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Metabotropic glutamate receptor 6 (mGluR6)

 GRM6_MOUSE              Reviewed;         871 AA.
Q5NCH9;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 1.
28-MAR-2018, entry version 102.
RecName: Full=Metabotropic glutamate receptor 6;
Short=mGluR6;
Flags: Precursor;
Name=Grm6; Synonyms=Gprc1f, Mglur6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=7889569; DOI=10.1016/0092-8674(95)90354-2;
Masu M., Iwakabe H., Tagawa Y., Miyoshi T., Yamashita M., Fukuda Y.,
Sasaki H., Hiroi K., Nakamura Y., Shigemoto R., Takada M.,
Nakamura K., Nakao K., Katsuki M., Nakanishi S.;
"Specific deficit of the ON response in visual transmission by
targeted disruption of the mGluR6 gene.";
Cell 80:757-765(1995).
[3]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9144650; DOI=10.1016/S0028-3908(96)00167-0;
Iwakabe H., Katsuura G., Ishibashi C., Nakanishi S.;
"Impairment of pupillary responses and optokinetic nystagmus in the
mGluR6-deficient mouse.";
Neuropharmacology 36:135-143(1997).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18001285; DOI=10.1111/j.1460-9568.2007.05867.x;
Morgans C.W., Wensel T.G., Brown R.L., Perez-Leon J.A., Bearnot B.,
Duvoisin R.M.;
"Gbeta5-RGS complexes co-localize with mGluR6 in retinal ON-bipolar
cells.";
Eur. J. Neurosci. 26:2899-2905(2007).
[5]
SUBCELLULAR LOCATION.
PubMed=18952919; DOI=10.1167/iovs.08-2758;
Specht D., Wu S.B., Turner P., Dearden P., Koentgen F., Wolfrum U.,
Maw M., Brandstatter J.H., tom Dieck S.;
"Effects of presynaptic mutations on a postsynaptic Cacna1s calcium
channel colocalized with mGluR6 at mouse photoreceptor ribbon
synapses.";
Invest. Ophthalmol. Vis. Sci. 50:505-515(2009).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=22131384; DOI=10.1152/jn.00933.2011;
Xu Y., Dhingra A., Fina M.E., Koike C., Furukawa T., Vardi N.;
"mGluR6 deletion renders the TRPM1 channel in retina inactive.";
J. Neurophysiol. 107:948-957(2012).
-!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
causes a conformation change that triggers signaling via guanine
nucleotide-binding proteins (G proteins) and modulates the
activity of down-stream effectors, such as adenylate cyclase.
Signaling inhibits adenylate cyclase activity (By similarity).
Signaling stimulates TRPM1 channel activity and Ca(2+) uptake.
Required for normal vision. {ECO:0000250,
ECO:0000269|PubMed:22131384, ECO:0000269|PubMed:9144650}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}. Cell projection,
dendrite. Note=Subject to trafficking from the endoplasmic
reticulum to the Golgi apparatus and then to the cell membrane (By
similarity). Detected at dendritic tips of bipolar cells.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in the outer plexiform layer in
retina (at protein level). {ECO:0000269|PubMed:18001285,
ECO:0000269|PubMed:7889569}.
-!- DISRUPTION PHENOTYPE: Retinal cells from mutant mice display a
subtly altered response to cycles of light and darkness, due to a
failure of the ON bipolar cells in the retina to become
depolarized in response to light. As a consequence, mutant mice
display little or no pupillary contraction in adaptation to low
light intensity. Besides, they exhibit strongly impaired responses
to moving stimuli, and fail to produce a response when the visual
constrast is low. Besides, rod bipolar cells from mutant mice lack
TRPM1 channel activity. {ECO:0000269|PubMed:22131384,
ECO:0000269|PubMed:7889569, ECO:0000269|PubMed:9144650}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL627215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS48785.1; -.
RefSeq; NP_775548.2; NM_173372.2.
RefSeq; XP_006532024.1; XM_006531961.2.
UniGene; Mm.134265; -.
ProteinModelPortal; Q5NCH9; -.
SMR; Q5NCH9; -.
