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Q9V3T9 (ADRO_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH:adrenodoxin oxidoreductase, mitochondrial

Short name=AR
Short name=Adrenodoxin reductase
EC=1.18.1.2
Alternative name(s):
Ferredoxin--NADP(+) reductase
Short name=Ferredoxin reductase
Gene names
Name:dare
ORF Names:CG12390
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Required for synthesis of steroid hormones, for olfactory sensory behavior and completion of the second larval molt (a steroid mediated developmental transition) and pupariation. Ref.1

Catalytic activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

Cofactor

FAD.

Pathway

Steroid metabolism; cholesterol metabolism.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Expressed predominantly in prothoracic gland of the larval ring gland and nurse cells of the adult ovary. Low expression is all adult tissues examined. Ref.1

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 466NADPH:adrenodoxin oxidoreductase, mitochondrialPRO_0000019424

Regions

Nucleotide binding176 – 1794NADP By similarity
Nucleotide binding220 – 2212NADP By similarity
Nucleotide binding386 – 3883FAD

Sites

Binding site401FAD; via amide nitrogen
Binding site611FAD
Binding site691FAD; via amide nitrogen
Binding site1051FAD; via amide nitrogen and carbonyl oxygen
Binding site2321NADP By similarity
Binding site3791FAD; via amide nitrogen
Binding site3861NADP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V3T9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 64D7C1FF0F1CAFD6

FASTA46651,353
        10         20         30         40         50         60 
MGINCLNIFR RGLHTSSARL QVIQSTTPTK RICIVGAGPA GFYAAQLILK QLDNCVVDVV 

        70         80         90        100        110        120 
EKLPVPFGLV RFGVAPDHPE VKNVINTFTK TAEHPRLRYF GNISLGTDVS LRELRDRYHA 

       130        140        150        160        170        180 
VLLTYGADQD RQLELENEQL DNVISARKFV AWYNGLPGAE NLAPDLSGRD VTIVGQGNVA 

       190        200        210        220        230        240 
VDVARMLLSP LDALKTTDTT EYALEALSCS QVERVHLVGR RGPLQAAFTI KELREMLKLP 

       250        260        270        280        290        300 
NVDTRWRTED FSGIDMQLDK LQRPRKRLTE LMLKSLKEQG RISGSKQFLP IFLRAPKAIA 

       310        320        330        340        350        360 
PGEMEFSVTE LQQEAAVPTS STERLPSHLI LRSIGYKSSC VDTGINFDTR RGRVHNINGR 

       370        380        390        400        410        420 
ILKDDATGEV DPGLYVAGWL GTGPTGVIVT TMNGAFAVAK TICDDINTNA LDTSSVKPGY 

       430        440        450        460 
DADGKRVVTW DGWQRINDFE SAAGKAKGKP REKIVSIEEM LRVAGV 

« Hide

References

« Hide 'large scale' references
[1]"The dare gene: steroid hormone production, olfactory behavior, and neural degeneration in Drosophila."
Freeman M.R., Dobritsa A., Gaines P., Segraves W.A., Carlson J.R.
Development 126:4591-4602(1999) [PubMed: 10498693] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: W1118.
Tissue: Head and Testis.
[2]"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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF168685 mRNA. Translation: AAD50819.1.
AE013599 Genomic DNA. Translation: AAF58678.1.
RefSeqNP_477150.1. NM_057802.5.

3D structure databases

ProteinModelPortalQ9V3T9.
SMRQ9V3T9. Positions 29-465.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9V3T9.

Proteomic databases

PRIDEQ9V3T9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088176; FBpp0087272; FBgn0015582.
GeneID36203.
KEGGdme:Dmel_CG12390.
NMPDRfig|7227.3.peg.4615.

Organism-specific databases

CTD36203.
FlyBaseFBgn0015582. dare.

Phylogenomic databases

GeneTreeEMGT00050000010541.
InParanoidQ9V3T9.
OMAYHAVLLT.
OrthoDBEOG4JWSVK.
PhylomeDBQ9V3T9.

Gene expression databases

BgeeQ9V3T9.
GermOnlineCG12390. Drosophila melanogaster.

Family and domain databases

InterProIPR021163. Adrenodoxin_Rdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00528.
PIRSFPIRSF000362. FNR. 1 hit.
ProtoNetSearch...

Other

NextBio797327.

Entry information

Entry nameADRO_DROME
AccessionPrimary (citable) accession number: Q9V3T9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families