ID GRM_DROME Reviewed; 976 AA.
AC P91685; Q9V485;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 24-JAN-2024, entry version 181.
DE RecName: Full=Metabotropic glutamate receptor;
DE Short=DmGluRA;
DE Flags: Precursor;
GN Name=mGluR; Synonyms=Glu-RA, GluRA, mGluRA; ORFNames=CG11144;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=8824309; DOI=10.1523/jneurosci.16-21-06687.1996;
RA Parmentier M.L., Pin J.P., Bockaert J., Grau Y.;
RT "Cloning and functional expression of a Drosophila metabotropic glutamate
RT receptor expressed in the embryonic CNS.";
RL J. Neurosci. 16:6687-6694(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP FUNCTION.
RX PubMed=10821630; DOI=10.1016/s0304-3940(99)00294-3;
RA Raymond V., Hamon A., Grau Y., Lapied B.;
RT "DmGluRA, a Drosophila metabotropic glutamate receptor, activates G-protein
RT inwardly rectifying potassium channels in Xenopus oocytes.";
RL Neurosci. Lett. 269:1-4(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11536189; DOI=10.1002/cne.1310;
RA Ramaekers A., Parmentier M.L., Lasnier C., Bockaert J., Grau Y.;
RT "Distribution of metabotropic glutamate receptor DmGlu-A in Drosophila
RT melanogaster central nervous system.";
RL J. Comp. Neurol. 438:213-225(2001).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
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. {ECO:0000269|PubMed:10821630,
CC ECO:0000269|PubMed:8824309}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8824309};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8824309}.
CC -!- TISSUE SPECIFICITY: Expressed in the neurons of the larval CNS from the
CC beginning of the first until the third instar. Expression in the third-
CC instar larval CNS is restricted to a discrete number of somas and
CC projections in the brain lobes and in the ventral ganglion. In the
CC ventral nerve cord, expression is detected both in somas and
CC projections. Expressed in the antennal lobes, the optic lobes, the
CC central complex and the median bundle in the adult CNS.
CC {ECO:0000269|PubMed:11536189}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the CNS of the late embryo.
CC {ECO:0000269|PubMed:8824309}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; X99675; CAA67993.1; -; mRNA.
DR EMBL; AE014135; AAF59402.1; -; Genomic_DNA.
DR RefSeq; NP_001259076.1; NM_001272147.1.
DR RefSeq; NP_524639.2; NM_079900.3.
DR AlphaFoldDB; P91685; -.
DR SMR; P91685; -.
DR BioGRID; 68663; 7.
DR DIP; DIP-19294N; -.
DR IntAct; P91685; 1.
DR STRING; 7227.FBpp0305080; -.
DR GlyCosmos; P91685; 7 sites, No reported glycans.
DR GlyGen; P91685; 7 sites.
DR iPTMnet; P91685; -.
DR PaxDb; 7227-FBpp0305080; -.
DR DNASU; 43838; -.
DR EnsemblMetazoa; FBtr0089184; FBpp0088248; FBgn0019985.
DR EnsemblMetazoa; FBtr0332858; FBpp0305080; FBgn0019985.
DR GeneID; 43838; -.
DR KEGG; dme:Dmel_CG11144; -.
DR AGR; FB:FBgn0019985; -.
DR CTD; 43838; -.
DR FlyBase; FBgn0019985; mGluR.
DR VEuPathDB; VectorBase:FBgn0019985; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; P91685; -.
DR OMA; ILKCNIQ; -.
DR OrthoDB; 1331864at2759; -.
DR PhylomeDB; P91685; -.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR BioGRID-ORCS; 43838; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43838; -.
DR PRO; PR:P91685; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0019985; Expressed in brain and 6 other cell types or tissues.
DR ExpressionAtlas; P91685; baseline and differential.
DR Genevisible; P91685; DM.
DR GO; GO:0038038; C:G protein-coupled receptor homodimeric complex; ISS:FlyBase.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0045121; C:membrane raft; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0015485; F:cholesterol binding; IDA:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:FlyBase.
DR GO; GO:0016595; F:glutamate binding; IDA:FlyBase.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:FlyBase.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IDA:FlyBase.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
DR CDD; cd15934; 7tmC_mGluRs_group2_3; 1.
DR CDD; cd06375; PBP1_mGluR_groupII; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
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 PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR24060:SF158; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR00593; MTABOTROPICR.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..976
FT /note="Metabotropic glutamate receptor"
FT /id="PRO_0000012944"
FT TOPO_DOM 26..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..649
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..695
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..714
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..759
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..782
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..804
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..840
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..850
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 851..876
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 920..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 179..181
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 834
FT /note="V -> A (in Ref. 1; CAA67993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 108486 MW; 43A0E1F918EDACC4 CRC64;
MKQKNNNGTI LVVVMVLSWS RVVDLKSPSN THTQDSVSVS LPGDIILGGL FPVHEKGEGA
PCGPKVYNRG VQRLEAMLYA IDRVNNDPNI LPGITIGVHI LDTCSRDTYA LNQSLQFVRA
SLNNLDTSGY ECADGSSPQL RKNASSGPVF GVIGGSYSSV SLQVANLLRL FHIPQVSPAS
TAKTLSDKTR FDLFARTVPP DTFQSVALVD ILKNFNWSYV STIHSEGSYG EYGIEALHKE
ATERNVCIAV AEKVPSAADD KVFDSIISKL QKKPNARGVV LFTRAEDARR ILQAAKRANL
SQPFHWIASD GWGKQQKLLE GLEDIAEGAI TVELQSEIIA DFDRYMMQLT PETNQRNPWF
AEYWEDTFNC VLTSLSVKPD TSNSANSTDN KIGVKAKTEC DDSYRLSEKV GYEQESKTQF
VVDAVYAFAY ALHNLHNDRC NTQSDQTTET RKHLQSESVW YRKISTDTKS QACPDMANYD
GKEFYNNYLL NVSFIDLAGS EVKFDRQGDG LARYDILNYQ RQENSSGYQY KVIGKWFNGL
QLNSETVVWN KETEQPTSAC SLPCEVGMIK KQQGDTCCWI CDSCESFEYV YDEFTCKDCG
PGLWPYADKL SCYALDIQYM KWNSLFALIP MAIAIFGIAL TSIVIVLFAK NHDTPLVRAS
GRELSYTLLF GILVCYCNTF ALIAKPTIGS CVLQRFGIGV GFSIIYSALL TKTNRISRIF
HSASKSAQRL KYISPQSQVV ITTSLIAIQV LITMIWMVVE PPGTRFYYPD RREVILKCKI
QDMSFLFSQL YNMILITICT IYAIKTRKIP ENFNESKFIG FTMYTTCIIW LAFVPIYFGT
GNSYEVQTTT LCISISLSAS VALVCLYSPK VYILVFHPDK NVRKLTMNST VYRRSAAAVA
QGAPTSSGYS RTHAPGTSAL TGGAVGTNAS SSTLPTQNSP HLDEASAQTN VAHKTNGEFL
PEVGERVEPI CHIVNK
//
