ADXH2_DROME
ID ADXH2_DROME Reviewed; 152 AA.
AC Q8SZA8; Q9VZE1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Adrenodoxin-like protein 2, mitochondrial {ECO:0000305};
DE AltName: Full=Ferredoxin-2 {ECO:0000312|FlyBase:FBgn0035529};
DE Flags: Precursor;
GN Name=Fdx2 {ECO:0000312|FlyBase:FBgn0035529};
GN Synonyms=Fdxh2 {ECO:0000312|FlyBase:FBgn0035529};
GN ORFNames=CG1319 {ECO:0000312|FlyBase:FBgn0035529};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:AAL48623.1, ECO:0000312|EMBL:AAM51020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48623.1, ECO:0000312|EMBL:AAM51020.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48623.1}, and
RC Head {ECO:0000312|EMBL:AAM51020.1};
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 [4] {ECO:0000312|EMBL:ANY27736.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Wan K., Booth B., Spirohn K., Hao T., Hu Y., Calderwood M., Hill D.,
RA Mohr S., Vidal M., Celniker S., Perrimon N.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25628335; DOI=10.1093/hmg/ddv024;
RA Palandri A., L'hote D., Cohen-Tannoudji J., Tricoire H., Monnier V.;
RT "Frataxin inactivation leads to steroid deficiency in flies and human
RT ovarian cells.";
RL Hum. Mol. Genet. 24:2615-2626(2015).
CC -!- FUNCTION: Required for ecdysteroidogenesis in the prothoracic gland
CC which is necessary for larval to pupal transition.
CC {ECO:0000269|PubMed:25628335}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in larval growth
CC defects, strong larval lethality and strong reduction of ecdysteroid
CC peak level required to proceed to pupal stage (PubMed:25628335). RNAi-
CC mediated knockdown in the prothoracic gland results in larval growth
CC defects and lethality at the third larval stage, with a complete lack
CC of pupariation (PubMed:25628335). {ECO:0000269|PubMed:25628335}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF47883.2; -; Genomic_DNA.
DR EMBL; AY071001; AAL48623.1; -; mRNA.
DR EMBL; AY119160; AAM51020.1; -; mRNA.
DR EMBL; KX531926; ANY27736.1; -; mRNA.
DR RefSeq; NP_647889.2; NM_139632.3.
DR AlphaFoldDB; Q8SZA8; -.
DR SMR; Q8SZA8; -.
DR IntAct; Q8SZA8; 3.
DR STRING; 7227.FBpp0289999; -.
DR PaxDb; Q8SZA8; -.
DR PRIDE; Q8SZA8; -.
DR DNASU; 38530; -.
DR EnsemblMetazoa; FBtr0300775; FBpp0289999; FBgn0035529.
DR GeneID; 38530; -.
DR KEGG; dme:Dmel_CG1319; -.
DR UCSC; CG1319-RA; d. melanogaster.
DR CTD; 112812; -.
DR FlyBase; FBgn0035529; Fdx2.
DR VEuPathDB; VectorBase:FBgn0035529; -.
DR eggNOG; KOG3309; Eukaryota.
DR GeneTree; ENSGT00940000166318; -.
DR HOGENOM; CLU_082632_2_2_1; -.
DR InParanoid; Q8SZA8; -.
DR OMA; VINTCRN; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; Q8SZA8; -.
DR Reactome; R-DME-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Reactome; R-DME-2395516; Electron transport from NADPH to Ferredoxin.
DR BioGRID-ORCS; 38530; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Fdx2; fly.
DR GenomeRNAi; 38530; -.
DR PRO; PR:Q8SZA8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035529; Expressed in adult Malpighian tubule (Drosophila) and 43 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0045998; P:positive regulation of ecdysteroid biosynthetic process; IMP:FlyBase.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Lipid metabolism;
KW Metal-binding; Mitochondrion; Reference proteome; Steroid metabolism;
KW Steroidogenesis; Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..152
FT /note="Adrenodoxin-like protein 2, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000447491"
FT DOMAIN 41..146
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 127
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 152 AA; 16407 MW; 55E034F065BE412F CRC64;
MLVINSCRAA SRLALRSLNL RSPIATRTFS TGLALKTKDV VNITFVRANG DKIKTSGKVG
DSLLDVVVNN NVDLDGFGAC EGTLTCSTCH LIFKTSDFEK LPDKPGDEEL DMLDLAYELT
DTSRLGCQIT LSKDMEGLEV HVPSTINDAR AA
