GRM6_MOUSE
ID GRM6_MOUSE Reviewed; 871 AA.
AC Q5NCH9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Metabotropic glutamate receptor 6;
DE Short=mGluR6;
DE Flags: Precursor;
GN Name=Grm6; Synonyms=Gprc1f, Mglur6;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=7889569; DOI=10.1016/0092-8674(95)90354-2;
RA Masu M., Iwakabe H., Tagawa Y., Miyoshi T., Yamashita M., Fukuda Y.,
RA Sasaki H., Hiroi K., Nakamura Y., Shigemoto R., Takada M., Nakamura K.,
RA Nakao K., Katsuki M., Nakanishi S.;
RT "Specific deficit of the ON response in visual transmission by targeted
RT disruption of the mGluR6 gene.";
RL Cell 80:757-765(1995).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9144650; DOI=10.1016/s0028-3908(96)00167-0;
RA Iwakabe H., Katsuura G., Ishibashi C., Nakanishi S.;
RT "Impairment of pupillary responses and optokinetic nystagmus in the mGluR6-
RT deficient mouse.";
RL Neuropharmacology 36:135-143(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18001285; DOI=10.1111/j.1460-9568.2007.05867.x;
RA Morgans C.W., Wensel T.G., Brown R.L., Perez-Leon J.A., Bearnot B.,
RA Duvoisin R.M.;
RT "Gbeta5-RGS complexes co-localize with mGluR6 in retinal ON-bipolar
RT cells.";
RL Eur. J. Neurosci. 26:2899-2905(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18952919; DOI=10.1167/iovs.08-2758;
RA Specht D., Wu S.B., Turner P., Dearden P., Koentgen F., Wolfrum U., Maw M.,
RA Brandstatter J.H., tom Dieck S.;
RT "Effects of presynaptic mutations on a postsynaptic Cacna1s calcium channel
RT colocalized with mGluR6 at mouse photoreceptor ribbon synapses.";
RL Invest. Ophthalmol. Vis. Sci. 50:505-515(2009).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22131384; DOI=10.1152/jn.00933.2011;
RA Xu Y., Dhingra A., Fina M.E., Koike C., Furukawa T., Vardi N.;
RT "mGluR6 deletion renders the TRPM1 channel in retina inactive.";
RL J. Neurophysiol. 107:948-957(2012).
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:22131384, ECO:0000269|PubMed:9144650}.
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 Note=Subject to trafficking from the endoplasmic reticulum to the Golgi
CC apparatus and then to the cell membrane (By similarity). Detected at
CC dendritic tips of bipolar cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in the outer plexiform layer in retina (at
CC protein level). {ECO:0000269|PubMed:18001285,
CC ECO:0000269|PubMed:7889569}.
CC -!- DISRUPTION PHENOTYPE: Retinal cells from mutant mice display a subtly
CC altered response to cycles of light and darkness, due to a failure of
CC the ON bipolar cells in the retina to become depolarized in response to
CC light. As a consequence, mutant mice display little or no pupillary
CC contraction in adaptation to low light intensity. Besides, they exhibit
CC strongly impaired responses to moving stimuli, and fail to produce a
CC response when the visual constrast is low. Besides, rod bipolar cells
CC from mutant mice lack TRPM1 channel activity.
CC {ECO:0000269|PubMed:22131384, ECO:0000269|PubMed:7889569,
CC ECO:0000269|PubMed:9144650}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AL627215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48785.1; -.
DR RefSeq; NP_775548.2; NM_173372.2.
DR RefSeq; XP_006532024.1; XM_006531961.2.
DR AlphaFoldDB; Q5NCH9; -.
DR SMR; Q5NCH9; -.
DR BioGRID; 223810; 1.
DR IntAct; Q5NCH9; 1.
DR STRING; 10090.ENSMUSP00000130728; -.
DR GlyGen; Q5NCH9; 4 sites.
DR iPTMnet; Q5NCH9; -.
DR PhosphoSitePlus; Q5NCH9; -.
DR PaxDb; Q5NCH9; -.
DR PRIDE; Q5NCH9; -.
DR ProteomicsDB; 271171; -.
DR Antibodypedia; 17632; 368 antibodies from 32 providers.
DR DNASU; 108072; -.
DR Ensembl; ENSMUST00000000631; ENSMUSP00000000631; ENSMUSG00000000617.
DR Ensembl; ENSMUST00000171427; ENSMUSP00000130728; ENSMUSG00000000617.
DR GeneID; 108072; -.
DR KEGG; mmu:108072; -.
DR UCSC; uc007isu.2; mouse.
DR CTD; 2916; -.
DR MGI; MGI:1351343; Grm6.
DR VEuPathDB; HostDB:ENSMUSG00000000617; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; Q5NCH9; -.
DR OMA; TAVMFNE; -.
DR OrthoDB; 1154468at2759; -.
DR PhylomeDB; Q5NCH9; -.
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; 108072; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Grm6; mouse.
DR PRO; PR:Q5NCH9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NCH9; protein.
DR Bgee; ENSMUSG00000000617; Expressed in retinal neural layer and 6 other tissues.
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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0035841; C:new growing cell tip; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; TAS:UniProtKB.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; TAS:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
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; IMP:MGI.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IGI:MGI.
DR GO; GO:0007601; P:visual perception; 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; 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 1: Evidence at protein 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_0000012935"
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 848..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; 95193 MW; FB07056ABA7B259D CRC64;
MGRLRVLLLW LAWWLSQAGI AHGAGSVRLA GGLTLGGLFP VHARGAAGRA CGTLKKEQGV
HRLEAMLYAL DRINADPELL PGVRLGARLL DTCSRDTYAL EQALSFVQAL IRGRGDGEEA
SVRCPGGVPP LRAAPPERVV AVVGASASSV SIMVANVLRL FAIPQISYAS TAPELSDSTR
YDFFSRVVPP DSYQAQAMVD IVRALGWNYV STLASEGNYG ESGVEAFVQI SREAGGVCIA
QSIKIPREPK PGEFHKVIRR LMETPNARGI IIFANEDDIR RVLEATRQAN LTGHFLWVGS
DSWGSKISPI LNLEEEAVGA ITILPKRASI DGFDQYFMTR SLENNRRNIW FAEFWEENFN
CKLTSSGGQS DDSTRKCTGE ERIGQDSTYE QEGKVQFVID AVYAIAHALH SMHQALCPGH
TGLCPAMEPT DGRTLLHYIR AVRFNGSAGT PVMFNENGDA PGRYDIFQYQ ATNGSASSGG
YQAVGQWAEA LRLDMEALQW SGDPHEVPPS QCSLPCGPGE RKKMVKGVPC CWHCEACDGY
RFQVDEFTCE ACPGHMRPTP NHTGCRPTPV VRLTWSSPWA ALPLLLAVLG IMATTTIIAT
FMRHNDTPIV RASGRELSYV LLTGIFLIYA ITFLMVAEPC AAVCASRRLL LGLGTTLSYS
ALLTKTNRIY RIFEQGKRSV TPPPFISPTS QLVITFGLTS LQVVGVIAWL GAQPPHSVID
YEEQRTVDPE QARGVLKCDM SDLSLIGCLG YSLLLMVTCT VYAIKARGVP ETFNEAKPIG
FTMYTTCIIW LAFVPIFFGT AQSAEKIYIQ TTTLTVSLSL SASVSLGMLY VPKTYVILFH
PEQNVQKRKR SLKKTSTMAA PPKSENSEDA K
