GRM6_RAT
ID GRM6_RAT Reviewed; 871 AA.
AC P35349;
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 6;
DE Short=mGluR6;
DE Flags: Precursor;
GN Name=Grm6; Synonyms=Gprc1f, Mglur6;
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=Retina;
RX PubMed=8389366; DOI=10.1016/s0021-9258(19)50280-0;
RA Nakajima Y., Iwakabe H., Akazawa C., Nawa H., Shigemoto R., Nakanishi S.;
RT "Molecular characterization of a novel retinal metabotropic glutamate
RT receptor mGluR6 with a high agonist selectivity for L-2-amino-4-
RT phosphonobutyrate.";
RL J. Biol. Chem. 268:11868-11873(1993).
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, such as adenylate cyclase. Signaling inhibits
CC adenylate cyclase activity (By similarity). Signaling stimulates TRPM1
CC channel activity and Ca(2+) uptake. Required for normal vision.
CC {ECO:0000250, ECO:0000269|PubMed:8389366}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Note=Subject to trafficking from the endoplasmic
CC reticulum to the Golgi apparatus and then to the cell membrane.
CC Detected at dendritic tips of bipolar cells (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Restricted expression in the inner nuclear layer of
CC the retina. {ECO:0000269|PubMed:8389366}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; D13963; BAA03066.1; -; mRNA.
DR PIR; A46742; A46742.
DR RefSeq; NP_075209.1; NM_022920.1.
DR RefSeq; XP_017452483.1; XM_017596994.1.
DR AlphaFoldDB; P35349; -.
DR SMR; P35349; -.
DR BioGRID; 246584; 4.
DR IntAct; P35349; 2.
DR MINT; P35349; -.
DR STRING; 10116.ENSRNOP00000000249; -.
DR BindingDB; P35349; -.
DR ChEMBL; CHEMBL3842; -.
DR DrugCentral; P35349; -.
DR GuidetoPHARMACOLOGY; 294; -.
DR GlyGen; P35349; 4 sites.
DR PhosphoSitePlus; P35349; -.
DR PaxDb; P35349; -.
DR PRIDE; P35349; -.
DR Ensembl; ENSRNOT00000000249; ENSRNOP00000000249; ENSRNOG00000000233.
DR GeneID; 24419; -.
DR KEGG; rno:24419; -.
DR UCSC; RGD:2747; rat.
DR CTD; 2916; -.
DR RGD; 2747; Grm6.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; P35349; -.
DR OMA; TAVMFNE; -.
DR OrthoDB; 1154468at2759; -.
DR PhylomeDB; P35349; -.
DR TreeFam; TF313240; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR PRO; PR:P35349; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000000233; Expressed in cerebellum and 1 other tissue.
DR Genevisible; P35349; RN.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0035841; C:new growing cell tip; ISO:RGD.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IDA:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IEP:RGD.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISS:UniProtKB.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; 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; IPR000112; GPCR_3__mGluR6.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
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; PR01056; MTABOTROPC6R.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Membrane;
KW Receptor; Reference proteome; Sensory transduction; Signal; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..871
FT /note="Metabotropic glutamate receptor 6"
FT /id="PRO_0000012937"
FT TOPO_DOM 24..579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..602
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..648
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..667
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..742
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 743..764
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..800
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..813
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..839
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 850..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 169..171
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 219
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 394
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..93
FT /evidence="ECO:0000250"
FT DISULFID 238..530
FT /evidence="ECO:0000250"
FT DISULFID 361..377
FT /evidence="ECO:0000250"
FT DISULFID 417..424
FT /evidence="ECO:0000250"
FT DISULFID 512..531
FT /evidence="ECO:0000250"
FT DISULFID 516..534
FT /evidence="ECO:0000250"
FT DISULFID 537..549
FT /evidence="ECO:0000250"
FT DISULFID 552..565
FT /evidence="ECO:0000250"
SQ SEQUENCE 871 AA; 95089 MW; 9F70B4D6A13B186D CRC64;
MGRLPVLLLW LAWWLSQAGI ACGAGSVRLA GGLTLGGLFP VHARGAAGRA CGALKKEQGV
HRLEAMLYAL DRVNADPELL PGVRLGARLL DTCSRDTYAL EQALSFVQAL IRGRGDGDEA
SVRCPGGVPP LRSAPPERVV AVVGASASSV SIMVANVLRL FAIPQISYAS TAPELSDSTR
YDFFSRVVPP DSYQAQAMVD IVRALGWNYV STLASEGNYG ESGVEAFVQI SREAGGVCIA
QSIKIPREPK PGEFHKVIRR LMETPNARGI IIFANEDDIR RVLEATRQAN LTGHFLWVGS
DSWGSKISPI LNLEEEAVGA ITILPKRASI DGFDQYFMTR SLENNRRNIW FAEFWEENFN
CKLTSSGGQS DDSTRKCTGE ERIGQDSAYE QEGKVQFVID AVYAIAHALH SMHQALCPGH
TGLCPAMEPT DGRTLLHYIR AVRFNGSAGT PVMFNENGDA PGRYDIFQYQ ATNGSASSGG
YQAVGQWAEA LRLDMEVLRW SGDPHEVPPS QCSLPCGPGE RKKMVKGVPC CWHCEACDGY
RFQVDEFTCE ACPGDMRPTP NHTGCRPTPV VRLTWSSPWA ALPLLLAVLG IMATTTIMAT
FMRHNDTPIV RASGRELSYV LLTGIFLIYA ITFLMVAEPC AAICAARRLL LGLGTTLSYS
ALLTKTNRIY RIFEQGKRSV TPPPFISPTS QLVITFGLTS LQVVGVIAWL GAQPPHSVID
YEEQRTVDPE QARGVLKCDM SDLSLIGCLG YSLLLMVTCT VYAIKARGVP ETFNEAKPIG
FTMYTTCIIW LAFVPIFFGT AQSAEKIYIQ TTTLTVSLSL SASVSLGMLY VPKTYVILFH
PEQNVQKRKR SLKKTSTMAA PPQNENAEDA K
