GRM6_RABIT
ID GRM6_RABIT Reviewed; 868 AA.
AC Q863I4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Metabotropic glutamate receptor 6;
DE Short=mGluR6;
DE Flags: Precursor;
GN Name=GRM6;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Retina;
RA Keung J.W., Massey S.C.;
RT "Cloning of mGluR6 in the rabbit retina.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC projection, dendrite {ECO:0000250}. Note=Subject to trafficking from
CC the endoplasmic reticulum to the Golgi apparatus and then to the cell
CC membrane. Detected at dendritic tips of bipolar cells (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AY275542; AAP31684.1; -; mRNA.
DR RefSeq; NP_001076204.1; NM_001082735.1.
DR AlphaFoldDB; Q863I4; -.
DR SMR; Q863I4; -.
DR STRING; 9986.ENSOCUP00000014505; -.
DR PRIDE; Q863I4; -.
DR GeneID; 100009501; -.
DR KEGG; ocu:100009501; -.
DR CTD; 2916; -.
DR eggNOG; KOG1056; Eukaryota.
DR InParanoid; Q863I4; -.
DR OrthoDB; 1154468at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
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:1905665; P:positive regulation of calcium ion import across plasma membrane; ISS: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 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..868
FT /note="Metabotropic glutamate receptor 6"
FT /id="PRO_0000012936"
FT TOPO_DOM 21..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..599
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..664
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..739
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..761
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..774
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..797
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..810
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 811..836
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 837..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 845..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 166..168
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..90
FT /evidence="ECO:0000250"
FT DISULFID 235..527
FT /evidence="ECO:0000250"
FT DISULFID 358..374
FT /evidence="ECO:0000250"
FT DISULFID 414..421
FT /evidence="ECO:0000250"
FT DISULFID 509..528
FT /evidence="ECO:0000250"
FT DISULFID 513..531
FT /evidence="ECO:0000250"
FT DISULFID 534..546
FT /evidence="ECO:0000250"
FT DISULFID 549..562
FT /evidence="ECO:0000250"
SQ SEQUENCE 868 AA; 94469 MW; BC50CA12FFAD65DD CRC64;
MARLLLALLA WLAQMSPVRA AGSVRLAGGL TLGGLFPVHA RGAAGRACGQ LKKEQGVHRL
EAMLYALDRV NADPELLPGV RLGARLLDTC SRDTYALEQA LSFVQALIRG RGDGDEAAVR
CPGGVPPLRA APPERVVAVV GASASSVSIM VANVLRLFAI PQISYASTAP ELSDSTRYDF
FSRVVPPDSY QAQAMVDIVR ALGWNYVSTL ASEGNYGESG VEAFVQISRE AGGVCIAQSI
KIPREPKPGE FNKVIKRLME TPNARGIIIF ANEDDIRRVL EATRQANLTG HFLWVGSDSW
GSKTSPVLSL EDVAVGAITI LPKRASIDGF DQYFMTRSLE NNRRNIWFAE FWEENFNCKL
TSSGGQSDEA TRKCTGEERI GQDSAYEQEG KVQFVIDAVY AIAHALHSMH QALCPGYTGL
CPAMEPTDGR TLLQYIRAVR FNGSAGTPVM FNENGDAPGR YDIFQYQATN GSASSGGYQV
VGQWAEALRL DVEALQWSGD PHEVPPSQCS LPCGPGERKK MVKGVPCCWH CEACDGYRFQ
VDEFTCEACP RDMRPTPNHT GCRPTPVVRL TWSSPWAAPP LLLAVLGIMA TTTVVGTFVR
HNNTPIVRAS GRELSYVLLT GIFLIYAVTF LMVAEPGAAV CATRRLFLGL GTTLSYSALL
TKTNRIYRIF EQGKRSVTPP PFISPTSQLV ITFSLTSLQV VGVIAWLGAQ PPHSVIDYEE
QRTVDPEQAR GVLKCDMSDL SLIGCLGYSL LLMVTCTVYA IKARGVPETF NEAKPIGFTM
YTTCIVWLAF VPIFFGTAQS AEKIYIQTTT LTVSLSLSAS VSLGMLYVPK TYVILFHPEQ
NVQKRKRSLK TTSTVAAPPK GADTEDPK
