GRM3_MOUSE
ID GRM3_MOUSE Reviewed; 879 AA.
AC Q9QYS2; Q14DJ9;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Metabotropic glutamate receptor 3;
DE Short=mGluR3;
DE Flags: Precursor;
GN Name=Grm3; Synonyms=Gprc1c, Mglur3;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10544282; DOI=10.1093/oxfordjournals.jbchem.a022531;
RA Minoshima T., Nakanishi S.;
RT "Structural organization of the mouse metabotropic glutamate receptor
RT subtype 3 gene and its regulation by growth factors in cultured cortical
RT astrocytes.";
RL J. Biochem. 126:889-896(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AF170701; AAF06741.1; -; Genomic_DNA.
DR EMBL; AF170697; AAF06741.1; JOINED; Genomic_DNA.
DR EMBL; AF170698; AAF06741.1; JOINED; Genomic_DNA.
DR EMBL; AF170699; AAF06741.1; JOINED; Genomic_DNA.
DR EMBL; AF170700; AAF06741.1; JOINED; Genomic_DNA.
DR EMBL; BC111891; AAI11892.1; -; mRNA.
DR EMBL; BC113170; AAI13171.1; -; mRNA.
DR CCDS; CCDS19090.1; -.
DR PIR; JC7160; JC7160.
DR RefSeq; NP_862898.1; NM_181850.2.
DR AlphaFoldDB; Q9QYS2; -.
DR SMR; Q9QYS2; -.
DR BioGRID; 223808; 6.
DR IntAct; Q9QYS2; 4.
DR STRING; 10090.ENSMUSP00000004076; -.
DR GlyConnect; 2508; 12 N-Linked glycans (1 site).
DR GlyGen; Q9QYS2; 4 sites, 12 N-linked glycans (1 site).
DR iPTMnet; Q9QYS2; -.
DR PhosphoSitePlus; Q9QYS2; -.
DR MaxQB; Q9QYS2; -.
DR PaxDb; Q9QYS2; -.
DR PeptideAtlas; Q9QYS2; -.
DR PRIDE; Q9QYS2; -.
DR ProteomicsDB; 271170; -.
DR Antibodypedia; 15243; 392 antibodies from 35 providers.
DR DNASU; 108069; -.
DR Ensembl; ENSMUST00000004076; ENSMUSP00000004076; ENSMUSG00000003974.
DR GeneID; 108069; -.
DR KEGG; mmu:108069; -.
DR UCSC; uc008wll.1; mouse.
DR CTD; 2913; -.
DR MGI; MGI:1351340; Grm3.
DR VEuPathDB; HostDB:ENSMUSG00000003974; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; Q9QYS2; -.
DR OMA; CIARIFN; -.
DR OrthoDB; 1154468at2759; -.
DR PhylomeDB; Q9QYS2; -.
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; 108069; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Grm3; mouse.
DR PRO; PR:Q9QYS2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9QYS2; protein.
DR Bgee; ENSMUSG00000003974; Expressed in dorsal striatum and 93 other tissues.
DR Genevisible; Q9QYS2; MM.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; NAS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
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:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0051930; P:regulation of sensory perception of pain; NAS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; 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; IPR001234; GPCR_3_mGluR3.
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; PR01053; MTABOTROPC3R.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..879
FT /note="Metabotropic glutamate receptor 3"
FT /id="PRO_0000012928"
FT TOPO_DOM 23..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..599
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..664
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..756
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..792
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..828
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 151
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..99
FT /evidence="ECO:0000250"
FT DISULFID 240..527
FT /evidence="ECO:0000250"
FT DISULFID 361..373
FT /evidence="ECO:0000250"
FT DISULFID 412..419
FT /evidence="ECO:0000250"
FT DISULFID 509..528
FT /evidence="ECO:0000250"
FT DISULFID 513..531
FT /evidence="ECO:0000250"
FT DISULFID 534..546
FT /evidence="ECO:0000250"
FT DISULFID 549..562
FT /evidence="ECO:0000250"
SQ SEQUENCE 879 AA; 99114 MW; F3A8B26CE96679EF CRC64;
MKMLTRLQVL MLALFSKGFL VSLGDHNFMR REIKIEGDLV LGGLFPINEK GTGTEECGRI
NEDRGIQRLE AMLFAIDEIN KDNYLLPGVK LGVHILDTCS RDTYALEQSL EFVRASLTKV
DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD
KSRYDYFART VPPDFYQAKA MAEILRYFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC
IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAASR VNASFTWVAS
DGWGAQESIV KGSEHVAYGA ITLELASHPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ
CSLQNKRNHR QICDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD
AMKILDGKKL YKDYLLKINF TAPFNPNKGA DSIVKFDTYG DGMGRYNVFN FQHIGGKYSY
LKVGHWAETL YLDVDSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL
VDEFTCMDCG PGQWPTADLS GCYNLPEDYI RWEDAWAIGP VTIACLGFMC TCIVITVFIK
HNNTPLVKAS GRELCYILLF GVSLSYCMTF FFIAKPSPVI CALRRLGLGT SFAICYSALL
TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE TPGTRRYTLP
EKRETVILKC NVKDSSMLIS LTYDVVLVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI
IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIVLFQP QKNVVTHRLH
LNRFSVSGTA TTYSQSSAST YVPTVCNGRE VLDSTTSSL
