Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9W534 (MOODY_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein coupled receptor moody
Gene names
Name:moody
ORF Names:CG4322
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. G-ialpha65A and G-oalpha47A, 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. Ref.5 Ref.6

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.6.

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. Ref.5 Ref.6

Developmental stage

Expressed throughout development and in adults. Ref.6

Disruption phenotype

Flies display an increased sensitivity to cocaine and nicotine exposure. In contrast, sensitivity to the acute intoxicating effects of ethanol is reduced. Ref.6

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A Ref.6 (identifier: Q9W534-1)

Also known as: alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B Ref.6 (identifier: Q9W534-2)

Also known as: beta;

The sequence of this isoform differs from the canonical sequence as follows:
     401-407: KWKDTGL → RNGKIPG
     408-670: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670G-protein coupled receptor moody
PRO_0000355097

Regions

Topological domain1 – 4040Extracellular Potential
Transmembrane41 – 6121Helical; Name=1; Potential
Topological domain62 – 698Cytoplasmic Potential
Transmembrane70 – 9021Helical; Name=2; Potential
Topological domain91 – 11121Extracellular Potential
Transmembrane112 – 13221Helical; Name=3; Potential
Topological domain133 – 15220Cytoplasmic Potential
Transmembrane153 – 17321Helical; Name=4; Potential
Topological domain174 – 20229Extracellular Potential
Transmembrane203 – 22321Helical; Name=5; Potential
Topological domain224 – 31390Cytoplasmic Potential
Transmembrane314 – 33421Helical; Name=6; Potential
Topological domain335 – 34511Extracellular Potential
Transmembrane346 – 36621Helical; Name=7; Potential
Topological domain367 – 670304Cytoplasmic Potential
Compositional bias564 – 58724Pro-rich

Amino acid modifications

Disulfide bond109 ↔ 188 By similarity

Natural variations

Alternative sequence401 – 4077KWKDTGL → RNGKIPG in isoform B. Ref.6
VSP_052910
Alternative sequence408 – 670263Missing in isoform B. Ref.6
VSP_052911

Experimental info

Sequence conflict1061Q → L in AAM51987. Ref.4
Sequence conflict4721N → T in CAA21123. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A (alpha) [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 90B894941A366546

FASTA67071,932
        10         20         30         40         50         60 
MSDETTISLE DGYPPLEALT TMVPPADATG FSQSLLTFAA VMTFLIMIVG ICGNLLTVVA 

        70         80         90        100        110        120 
LLKCPKVRNV AAAFIISLCI ADLLFCALVL PFQGLRFVQG TWRHGQVLCR LIPFIQYGNI 

       130        140        150        160        170        180 
GVSLLCIAMI TINRYVMITH HGLYARIYKR HWIAVMIAAC WLFSYGMQLP TLLGEWGRFG 

       190        200        210        220        230        240 
YDSRLQTCSI MTDDHGHSSK TTLFITAFVI PCLVIIACYA KIFWVVHKSE QRLKRHATKQ 

       250        260        270        280        290        300 
NSIPNNLRPL ASTGSGALPS GAECQPSNRV SSDSSSSFSI DVPETAPSGK QQPTRVKDQR 

       310        320        330        340        350        360 
EVRAKRNEWR ITKMVLAIFL SFVVCYLPIT IVKVADKNVE HPSLHICSYI LLYLSACINP 

       370        380        390        400        410        420 
IIYVIMNKQY RKAYKTVVFC QPARLLLPFG KTNGASSAAE KWKDTGLSNN HSRTIVSQMS 

       430        440        450        460        470        480 
GGTGAASGAG TATGTAAVAV MQTPPEVQQA QALEMVSRGP DLISKSNLPQ PNVTPPPPSV 

       490        500        510        520        530        540 
LTATPNGSNS NSLTLRLPLK KNNHCYTNSG FNSSTPSPSS GLGIGISSSS IYRPGVGSLG 

       550        560        570        580        590        600 
SGSASIRRIT MVGDDIILEE EELPPTPPAT SAPTTPAPPP PSSPLHPLST DSSTTTISGG 

       610        620        630        640        650        660 
AVVAGSSAPK PATPTPHIYM NVDSPKRNQY YMDRNTNAVA PESDSGPANT SATVSISGSK 

       670 
LTAKMKFPKD

« Hide

Isoform B (beta) [UniParc].

Checksum: 86906B70A01C732A
Show »

FASTA40745,173

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
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. expand/collapse author list , 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.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[4]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[5]"GPCR signaling is required for blood-brain barrier formation in Drosophila."
Schwabe T., Bainton R.J., Fetter R.D., Heberlein U., Gaul U.
Cell 123:133-144(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]"moody encodes two GPCRs that regulate cocaine behaviors and blood-brain barrier permeability in Drosophila."
Bainton R.J., Tsai L.T.-Y., Schwabe T., DeSalvo M., Gaul U., Heberlein U.
Cell 123:145-156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014298 Genomic DNA. Translation: AAF45709.2.
AL031765 Genomic DNA. Translation: CAA21123.1.
AY121660 mRNA. Translation: AAM51987.1.
PIRT13739.
RefSeqNP_001188534.1. NM_001201605.2.
NP_001259170.1. NM_001272241.1.
NP_001259171.1. NM_001272242.1.
NP_569970.2. NM_130614.3.
UniGeneDm.12246.

3D structure databases

ProteinModelPortalQ9W534.
SMRQ9W534. Positions 45-380.
ModBaseSearch...

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PaxDbQ9W534.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070341; FBpp0070327; FBgn0025631.
FBtr0303043; FBpp0292162; FBgn0025631.
FBtr0310288; FBpp0301971; FBgn0025631.
FBtr0310289; FBpp0301972; FBgn0025631.
GeneID31168.
KEGGdme:Dmel_CG4322.
UCSCCG4322-RA. d. melanogaster.

Organism-specific databases

CTD31168.
FlyBaseFBgn0025631. moody.

Phylogenomic databases

eggNOGNOG267354.
GeneTreeENSGT00650000093442.
InParanoidQ9W534.
OMACIAMITI.
OrthoDBEOG4J6Q63.
PhylomeDBQ9W534.

Gene expression databases

BgeeQ9W534.

Family and domain databases

InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi31168.
NextBio772266.

Entry information

Entry nameMOODY_DROME
AccessionPrimary (citable) accession number: Q9W534
Secondary accession number(s): O77270, Q8MRD0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2002
Last modified: May 29, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents