MOODY_DROME
ID MOODY_DROME Reviewed; 670 AA.
AC Q9W534; O77270; Q8MRD0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=G-protein coupled receptor moody {ECO:0000303|PubMed:16213219};
GN Name=moody {ECO:0000312|FlyBase:FBgn0025631}; ORFNames=CG4322;
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] {ECO:0000312|EMBL:AAF45709.2}
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF45709.2}
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 [3] {ECO:0000312|EMBL:CAA21123.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAM51987.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16213218; DOI=10.1016/j.cell.2005.08.037;
RA Schwabe T., Bainton R.J., Fetter R.D., Heberlein U., Gaul U.;
RT "GPCR signaling is required for blood-brain barrier formation in
RT Drosophila.";
RL Cell 123:133-144(2005).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16213219; DOI=10.1016/j.cell.2005.07.029;
RA Bainton R.J., Tsai L.T.-Y., Schwabe T., DeSalvo M., Gaul U., Heberlein U.;
RT "moody encodes two GPCRs that regulate cocaine behaviors and blood-brain
RT barrier permeability in Drosophila.";
RL Cell 123:145-156(2005).
CC -!- FUNCTION: Isoform A and isoform B are required in glia to regulate the
CC acute sensitivity to cocaine and to continuously maintain the proper
CC blood-brain barrier (BBB) function. A moody-mediated signaling pathway
CC functions in glia to regulate nervous system insulation and drug-
CC related behaviors. Galphai and Galphao, and the regulator of G protein
CC signaling, loco, are required in the surface glia to achieve effective
CC insulation. The components function by regulating the cortical actin
CC and thereby stabilizing the extended morphology of the surface glia,
CC which in turn is necessary for the formation of septate junctions of
CC sufficient length to achieve proper sealing of the nerve cord.
CC {ECO:0000269|PubMed:16213218, ECO:0000269|PubMed:16213219}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16213219};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16213219}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:16213219}; Synonyms=alpha
CC {ECO:0000269|PubMed:16213219};
CC IsoId=Q9W534-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:16213219}; Synonyms=beta
CC {ECO:0000269|PubMed:16213219};
CC IsoId=Q9W534-2; Sequence=VSP_052910, VSP_052911;
CC -!- TISSUE SPECIFICITY: Isoform A and isoform B are expressed in the head.
CC Isoform B only is expressed in the body. Expressed in embryonic glial
CC cells that are involved in ensheathment and insulation of the nervous
CC system. Both isoforms are expressed in glia that insulate the larval
CC and adult nervous system. Also expressed in the germ cells, the gut,
CC and the heart. {ECO:0000269|PubMed:16213218,
CC ECO:0000269|PubMed:16213219}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adults.
CC {ECO:0000269|PubMed:16213219}.
CC -!- DISRUPTION PHENOTYPE: Mutant flies display an increased sensitivity to
CC cocaine and nicotine exposure. In contrast, sensitivity to the acute
CC intoxicating effects of ethanol is reduced.
CC {ECO:0000269|PubMed:16213219}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AE014298; AAF45709.2; -; Genomic_DNA.
DR EMBL; AL031765; CAA21123.1; -; Genomic_DNA.
DR EMBL; AY121660; AAM51987.1; -; mRNA.
DR PIR; T13739; T13739.
DR RefSeq; NP_001188534.1; NM_001201605.2. [Q9W534-1]
DR RefSeq; NP_001259170.1; NM_001272241.2. [Q9W534-1]
DR RefSeq; NP_001259171.1; NM_001272242.2. [Q9W534-1]
DR RefSeq; NP_569970.2; NM_130614.4. [Q9W534-1]
DR AlphaFoldDB; Q9W534; -.
DR SMR; Q9W534; -.
DR BioGRID; 57712; 1.
DR STRING; 7227.FBpp0292162; -.
DR PaxDb; Q9W534; -.
DR EnsemblMetazoa; FBtr0070341; FBpp0070327; FBgn0025631. [Q9W534-1]
DR EnsemblMetazoa; FBtr0303043; FBpp0292162; FBgn0025631. [Q9W534-1]
DR EnsemblMetazoa; FBtr0310288; FBpp0301971; FBgn0025631. [Q9W534-1]
DR EnsemblMetazoa; FBtr0310289; FBpp0301972; FBgn0025631. [Q9W534-1]
DR GeneID; 31168; -.
DR KEGG; dme:Dmel_CG4322; -.
DR UCSC; CG4322-RA; d. melanogaster. [Q9W534-1]
DR CTD; 31168; -.
DR FlyBase; FBgn0025631; moody.
DR VEuPathDB; VectorBase:FBgn0025631; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000170714; -.
DR HOGENOM; CLU_421673_0_0_1; -.
DR InParanoid; Q9W534; -.
DR PhylomeDB; Q9W534; -.
DR Reactome; R-DME-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-DME-375276; Peptide ligand-binding receptors.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 31168; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31168; -.
DR PRO; PR:Q9W534; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0025631; Expressed in somatic cell and 66 other tissues.
DR ExpressionAtlas; Q9W534; baseline and differential.
DR Genevisible; Q9W534; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005919; C:pleated septate junction; IDA:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR GO; GO:0008366; P:axon ensheathment; IMP:UniProtKB.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Membrane; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..670
FT /note="G-protein coupled receptor moody"
FT /id="PRO_0000355097"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 258..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 109..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 401..407
FT /note="KWKDTGL -> RNGKIPG (in isoform B)"
FT /evidence="ECO:0000303|PubMed:16213219"
FT /id="VSP_052910"
FT VAR_SEQ 408..670
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:16213219"
FT /id="VSP_052911"
FT CONFLICT 106
FT /note="Q -> L (in Ref. 4; AAM51987)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="N -> T (in Ref. 3; CAA21123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 71932 MW; 90B894941A366546 CRC64;
MSDETTISLE DGYPPLEALT TMVPPADATG FSQSLLTFAA VMTFLIMIVG ICGNLLTVVA
LLKCPKVRNV AAAFIISLCI ADLLFCALVL PFQGLRFVQG TWRHGQVLCR LIPFIQYGNI
GVSLLCIAMI TINRYVMITH HGLYARIYKR HWIAVMIAAC WLFSYGMQLP TLLGEWGRFG
YDSRLQTCSI MTDDHGHSSK TTLFITAFVI PCLVIIACYA KIFWVVHKSE QRLKRHATKQ
NSIPNNLRPL ASTGSGALPS GAECQPSNRV SSDSSSSFSI DVPETAPSGK QQPTRVKDQR
EVRAKRNEWR ITKMVLAIFL SFVVCYLPIT IVKVADKNVE HPSLHICSYI LLYLSACINP
IIYVIMNKQY RKAYKTVVFC QPARLLLPFG KTNGASSAAE KWKDTGLSNN HSRTIVSQMS
GGTGAASGAG TATGTAAVAV MQTPPEVQQA QALEMVSRGP DLISKSNLPQ PNVTPPPPSV
LTATPNGSNS NSLTLRLPLK KNNHCYTNSG FNSSTPSPSS GLGIGISSSS IYRPGVGSLG
SGSASIRRIT MVGDDIILEE EELPPTPPAT SAPTTPAPPP PSSPLHPLST DSSTTTISGG
AVVAGSSAPK PATPTPHIYM NVDSPKRNQY YMDRNTNAVA PESDSGPANT SATVSISGSK
LTAKMKFPKD
