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Metabotropic glutamate receptor (DmGluRA)

 GRM_DROME               Reviewed;         976 AA.
P91685; Q9V485;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
22-NOV-2017, entry version 152.
RecName: Full=Metabotropic glutamate receptor;
Short=DmGluRA;
Flags: Precursor;
Name=mGluR; Synonyms=Glu-RA, GluRA, mGluRA; ORFNames=CG11144;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=8824309;
Parmentier M.L., Pin J.P., Bockaert J., Grau Y.;
"Cloning and functional expression of a Drosophila metabotropic
glutamate receptor expressed in the embryonic CNS.";
J. Neurosci. 16:6687-6694(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
FUNCTION.
PubMed=10821630; DOI=10.1016/S0304-3940(99)00294-3;
Raymond V., Hamon A., Grau Y., Lapied B.;
"DmGluRA, a Drosophila metabotropic glutamate receptor, activates G-
protein inwardly rectifying potassium channels in Xenopus oocytes.";
Neurosci. Lett. 269:1-4(1999).
[5]
TISSUE SPECIFICITY.
PubMed=11536189; DOI=10.1002/cne.1310;
Ramaekers A., Parmentier M.L., Lasnier C., Bockaert J., Grau Y.;
"Distribution of metabotropic glutamate receptor DmGlu-A in Drosophila
melanogaster central nervous system.";
J. Comp. Neurol. 438:213-225(2001).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
-!- 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. {ECO:0000269|PubMed:10821630,
ECO:0000269|PubMed:8824309}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8824309};
Multi-pass membrane protein {ECO:0000269|PubMed:8824309}.
-!- TISSUE SPECIFICITY: Expressed in the neurons of the larval CNS
from the beginning of the first until the third instar. Expression
in the third-instar larval CNS is restricted to a discrete number
of somas and projections in the brain lobes and in the ventral
ganglion. In the ventral nerve cord, expression is detected both
in somas and projections. Expressed in the antennal lobes, the
optic lobes, the central complex and the median bundle in the
adult CNS. {ECO:0000269|PubMed:11536189}.
-!- DEVELOPMENTAL STAGE: Expressed in the CNS of the late embryo.
{ECO:0000269|PubMed:8824309}.
-!- 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; X99675; CAA67993.1; -; mRNA.
EMBL; AE014135; AAF59402.1; -; Genomic_DNA.
RefSeq; NP_001259076.1; NM_001272147.1.
RefSeq; NP_524639.2; NM_079900.3.
UniGene; Dm.1789; -.
ProteinModelPortal; P91685; -.
SMR; P91685; -.
BioGrid; 68663; 6.
DIP; DIP-19294N; -.
IntAct; P91685; 1.
MINT; MINT-1643069; -.
STRING; 7227.FBpp0305080; -.
iPTMnet; P91685; -.
PaxDb; P91685; -.
PRIDE; P91685; -.
EnsemblMetazoa; FBtr0089184; FBpp0088248; FBgn0019985.
EnsemblMetazoa; FBtr0332858; FBpp0305080; FBgn0019985.
GeneID; 43838; -.
KEGG; dme:Dmel_CG11144; -.
CTD; 43838; -.
FlyBase; FBgn0019985; mGluR.
eggNOG; KOG1056; Eukaryota.
eggNOG; ENOG410XR6W; LUCA.
GeneTree; ENSGT00760000118884; -.
InParanoid; P91685; -.
KO; K04605; -.
OMA; TYVPTVC; -.
OrthoDB; EOG091G177R; -.
PhylomeDB; P91685; -.
Reactome; R-DME-418594; G alpha (i) signalling events.
Reactome; R-DME-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
GenomeRNAi; 43838; -.
PRO; PR:P91685; -.
Proteomes; UP000000803; Chromosome 4.
Bgee; FBgn0019985; -.
ExpressionAtlas; P91685; differential.
Genevisible; P91685; DM.
GO; GO:0038038; C:G-protein coupled receptor homodimeric complex; ISS:FlyBase.
GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0045121; C:membrane raft; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0015485; F:cholesterol binding; IDA:FlyBase.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:FlyBase.
GO; GO:0016595; F:glutamate binding; IDA:FlyBase.
GO; GO:0008066; F:glutamate receptor activity; ISS:FlyBase.
GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IDA:FlyBase.
GO; GO:0007216; P:G-protein coupled glutamate receptor signaling pathway; IDA:FlyBase.
GO; GO:0007612; P:learning; IMP:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:FlyBase.
GO; GO:0007614; P:short-term memory; IMP:FlyBase.
GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR000337; GPCR_3.
InterPro; IPR011500; GPCR_3_9-Cys_dom.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR000162; GPCR_3_mtglu_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF07562; NCD3G; 1.
PRINTS; PR00248; GPCRMGR.
PRINTS; PR00593; MTABOTROPICR.
SUPFAM; SSF53822; SSF53822; 2.
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; Complete proteome; G-protein coupled receptor;
Glycoprotein; Membrane; Receptor; Reference proteome; Signal;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 976 Metabotropic glutamate receptor.
/FTId=PRO_0000012944.
TOPO_DOM 26 626 Extracellular. {ECO:0000255}.
TRANSMEM 627 649 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 650 663 Cytoplasmic. {ECO:0000255}.
TRANSMEM 664 684 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 685 695 Extracellular. {ECO:0000255}.
TRANSMEM 696 714 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 715 738 Cytoplasmic. {ECO:0000255}.
TRANSMEM 739 759 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 760 782 Extracellular. {ECO:0000255}.
TRANSMEM 783 804 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 805 817 Cytoplasmic. {ECO:0000255}.
TRANSMEM 818 840 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 841 850 Extracellular. {ECO:0000255}.
TRANSMEM 851 876 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 877 976 Cytoplasmic. {ECO:0000255}.
REGION 179 181 Glutamate binding. {ECO:0000250}.
BINDING 158 158 Glutamate. {ECO:0000250}.
BINDING 229 229 Glutamate. {ECO:0000250}.
BINDING 310 310 Glutamate. {ECO:0000250}.
BINDING 417 417 Glutamate. {ECO:0000250}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 834 834 V -> A (in Ref. 1; CAA67993).
{ECO:0000305}.
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


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