GRM7_RAT
ID GRM7_RAT Reviewed; 915 AA.
AC P35400;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Metabotropic glutamate receptor 7;
DE Short=mGluR7;
DE Flags: Precursor;
GN Name=Grm7; Synonyms=Gprc1g, Mglur7;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8288585; DOI=10.1016/s0021-9258(17)42247-2;
RA Okamoto N., Hori S., Akazawa C., Hayashi Y., Shigemoto R., Mizuno N.,
RA Nakanishi S.;
RT "Molecular characterization of a new metabotropic glutamate receptor mGluR7
RT coupled to inhibitory cyclic AMP signal transduction.";
RL J. Biol. Chem. 269:1231-1236(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX PubMed=8145723;
RA Saugstad J.A., Kinzie J.M., Mulvihill E.R., Segerson T.P., Westbrook G.L.;
RT "Cloning and expression of a new member of the L-2-amino-4-phosphonobutyric
RT acid-sensitive class of metabotropic glutamate receptors.";
RL Mol. Pharmacol. 45:367-372(1994).
RN [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-521, AND DISULFIDE BONDS.
RX PubMed=17360426; DOI=10.1073/pnas.0611577104;
RA Muto T., Tsuchiya D., Morikawa K., Jingami H.;
RT "Structures of the extracellular regions of the group II/III metabotropic
RT glutamate receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3759-3764(2007).
RN [5]
RP FUNCTION.
RX PubMed=33500274; DOI=10.1523/jneurosci.2108-20.2021;
RA Song J.M., Kang M., Park D.H., Park S., Lee S., Suh Y.H.;
RT "Pathogenic GRM7 mutations associated with neurodevelopmental disorders
RT impair axon outgrowth and presynaptic terminal development.";
RL J. Neurosci. 41:2344-2359(2021).
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.
CC {ECO:0000250|UniProtKB:Q14831, ECO:0000269|PubMed:33500274,
CC ECO:0000269|PubMed:8145723, ECO:0000269|PubMed:8288585}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PICK1.
CC {ECO:0000250|UniProtKB:Q14831, ECO:0000269|PubMed:11122333}.
CC -!- INTERACTION:
CC P35400; P97879: Grip1; NbExp=3; IntAct=EBI-6936416, EBI-936113;
CC P35400; Q9EP80: Pick1; NbExp=2; IntAct=EBI-6936416, EBI-77728;
CC P35400; P63088: Ppp1cc; NbExp=4; IntAct=EBI-6936416, EBI-80049;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14831};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14831}.
CC -!- TISSUE SPECIFICITY: Widely distributed throughout the brain.
CC {ECO:0000269|PubMed:8145723, ECO:0000269|PubMed:8288585}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; D16817; BAA04092.1; -; mRNA.
DR EMBL; U06832; AAA20655.1; -; mRNA.
DR PIR; A49874; A49874.
DR RefSeq; NP_112302.1; NM_031040.1.
DR PDB; 2E4Z; X-ray; 3.30 A; A=33-521.
DR PDBsum; 2E4Z; -.
DR AlphaFoldDB; P35400; -.
DR SMR; P35400; -.
DR BioGRID; 249569; 9.
DR DIP; DIP-41145N; -.
DR IntAct; P35400; 7.
DR MINT; P35400; -.
DR STRING; 10116.ENSRNOP00000053411; -.
DR BindingDB; P35400; -.
DR ChEMBL; CHEMBL3879; -.
DR GuidetoPHARMACOLOGY; 295; -.
DR CarbonylDB; P35400; -.
DR GlyGen; P35400; 4 sites.
DR iPTMnet; P35400; -.
DR PhosphoSitePlus; P35400; -.
DR PaxDb; P35400; -.
DR PRIDE; P35400; -.
DR Ensembl; ENSRNOT00000056570; ENSRNOP00000053411; ENSRNOG00000005662.
DR GeneID; 81672; -.
DR KEGG; rno:81672; -.
DR CTD; 2917; -.
DR RGD; 619857; Grm7.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR InParanoid; P35400; -.
DR OrthoDB; 483746at2759; -.
DR PhylomeDB; P35400; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR EvolutionaryTrace; P35400; -.
DR PRO; PR:P35400; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
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; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IDA:RGD.
DR GO; GO:0010855; F:adenylate cyclase inhibitor activity; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
DR GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; ISO:RGD.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0070905; F:serine binding; ISO:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0001661; P:conditioned taste aversion; ISO:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0070085; P:glycosylation; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; TAS:UniProtKB.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0033555; P:multicellular organismal response to stress; ISO:RGD.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; IDA:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
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:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0007614; P:short-term memory; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
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 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; 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_0000012940"
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:0000250|UniProtKB:Q68ED2"
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:0000269|PubMed:17360426"
FT DISULFID 249..541
FT /evidence="ECO:0000250"
FT DISULFID 374..390
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 430..437
FT /evidence="ECO:0000269|PubMed:17360426"
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"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 72..91
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2E4Z"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 229..244
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:2E4Z"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:2E4Z"
FT TURN 314..318
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:2E4Z"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 408..429
FT /evidence="ECO:0007829|PDB:2E4Z"
FT TURN 438..443
FT /evidence="ECO:0007829|PDB:2E4Z"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 491..504
FT /evidence="ECO:0007829|PDB:2E4Z"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:2E4Z"
SQ SEQUENCE 915 AA; 102232 MW; F28AFC4C6454A6C2 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 YIRHVNFNGS AGTPVMFNKN GDAPGRYDIF
QYQTTNTTNP GYRLIGQWTD ELQLNIEDMQ WGKGVREIPS 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
