GRM7_MOUSE
ID GRM7_MOUSE Reviewed; 915 AA.
AC Q68ED2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Metabotropic glutamate receptor 7;
DE Short=mGluR7;
DE Flags: Precursor;
GN Name=Grm7; Synonyms=Gprc1g, Mglur7;
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].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, AND IDENTIFICATION BY
RP 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 activated by glutamate that
CC regulates axon outgrowth through the MAPK-cAMP-PKA signaling pathway
CC during neuronal development (By similarity). Ligand binding causes a
CC conformation change that triggers signaling via guanine nucleotide-
CC binding proteins (G proteins) and modulates the activity of downstream
CC effectors, such as adenylate cyclase that it inhibits (By similarity).
CC {ECO:0000250|UniProtKB:Q14831}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PICK1.
CC {ECO:0000250|UniProtKB:P35400, ECO:0000250|UniProtKB:Q14831}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14831};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14831}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; BC080315; AAH80315.1; -; mRNA.
DR CCDS; CCDS39587.1; -.
DR RefSeq; NP_796302.2; NM_177328.3.
DR AlphaFoldDB; Q68ED2; -.
DR SMR; Q68ED2; -.
DR BioGRID; 223811; 3.
DR DIP; DIP-32216N; -.
DR IntAct; Q68ED2; 2.
DR STRING; 10090.ENSMUSP00000133957; -.
DR ChEMBL; CHEMBL3966; -.
DR GlyGen; Q68ED2; 4 sites.
DR iPTMnet; Q68ED2; -.
DR PhosphoSitePlus; Q68ED2; -.
DR MaxQB; Q68ED2; -.
DR PaxDb; Q68ED2; -.
DR PRIDE; Q68ED2; -.
DR ProteomicsDB; 271307; -.
DR Antibodypedia; 10079; 428 antibodies from 35 providers.
DR Ensembl; ENSMUST00000172951; ENSMUSP00000133957; ENSMUSG00000056755.
DR GeneID; 108073; -.
DR KEGG; mmu:108073; -.
DR UCSC; uc009dds.1; mouse.
DR CTD; 2917; -.
DR MGI; MGI:1351344; Grm7.
DR VEuPathDB; HostDB:ENSMUSG00000056755; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; Q68ED2; -.
DR OrthoDB; 483746at2759; -.
DR PhylomeDB; Q68ED2; -.
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; 108073; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Grm7; mouse.
DR PRO; PR:Q68ED2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q68ED2; protein.
DR Bgee; ENSMUSG00000056755; Expressed in medial dorsal nucleus of thalamus and 112 other tissues.
DR ExpressionAtlas; Q68ED2; baseline and differential.
DR Genevisible; Q68ED2; MM.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; TAS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; ISO:MGI.
DR GO; GO:0010855; F:adenylate cyclase inhibitor activity; ISO:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0070905; F:serine binding; ISO:MGI.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:UniProtKB.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0070085; P:glycosylation; ISO:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0050877; P:nervous system process; IMP:MGI.
DR GO; GO:1901214; P:regulation of neuron death; TAS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0007614; P:short-term memory; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP: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; IPR001883; GPCR_3_mGluR7.
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; PR01057; MTABOTROPC7R.
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; Phosphoprotein; Receptor; Reference proteome;
KW Sensory transduction; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..915
FT /note="Metabotropic glutamate receptor 7"
FT /id="PRO_0000012939"
FT TOPO_DOM 35..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..615
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..775
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..810
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..825
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..850
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 851..915
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 874..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 314
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT /evidence="ECO:0000250"
FT DISULFID 249..541
FT /evidence="ECO:0000250"
FT DISULFID 374..390
FT /evidence="ECO:0000250"
FT DISULFID 430..437
FT /evidence="ECO:0000250"
FT DISULFID 523..542
FT /evidence="ECO:0000250"
FT DISULFID 527..545
FT /evidence="ECO:0000250"
FT DISULFID 548..560
FT /evidence="ECO:0000250"
FT DISULFID 563..576
FT /evidence="ECO:0000250"
SQ SEQUENCE 915 AA; 102219 MW; F0AF7AEDBFBCCF71 CRC64;
MVQLGKLLRV LTLMKFPCCV LEVLLCVLAA AARGQEMYAP HSIRIEGDVT LGGLFPVHAK
GPSGVPCGDI KRENGIHRLE AMLYALDQIN SDPNLLPNVT LGARILDTCS RDTYALEQSL
TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA
STAPELSDDR RYDFFSRVVP PDSFQAQAMV DIVKALGWNY VSTLASEGSY GEKGVESFTQ
ISKEAGGLCI AQSVRIPQER KDRTIDFDRI IKQLLDTPNS RAVVIFANDE DIKQILAAAK
RADQVGHFLW VGSDSWGSKI NPLHQHEDIA EGAITIQPKR ATVEGFDAYF TSRTLENNRR
NVWFAEYWEE NFNCKLTISG SKKEDTDRKC TGQERIGKDS NYEQEGKVQF VIDAVYAMAH
ALHHMNKDLC ADYRGVCPEM EQAGGKKLLK YIRNVNFNGS AGTPVMFNKN GDAPGRYDIF
QYQTTNTTNP GYRLIGQWTD ELQLNIEDMQ WGKGVREIPP SVCTLPCKPG QRKKTQKGTP
CCWTCEPCDG YQYQFDEMTC QHCPYDQRPN ENRTGCQNIP IIKLEWHSPW AVIPVFLAML
GIIATIFVMA TFIRYNDTPI VRASGRELSY VLLTGIFLCY IITFLMIAKP DVAVCSFRRV
FLGLGMCISY AALLTKTNRI YRIFEQGKKS VTAPRLISPT SQLAITSSLI SVQLLGVFIW
FGVDPPNIII DYDEHKTMNP EQARGVLKCD ITDLQIICSL GYSILLMVTC TVYAIKTRGV
PENFNEAKPI GFTMYTTCIV WLAFIPIFFG TAQSAEKLYI QTTTLTISMN LSASVALGML
YMPKVYIIIF HPELNVQKRK RSFKAVVTAA TMSSRLSHKP SDRPNGEAKT ELCENVDPNS
PAAKKKYVSY NNLVI
