNASL TGCFELPQEY IRWGDAWAVG PVTIACLGAL ATLFVLGVFV RHNATPVVKA
SGRELCYILL GGVFLCYCMT FVFIAKPSTA VCTLRRLGLG TAFSVCYSAL LTKTNRIARI
FGGAREGAQR PRFISPASQV AICLALISGQ LLIVAAWLVV EAPGTGKETA PERREVVTLR
CNHRDASMLG SLAYNVLLIA LCTLYAFKTR KCPENFNEAK FIGFTMYTTC IIWLAFLPIF
YVTSSDYRVQ TTTMCVSVSL SGSVVLGCLF APKLHIILFQ PQKNVVSHRA PTSRFGSAAP
RASANLGQGS GSQFVPTVCN GREVVDSTTS SL
//
