GRM2_MOUSE
ID GRM2_MOUSE Reviewed; 872 AA.
AC Q14BI2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Metabotropic glutamate receptor 2;
DE Short=mGluR2;
DE Flags: Precursor;
GN Name=Grm2; Synonyms=Gprc1b, Mglur2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-470.
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 [3]
RP INTERACTION WITH HTR2A, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18297054; DOI=10.1038/nature06612;
RA Gonzalez-Maeso J., Ang R.L., Yuen T., Chan P., Weisstaub N.V.,
RA Lopez-Gimenez J.F., Zhou M., Okawa Y., Callado L.F., Milligan G.,
RA Gingrich J.A., Filizola M., Meana J.J., Sealfon S.C.;
RT "Identification of a serotonin/glutamate receptor complex implicated in
RT psychosis.";
RL Nature 452:93-97(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23129762; DOI=10.1074/jbc.m112.413161;
RA Moreno J.L., Muguruza C., Umali A., Mortillo S., Holloway T.,
RA Pilar-Cuellar F., Mocci G., Seto J., Callado L.F., Neve R.L., Milligan G.,
RA Sealfon S.C., Lopez-Gimenez J.F., Meana J.J., Benson D.L.,
RA Gonzalez-Maeso J.;
RT "Identification of three residues essential for 5-hydroxytryptamine 2A-
RT metabotropic glutamate 2 (5-HT2A.mGlu2) receptor heteromerization and its
RT psychoactive behavioral function.";
RL J. Biol. Chem. 287:44301-44319(2012).
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. {ECO:0000269|PubMed:18297054,
CC ECO:0000269|PubMed:23129762}.
CC -!- SUBUNIT: Interacts with TAMALIN (By similarity). Interacts with HTR2A.
CC {ECO:0000250, ECO:0000269|PubMed:18297054}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Synapse. Cell projection, dendrite.
CC -!- TISSUE SPECIFICITY: Detected in neurons in brain cortex (at protein
CC level). {ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:23129762}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AC152452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115866; AAI15867.1; -; mRNA.
DR CCDS; CCDS52914.1; -.
DR RefSeq; NP_001153825.1; NM_001160353.1.
DR AlphaFoldDB; Q14BI2; -.
DR SMR; Q14BI2; -.
DR BioGRID; 223807; 2.
DR IntAct; Q14BI2; 6.
DR MINT; Q14BI2; -.
DR STRING; 10090.ENSMUSP00000023959; -.
DR GlyConnect; 2507; 2 N-Linked glycans (1 site).
DR GlyGen; Q14BI2; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q14BI2; -.
DR PhosphoSitePlus; Q14BI2; -.
DR MaxQB; Q14BI2; -.
DR PaxDb; Q14BI2; -.
DR PeptideAtlas; Q14BI2; -.
DR PRIDE; Q14BI2; -.
DR ProteomicsDB; 269839; -.
DR Antibodypedia; 14188; 549 antibodies from 44 providers.
DR Ensembl; ENSMUST00000023959; ENSMUSP00000023959; ENSMUSG00000023192.
DR GeneID; 108068; -.
DR KEGG; mmu:108068; -.
DR UCSC; uc009rkj.3; mouse.
DR CTD; 2912; -.
DR MGI; MGI:1351339; Grm2.
DR VEuPathDB; HostDB:ENSMUSG00000023192; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR InParanoid; Q14BI2; -.
DR OMA; SLIPWAE; -.
DR OrthoDB; 1154468at2759; -.
DR PhylomeDB; Q14BI2; -.
DR TreeFam; TF313240; -.
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; 108068; 1 hit in 76 CRISPR screens.
DR PRO; PR:Q14BI2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q14BI2; protein.
DR Bgee; ENSMUSG00000023192; Expressed in animal zygote and 41 other tissues.
DR ExpressionAtlas; Q14BI2; baseline and differential.
DR Genevisible; Q14BI2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IDA:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:MGI.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0090461; P:glutamate homeostasis; IGI:MGI.
DR GO; GO:0014047; P:glutamate secretion; ISO:MGI.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0014048; P:regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:2001023; P:regulation of response to drug; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0042220; P:response to cocaine; ISO:MGI.
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; IPR001458; GPCR_3_mGluR2.
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; PR01052; MTABOTROPC2R.
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; 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_0000306249"
FT TOPO_DOM 19..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..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..633
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..651
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..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..726
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..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..781
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 782..798
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..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; 95887 MW; FE1726B0684E256D CRC64;
MESLLRFLAL LLLRGAVAEG PAKKVLTLEG DLVLGGLFPV HQKGGPAEEC GPVNEHRGIQ
RLEAMLFALD RINRDPHLLP GVRLGAHILD SCSKDTHALE QALDFVRASL SRGADGSRHI
CPDGSYATLS DAPTAITGVI GGSYSDVSIQ VANLLRLFQI PQISYASTSA KLSDKSRYDY
FARTVPPDFF QAKAMAEILR FFNWTYVSTV ASEGDYGETG IEAFELEARA RNICVATSEK
VGRAMSRAAF EGVVRALLQK PSARVAVLFT RSEDARELLA ATQRLNASFT WVASDGWGAL
ESVVAGSERA AEGAITIELA SYPISDFASY FQNLDPWNNS RNPWFREFWE ERFRCSFRQR
DCAAHSLRAV PFEQESKIMF VVNAVYAMAH ALHNMHRALC PNTTRLCDAM RPVNGRRLYK
DFVLNVKFDA PFRPADTDDE VRFDRFGDGI GRYNIFTYLR AGNGRYRYQK VGYWAEGLTL
DTSIIPWASP SAGTLPASRC SEPCLQNEVK SVQPGEVCCW LCIPCQPYEY RLDEFTCADC
GLGYWPNASL TGCFELPQEY IRWGDAWAVG PVTIACLGAL ATLFVLGVFV RHNATPVVKA
SGRELCYILL GGVFLCYCMT FIFIAKPSTA VCTLRRLGLG TAFSVCYSAL LTKTNRIARI
FGGAREGAQR PRFISPASQV AICLALISGQ LLIVAAWLVV EAPGIGKETA PERREVVTLR
CNHRDASMLG SLAYNVLLIA LCTLYAFKTR KCPENFNEAK FIGFTMYTTC IIWLAFLPIF
YVTSSDYRVQ TTTMCVSVSL SGSVVLGCLF APKLHIILFQ PQKNVVSHRA PTSRFGSAAP
RASANLGQGS GSQLVPTVCN GREVVDSTTS SL
