GRM8_MOUSE
ID GRM8_MOUSE Reviewed; 908 AA.
AC P47743; Q6B964;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Metabotropic glutamate receptor 8;
DE Short=mGluR8;
DE Flags: Precursor;
GN Name=Grm8; Synonyms=Gprc1h, Mglur8;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=7722646; DOI=10.1523/jneurosci.15-04-03075.1995;
RA Duvoisin R.M., Zhang C., Ramonell K.;
RT "A novel metabotropic glutamate receptor expressed in the retina and
RT olfactory bulb.";
RL J. Neurosci. 15:3075-3083(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15755905; DOI=10.1124/mol.105.010975;
RA Guo J., Ikeda S.R.;
RT "Coupling of metabotropic glutamate receptor 8 to N-type Ca2+ channels in
RT rat sympathetic neurons.";
RL Mol. Pharmacol. 67:1840-1851(2005).
RN [3]
RP SUMOYLATION AT LYS-882, AND MUTAGENESIS OF LYS-868; LYS-872 AND LYS-882.
RX PubMed=16144832; DOI=10.1074/jbc.m508168200;
RA Tang Z., El Far O., Betz H., Scheschonka A.;
RT "Pias1 interaction and sumoylation of metabotropic glutamate receptor 8.";
RL J. Biol. Chem. 280:38153-38159(2005).
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 PICK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Strongly expressed in olfactory bulb, accessory
CC olfactory bulb, and mammillary body. Weaker expression in the retina,
CC and in scattered cells in the cortex and hindbrain.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; U17252; AAA68149.1; -; mRNA.
DR EMBL; AY673682; AAT76980.1; -; mRNA.
DR CCDS; CCDS80495.1; -.
DR PIR; I49142; I49142.
DR RefSeq; NP_001298001.1; NM_001311072.1.
DR RefSeq; XP_017176886.1; XM_017321397.1.
DR AlphaFoldDB; P47743; -.
DR SMR; P47743; -.
DR BioGRID; 200074; 5.
DR IntAct; P47743; 1.
DR MINT; P47743; -.
DR STRING; 10090.ENSMUSP00000110978; -.
DR BindingDB; P47743; -.
DR ChEMBL; CHEMBL4626; -.
DR DrugCentral; P47743; -.
DR GlyGen; P47743; 5 sites.
DR iPTMnet; P47743; -.
DR PhosphoSitePlus; P47743; -.
DR PaxDb; P47743; -.
DR PRIDE; P47743; -.
DR ProteomicsDB; 269638; -.
DR Antibodypedia; 17706; 380 antibodies from 34 providers.
DR DNASU; 14823; -.
DR Ensembl; ENSMUST00000090512; ENSMUSP00000087998; ENSMUSG00000024211.
DR GeneID; 14823; -.
DR KEGG; mmu:14823; -.
DR UCSC; uc009bcj.1; mouse.
DR CTD; 2918; -.
DR MGI; MGI:1351345; Grm8.
DR VEuPathDB; HostDB:ENSMUSG00000024211; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; P47743; -.
DR OrthoDB; 483746at2759; -.
DR PhylomeDB; P47743; -.
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; 14823; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Grm8; mouse.
DR PRO; PR:P47743; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P47743; protein.
DR Bgee; ENSMUSG00000024211; Expressed in ganglionic layer of retina and 82 other tissues.
DR ExpressionAtlas; P47743; baseline and differential.
DR Genevisible; P47743; MM.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO: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:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; IDA:MGI.
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:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; 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; IPR000144; GPCR_3_mGluR8.
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; PR01058; MTABOTROPC8R.
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 Isopeptide bond; Membrane; Receptor; Reference proteome;
KW Sensory transduction; Signal; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..908
FT /note="Metabotropic glutamate receptor 8"
FT /id="PRO_0000012942"
FT TOPO_DOM 34..583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..608
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..746
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..768
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..781
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..803
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 804..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..843
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 177..179
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..106
FT /evidence="ECO:0000250"
FT DISULFID 246..534
FT /evidence="ECO:0000250"
FT DISULFID 369..384
FT /evidence="ECO:0000250"
FT DISULFID 424..431
FT /evidence="ECO:0000250"
FT DISULFID 516..535
FT /evidence="ECO:0000250"
FT DISULFID 520..538
FT /evidence="ECO:0000250"
FT DISULFID 541..553
FT /evidence="ECO:0000250"
FT DISULFID 556..569
FT /evidence="ECO:0000250"
FT CROSSLNK 882
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:16144832"
FT MUTAGEN 868
FT /note="K->R: No change in sumoylation. Abolishes
FT sumoylation; when associated with R-872 and R-882."
FT /evidence="ECO:0000269|PubMed:16144832"
FT MUTAGEN 872
FT /note="K->R: No change in sumoylation. Abolishes
FT sumoylation; when associated with R-868 and R-882."
FT /evidence="ECO:0000269|PubMed:16144832"
FT MUTAGEN 882
FT /note="K->R: Abolishes sumoylation. Abolishes sumoylation;
FT when associated with R-868 and R-872."
FT /evidence="ECO:0000269|PubMed:16144832"
FT CONFLICT 86
FT /note="I -> T (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="R -> G (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
FT CONFLICT 363..365
FT /note="WEE -> SEG (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="L -> S (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="E -> G (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="F -> L (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="N -> D (in Ref. 1; AAA68149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 101828 MW; E9952B6D356EB8A8 CRC64;
MVCEGKRSTS CPCFFLLTAK FYWILTMMQR THSQEYAHSI RLDGDIILGG LFPVHAKGER
GVPCGDLKKE KGIHRLEAML YAIDQINKDP DLLSNITLGV RILDTCSRDT YALEQSLTFV
QALIEKDASD VKCANGDPPI FTKPDKISGV IGAAASSVSI MVANILRLFK IPQISYASTA
PELSDNTRYD FFSRVVPPDS YQAQAMVDIV TALGWNYVST LASEGNYGES GVEAFTQISR
EIGGVCIAQS QKIPREPRPG EFEKIIKRLL ETPNARAVIM FANEDDIRRI LEAAKKLNQS
GHFLWIGSDS WGSKIAPVYQ QEEIAEGAVT ILPKRASIDG FDRYFRSRTL ANNRRNVWFA
EFWEENFGCK LGSHGKRNSH IKKCTGLERI ARDSSYEQEG KVQFVIDAVY SMAYALHNMH
KELCPGYIGL CPRMVTIDGK ELLGYIRAVN FNGSAGTPVT FNENGDAPGR YDIFQYQINN
KSTEYKIIGH WTNQLHLKVE DMQWANREHT HPASVCSLPC KPGERKKTVK GVPCCWHCER
CEGYNYQVDE LSCELCPLDQ RPNINRTGCQ RIPIIKLEWH SPWAVVPVFI AILGIIATTF
VIVTFVRYND TPIVRASGRE LSYVLLTGIF LCYSITFLMI AAPDTIICSF RRIFLGLGMC
FSYAALLTKT NRIHRIFEQG KKSVTAPKFI SPASQLVITF SLISVQLLGV FVWFVVDPPH
TIIDYGEQRT LDPENARGVL KCDISDLSLI CSLGYSILLM VTCTVYAIKT RGVPETFNEA
KPIGFTMYTT CIIWLAFIPI FFGTAQSAEK MYIQTTTLTV SMSLSASVSL GMLYMPKVYI
IIFHPEQNVQ KRKRSFKAVV TAATMQSKLI QKGNDRPNGE VKSELCESLE TNTSSTKTTY
ISYSNHSI