BioGrid; 223810; 1.
STRING; 10090.ENSMUSP00000000631; -.
iPTMnet; Q5NCH9; -.
PhosphoSitePlus; Q5NCH9; -.
PaxDb; Q5NCH9; -.
PRIDE; Q5NCH9; -.
Ensembl; ENSMUST00000000631; ENSMUSP00000000631; ENSMUSG00000000617.
Ensembl; ENSMUST00000171427; ENSMUSP00000130728; ENSMUSG00000000617.
GeneID; 108072; -.
KEGG; mmu:108072; -.
UCSC; uc007isu.2; mouse.
CTD; 2916; -.
MGI; MGI:1351343; Grm6.
eggNOG; KOG1056; Eukaryota.
eggNOG; ENOG410XR6W; LUCA.
GeneTree; ENSGT00760000118884; -.
HOGENOM; HOG000218635; -.
HOVERGEN; HBG107965; -.
InParanoid; Q5NCH9; -.
KO; K04608; -.
OMA; YAIKARG; -.
OrthoDB; EOG091G177R; -.
PhylomeDB; Q5NCH9; -.
TreeFam; TF313240; -.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
ChiTaRS; Grm6; mouse.
PRO; PR:Q5NCH9; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000617; -.
CleanEx; MM_GRM6; -.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0035841; C:new growing cell tip; IDA:MGI.
GO; GO:0045211; C:postsynaptic membrane; TAS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
GO; GO:0001642; F:group III metabotropic glutamate receptor activity; TAS:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISS:UniProtKB.
GO; GO:0007216; P:G-protein coupled glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0050953; P:sensory perception of light stimulus; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IGI:MGI.
GO; GO:0007601; P:visual perception; TAS:UniProtKB.
Gene3D; 2.10.50.30; -; 1.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR000337; GPCR_3.
InterPro; IPR011500; GPCR_3_9-Cys_dom.
InterPro; IPR038550; GPCR_3_9-Cys_sf.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR000162; GPCR_3_mtglu_rcpt.
InterPro; IPR000112; GPCR_3_mtglu_rcpt_6.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF07562; NCD3G; 1.
PRINTS; PR00248; GPCRMGR.
PRINTS; PR01056; MTABOTROPC6R.
PRINTS; PR00593; MTABOTROPICR.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome; Disulfide bond;
Endoplasmic reticulum; G-protein coupled receptor; Glycoprotein;
Golgi apparatus; Membrane; Receptor; Reference proteome;
Sensory transduction; Signal; Transducer; Transmembrane;
Transmembrane helix; Vision.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 871 Metabotropic glutamate receptor 6.
/FTId=PRO_0000012935.
TOPO_DOM 24 579 Extracellular. {ECO:0000255}.
TRANSMEM 580 602 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 603 616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 617 637 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 638 648 Extracellular. {ECO:0000255}.
TRANSMEM 649 667 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 668 691 Cytoplasmic. {ECO:0000255}.
TRANSMEM 692 712 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 713 742 Extracellular. {ECO:0000255}.
TRANSMEM 743 764 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 765 777 Cytoplasmic. {ECO:0000255}.
TRANSMEM 778 800 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 801 813 Extracellular. {ECO:0000255}.
TRANSMEM 814 839 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 840 871 Cytoplasmic. {ECO:0000255}.
REGION 169 171 Glutamate binding. {ECO:0000250}.
BINDING 148 148 Glutamate. {ECO:0000250}.
BINDING 219 219 Glutamate. {ECO:0000250}.
BINDING 301 301 Glutamate. {ECO:0000250}.
BINDING 394 394 Glutamate. {ECO:0000250}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 473 473 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 93 {ECO:0000250}.
DISULFID 238 530 {ECO:0000250}.
DISULFID 361 377 {ECO:0000250}.
DISULFID 417 424 {ECO:0000250}.
DISULFID 512 531 {ECO:0000250}.
DISULFID 516 534 {ECO:0000250}.
DISULFID 537 549 {ECO:0000250}.
DISULFID 552 565 {ECO:0000250}.
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


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