CP302_DROME
ID CP302_DROME Reviewed; 489 AA.
AC Q9NGX9; Q059D3; Q9VZJ0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cytochrome P450 302a1, mitochondrial;
DE EC=1.14.99.-;
DE AltName: Full=Protein disembodied;
DE Flags: Precursor;
GN Name=dib; Synonyms=CYP302A1; ORFNames=CG12028;
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, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=10976044; DOI=10.1242/dev.127.19.4115;
RA Chavez V.M., Marques G., Delbecque J.P., Kobayashi K., Hollingsworth M.,
RA Burr J., Natzle J.E., O'Connor M.B.;
RT "The Drosophila disembodied gene controls late embryonic morphogenesis and
RT codes for a cytochrome P450 enzyme that regulates embryonic ecdysone
RT levels.";
RL Development 127:4115-4126(2000).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=12177427; DOI=10.1073/pnas.162375799;
RA Warren J.T., Petryk A., Marques G., Jarcho M.P., Parvy J.-P.,
RA Dauphin-Villemant C., O'Connor M.B., Gilbert L.I.;
RT "Molecular and biochemical characterization of two P450 enzymes in the
RT ecdysteroidogenic pathway of Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11043-11048(2002).
RN [6]
RP FUNCTION.
RX PubMed=12676319; DOI=10.1016/s0925-4773(03)00009-1;
RA Giesen K., Lammel U., Langehans D., Krukkert K., Bunse I., Klambt C.;
RT "Regulation of glial cell number and differentiation by ecdysone and Fos
RT signaling.";
RL Mech. Dev. 120:401-413(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=14610274; DOI=10.1073/pnas.2336088100;
RA Petryk A., Warren J.T., Marques G., Jarcho M.P., Gilbert L.I., Kahler J.,
RA Parvy J.-P., Li Y., Dauphin-Villemant C., O'Connor M.B.;
RT "Shade is the Drosophila P450 enzyme that mediates the hydroxylation of
RT ecdysone to the steroid insect molting hormone 20-hydroxyecdysone.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13773-13778(2003).
CC -!- FUNCTION: Required for CNS development; negatively regulates glial cell
CC division in the embryonic midline. Involved in the metabolism of insect
CC hormones; responsible for ecdysteroid C22-hydroxylase activity. May be
CC involved in the breakdown of synthetic insecticides.
CC {ECO:0000269|PubMed:10976044, ECO:0000269|PubMed:12177427,
CC ECO:0000269|PubMed:12676319}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid biosynthesis; ecdysteroid biosynthesis.
CC {ECO:0000269|PubMed:14610274}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14610274}.
CC -!- TISSUE SPECIFICITY: Complex coexpression pattern of dib (disembodied)
CC and sad (shade) in the early embryo that restricts to the prothoracic
CC gland cells of the developing ring gland during late embryogenesis. In
CC larvae and adult, coexpression is seen in prothoracic gland and
CC follicle cells of the ovary. In adults, coexpression is seen in the
CC follicle cells. {ECO:0000269|PubMed:10976044,
CC ECO:0000269|PubMed:12177427}.
CC -!- DEVELOPMENTAL STAGE: Expression starts during embryonic blastoderm
CC stages and is absent by stages 12/13. Reappears in stage 16.
CC {ECO:0000269|PubMed:10976044}.
CC -!- MISCELLANEOUS: Member of the Halloween gene group.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF237560; AAF60174.1; -; mRNA.
DR EMBL; AE014296; AAF47831.2; -; Genomic_DNA.
DR EMBL; BT029035; ABJ16968.1; -; mRNA.
DR RefSeq; NP_524810.2; NM_080071.3.
DR AlphaFoldDB; Q9NGX9; -.
DR SMR; Q9NGX9; -.
DR STRING; 7227.FBpp0073061; -.
DR PaxDb; Q9NGX9; -.
DR PRIDE; Q9NGX9; -.
DR DNASU; 45282; -.
DR EnsemblMetazoa; FBtr0073205; FBpp0073061; FBgn0000449.
DR GeneID; 45282; -.
DR KEGG; dme:Dmel_CG12028; -.
DR CTD; 45282; -.
DR FlyBase; FBgn0000449; dib.
DR VEuPathDB; VectorBase:FBgn0000449; -.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_28_0_1; -.
DR InParanoid; Q9NGX9; -.
DR OMA; GNLYNYM; -.
DR OrthoDB; 1273535at2759; -.
DR PhylomeDB; Q9NGX9; -.
DR BioCyc; MetaCyc:MON-18110; -.
DR UniPathway; UPA00765; -.
DR BioGRID-ORCS; 45282; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 45282; -.
DR PRO; PR:Q9NGX9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000449; Expressed in ring gland and 6 other tissues.
DR Genevisible; Q9NGX9; DM.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0042767; F:ecdysteroid 22-hydroxylase activity; IDA:FlyBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0006697; P:ecdysone biosynthetic process; IDA:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; IMP:FlyBase.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..489
FT /note="Cytochrome P450 302a1, mitochondrial"
FT /id="PRO_0000003629"
FT BINDING 434
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 186
FT /note="C -> S (in Ref. 1; AAF60174)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="R -> S (in Ref. 1; AAF60174)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> G (in Ref. 1; AAF60174)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="L -> M (in Ref. 1; AAF60174)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="R -> K (in Ref. 1; AAF60174)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="A -> R (in Ref. 1; AAF60174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55574 MW; AE1E5A97E79E502B CRC64;
MLTKLLKISC TSRQCTFAKP YQAIPGPRGP FGMGNLYNYL PGIGSYSWLR LHQAGQDKYE
KYGAIVRETI VPGQDIVWLY DPKDIALLLN ERDCPQRRSH LALAQYRKSR PDVYKTTGLL
PTNGPEWWRI RAQVQKELSA PKSVRNFVRQ VDGVTKEFIR FLQESRNGGA IDMLPKLTRL
NLELTCLLTF GARLQSFTAQ EQDPRSRSTR LMDAAETTNS CILPTDQGLQ LWRFLETPSF
RKLSQAQSYM ESVALELVEE NVRNGSVGSS LISAYVKNPE LDRSDVVGTA ADLLLAGIDT
TSYASAFLLY HIARNPEVQQ KLHEEARRVL PSAKDELSMD ALRTDITYTR AVLKESLRLN
PIAVGVGRIL NQDAIFSGYF VPKGTTVVTQ NMVACRLEQH FQDPLRFQPD RWLQHRSALN
PYLVLPFGHG MRACIARRLA EQNMHILLLR LLREYELIWS GSDDEMGVKT LLINKPDAPV
LIDLRLRRE
