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G-protein coupled receptor moody

 MOODY_DROME             Reviewed;         670 AA.
Q9W534; O77270; Q8MRD0;
25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
23-MAY-2018, entry version 132.
RecName: Full=G-protein coupled receptor moody {ECO:0000303|PubMed:16213219};
Name=moody {ECO:0000312|FlyBase:FBgn0025631}; ORFNames=CG4322;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000312|EMBL:AAF45709.2}
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).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF45709.2}
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).
[3] {ECO:0000312|EMBL:CAA21123.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAM51987.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16213218; DOI=10.1016/j.cell.2005.08.037;
Schwabe T., Bainton R.J., Fetter R.D., Heberlein U., Gaul U.;
"GPCR signaling is required for blood-brain barrier formation in
Drosophila.";
Cell 123:133-144(2005).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=16213219; DOI=10.1016/j.cell.2005.07.029;
Bainton R.J., Tsai L.T.-Y., Schwabe T., DeSalvo M., Gaul U.,
Heberlein U.;
"moody encodes two GPCRs that regulate cocaine behaviors and blood-
brain barrier permeability in Drosophila.";
Cell 123:145-156(2005).
-!- FUNCTION: Isoform A and isoform B are required in glia to regulate
the acute sensitivity to cocaine and to continuously maintain the
proper blood-brain barrier (BBB) function. A moody-mediated
signaling pathway functions in glia to regulate nervous system
insulation and drug-related behaviors. Galphai and Galphao, and
the regulator of G protein signaling, loco, are required in the
surface glia to achieve effective insulation. The components
function by regulating the cortical actin and thereby stabilizing
the extended morphology of the surface glia, which in turn is
necessary for the formation of septate junctions of sufficient
length to achieve proper sealing of the nerve cord.
{ECO:0000269|PubMed:16213218, ECO:0000269|PubMed:16213219}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16213219};
Multi-pass membrane protein {ECO:0000269|PubMed:16213219}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A {ECO:0000269|PubMed:16213219}; Synonyms=alpha
{ECO:0000269|PubMed:16213219};
IsoId=Q9W534-1; Sequence=Displayed;
Name=B {ECO:0000269|PubMed:16213219}; Synonyms=beta
{ECO:0000269|PubMed:16213219};
IsoId=Q9W534-2; Sequence=VSP_052910, VSP_052911;
-!- TISSUE SPECIFICITY: Isoform A and isoform B are expressed in the
head. Isoform B only is expressed in the body. Expressed in
embryonic glial cells that are involved in ensheathment and
insulation of the nervous system. Both isoforms are expressed in
glia that insulate the larval and adult nervous system. Also
expressed in the germ cells, the gut, and the heart.
{ECO:0000269|PubMed:16213218, ECO:0000269|PubMed:16213219}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development and in
adults. {ECO:0000269|PubMed:16213219}.
-!- DISRUPTION PHENOTYPE: Mutant flies display an increased
sensitivity to cocaine and nicotine exposure. In contrast,
sensitivity to the acute intoxicating effects of ethanol is
reduced. {ECO:0000269|PubMed:16213219}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; AE014298; AAF45709.2; -; Genomic_DNA.
EMBL; AL031765; CAA21123.1; -; Genomic_DNA.
EMBL; AY121660; AAM51987.1; -; mRNA.
PIR; T13739; T13739.
RefSeq; NP_001188534.1; NM_001201605.2. [Q9W534-1]
RefSeq; NP_001259170.1; NM_001272241.2. [Q9W534-1]
RefSeq; NP_001259171.1; NM_001272242.2. [Q9W534-1]
RefSeq; NP_569970.2; NM_130614.4. [Q9W534-1]
UniGene; Dm.12246; -.
ProteinModelPortal; Q9W534; -.
BioGrid; 57712; 1.
STRING; 7227.FBpp0292162; -.
PaxDb; Q9W534; -.
PRIDE; Q9W534; -.
EnsemblMetazoa; FBtr0070341; FBpp0070327; FBgn0025631. [Q9W534-1]
EnsemblMetazoa; FBtr0303043; FBpp0292162; FBgn0025631. [Q9W534-1]
EnsemblMetazoa; FBtr0310288; FBpp0301971; FBgn0025631. [Q9W534-1]
EnsemblMetazoa; FBtr0310289; FBpp0301972; FBgn0025631. [Q9W534-1]
GeneID; 31168; -.
KEGG; dme:Dmel_CG4322; -.
UCSC; CG4322-RA; d. melanogaster. [Q9W534-1]
CTD; 31168; -.
FlyBase; FBgn0025631; moody.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00840000129973; -.
InParanoid; Q9W534; -.
OrthoDB; EOG091G04YE; -.
PhylomeDB; Q9W534; -.
Reactome; R-DME-6798695; Neutrophil degranulation.
GenomeRNAi; 31168; -.
PRO; PR:Q9W534; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0025631; -.
ExpressionAtlas; Q9W534; baseline and differential.
Genevisible; Q9W534; DM.
GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0005919; C:pleated septate junction; IDA:FlyBase.
GO; GO:0004930; F:G-protein coupled receptor activity; IMP:UniProtKB.
GO; GO:0008366; P:axon ensheathment; IMP:UniProtKB.
GO; GO:0048148; P:behavioral response to cocaine; IMP:FlyBase.
GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
GO; GO:0035095; P:behavioral response to nicotine; IMP:FlyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Membrane; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 670 G-protein coupled receptor moody.
/FTId=PRO_0000355097.
TOPO_DOM 1 40 Extracellular. {ECO:0000255}.
TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 62 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 91 111 Extracellular. {ECO:0000255}.
TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 133 152 Cytoplasmic. {ECO:0000255}.
TRANSMEM 153 173 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 174 202 Extracellular. {ECO:0000255}.
TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 224 313 Cytoplasmic. {ECO:0000255}.
TRANSMEM 314 334 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 335 345 Extracellular. {ECO:0000255}.
TRANSMEM 346 366 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 367 670 Cytoplasmic. {ECO:0000255}.
COMPBIAS 564 587 Pro-rich. {ECO:0000255}.
DISULFID 109 188 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 401 407 KWKDTGL -> RNGKIPG (in isoform B).
{ECO:0000303|PubMed:16213219}.
/FTId=VSP_052910.
VAR_SEQ 408 670 Missing (in isoform B).
{ECO:0000303|PubMed:16213219}.
/FTId=VSP_052911.
CONFLICT 106 106 Q -> L (in Ref. 4; AAM51987).
{ECO:0000305}.
CONFLICT 472 472 N -> T (in Ref. 3; CAA21123).
{ECO:0000305}.
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


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