ADRO_DROME
ID ADRO_DROME Reviewed; 466 AA.
AC Q9V3T9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial;
DE Short=AR;
DE Short=Adrenodoxin reductase;
DE EC=1.18.1.6;
DE AltName: Full=Ferredoxin--NADP(+) reductase;
DE Short=Ferredoxin reductase;
DE Flags: Precursor;
GN Name=dare; ORFNames=CG12390;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=W1118; TISSUE=Head, and Testis;
RX PubMed=10498693; DOI=10.1242/dev.126.20.4591;
RA Freeman M.R., Dobritsa A., Gaines P., Segraves W.A., Carlson J.R.;
RT "The dare gene: steroid hormone production, olfactory behavior, and neural
RT degeneration in Drosophila.";
RL Development 126:4591-4602(1999).
RN [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 [3]
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).
CC -!- FUNCTION: Required for synthesis of steroid hormones, for olfactory
CC sensory behavior and completion of the second larval molt (a steroid
CC mediated developmental transition) and pupariation.
CC {ECO:0000269|PubMed:10498693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized
CC [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in prothoracic gland of the
CC larval ring gland and nurse cells of the adult ovary. Low expression is
CC all adult tissues examined. {ECO:0000269|PubMed:10498693}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF168685; AAD50819.1; -; mRNA.
DR EMBL; AE013599; AAF58678.1; -; Genomic_DNA.
DR RefSeq; NP_477150.1; NM_057802.6.
DR AlphaFoldDB; Q9V3T9; -.
DR SMR; Q9V3T9; -.
DR STRING; 7227.FBpp0087272; -.
DR PaxDb; Q9V3T9; -.
DR PRIDE; Q9V3T9; -.
DR DNASU; 36203; -.
DR EnsemblMetazoa; FBtr0088176; FBpp0087272; FBgn0015582.
DR GeneID; 36203; -.
DR KEGG; dme:Dmel_CG12390; -.
DR CTD; 36203; -.
DR FlyBase; FBgn0015582; dare.
DR VEuPathDB; VectorBase:FBgn0015582; -.
DR eggNOG; KOG1800; Eukaryota.
DR GeneTree; ENSGT00390000013574; -.
DR HOGENOM; CLU_024722_3_1_1; -.
DR InParanoid; Q9V3T9; -.
DR OMA; RFNFIGN; -.
DR OrthoDB; 1324510at2759; -.
DR PhylomeDB; Q9V3T9; -.
DR Reactome; R-DME-2395516; Electron transport from NADPH to Ferredoxin.
DR UniPathway; UPA00296; -.
DR BioGRID-ORCS; 36203; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 36203; -.
DR PRO; PR:Q9V3T9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0015582; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9V3T9; baseline and differential.
DR Genevisible; Q9V3T9; DM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; ISS:FlyBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0007591; P:molting cycle, chitin-based cuticle; IMP:FlyBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
DR GO; GO:0035073; P:pupariation; IMP:FlyBase.
DR GO; GO:0006694; P:steroid biosynthetic process; IDA:FlyBase.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR PIRSF; PIRSF000362; FNR; 1.
PE 2: Evidence at transcript level;
KW Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NADP; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..466
FT /note="NADPH:adrenodoxin oxidoreductase, mitochondrial"
FT /id="PRO_0000019424"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 176..179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 220..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 379
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 386..388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 386
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
SQ SEQUENCE 466 AA; 51353 MW; 64D7C1FF0F1CAFD6 CRC64;
MGINCLNIFR RGLHTSSARL QVIQSTTPTK RICIVGAGPA GFYAAQLILK QLDNCVVDVV
EKLPVPFGLV RFGVAPDHPE VKNVINTFTK TAEHPRLRYF GNISLGTDVS LRELRDRYHA
VLLTYGADQD RQLELENEQL DNVISARKFV AWYNGLPGAE NLAPDLSGRD VTIVGQGNVA
VDVARMLLSP LDALKTTDTT EYALEALSCS QVERVHLVGR RGPLQAAFTI KELREMLKLP
NVDTRWRTED FSGIDMQLDK LQRPRKRLTE LMLKSLKEQG RISGSKQFLP IFLRAPKAIA
PGEMEFSVTE LQQEAAVPTS STERLPSHLI LRSIGYKSSC VDTGINFDTR RGRVHNINGR
ILKDDATGEV DPGLYVAGWL GTGPTGVIVT TMNGAFAVAK TICDDINTNA LDTSSVKPGY
DADGKRVVTW DGWQRINDFE SAAGKAKGKP REKIVSIEEM LRVAGV
