CP315_DROME
ID CP315_DROME Reviewed; 520 AA.
AC Q9VGH1; Q5U131; Q8MTR7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytochrome P450 315a1, mitochondrial;
DE EC=1.14.99.-;
DE AltName: Full=CYPCCCXVA1;
DE AltName: Full=Protein shadow;
DE Flags: Precursor;
GN Name=sad; Synonyms=Cyp315a1; ORFNames=CG14728;
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, FUNCTION, ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
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 [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; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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: midline glial cells. Involved
CC in the metabolism of insect hormones: responsible for ecdysteroid C2-
CC hydroxylase activity. May be involved in the breakdown of synthetic
CC insecticides. {ECO:0000269|PubMed:12177427}.
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, sad only is expressed in nurse cells.
CC {ECO:0000269|PubMed:12177427}.
CC -!- MISCELLANEOUS: Member of the Halloween gene group.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY079170; AAL86019.1; -; mRNA.
DR EMBL; AE014297; AAF54711.1; -; Genomic_DNA.
DR EMBL; BT016061; AAV36946.1; -; mRNA.
DR RefSeq; NP_650123.1; NM_141866.2.
DR AlphaFoldDB; Q9VGH1; -.
DR SMR; Q9VGH1; -.
DR BioGRID; 69335; 1.
DR STRING; 7227.FBpp0081949; -.
DR PaxDb; Q9VGH1; -.
DR DNASU; 44858; -.
DR EnsemblMetazoa; FBtr0082475; FBpp0081949; FBgn0003312.
DR GeneID; 44858; -.
DR KEGG; dme:Dmel_CG14728; -.
DR CTD; 44858; -.
DR FlyBase; FBgn0003312; sad.
DR VEuPathDB; VectorBase:FBgn0003312; -.
DR eggNOG; KOG0159; Eukaryota.
DR GeneTree; ENSGT00950000182905; -.
DR HOGENOM; CLU_001570_28_2_1; -.
DR InParanoid; Q9VGH1; -.
DR OMA; VLPERWC; -.
DR OrthoDB; 481145at2759; -.
DR PhylomeDB; Q9VGH1; -.
DR BioCyc; MetaCyc:MON-18113; -.
DR Reactome; R-DME-193144; Estrogen biosynthesis.
DR Reactome; R-DME-211976; Endogenous sterols.
DR UniPathway; UPA00765; -.
DR BioGRID-ORCS; 44858; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 44858; -.
DR PRO; PR:Q9VGH1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003312; Expressed in prothoracic gland (Drosophila) and 9 other tissues.
DR Genevisible; Q9VGH1; DM.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0042768; F:ecdysteroid 2-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: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 GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
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 /evidence="ECO:0000255"
FT CHAIN ?..520
FT /note="Cytochrome P450 315a1, mitochondrial"
FT /id="PRO_0000003631"
FT BINDING 466
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 484
FT /note="A -> T (in Ref. 1; AAL86019)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="R -> Q (in Ref. 1; AAL86019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 59631 MW; 6DC4A2CCD8E07BC6 CRC64;
MTEKRERPGP LRWLRHLLDQ LLVRILSLSL FRSRCDPPPL QRFPATELPP AVAAKYVPIP
RVKGLPVVGT LVDLIAAGGA THLHKYIDAR HKQYGPIFRE RLGGTQDAVF VSSANLMRGV
FQHEGQYPQH PLPDAWTLYN QQHACQRGLF FMEGAEWLHN RRILNRLLLN GNLNWMDVHI
ESCTRRMVDQ WKRRTAEAAA IPLAESGEIR SYELPLLEQQ LYRWSIEVLC CIMFGTSVLT
CPKIQSSLDY FTQIVHKVFE HSSRLMTFPP RLAQILRLPI WRDFEANVDE VLREGAAIID
HCIRVQEDQR RPHDEALYHR LQAADVPGDM IKRIFVDLVI AAGDTTAFSS QWALFALSKE
PRLQQRLAKE RATNDSRLMH GLIKESLRLY PVAPFIGRYL PQDAQLGGHF IEKDTMVLLS
LYTAGRDPSH FEQPERVLPE RWCIGETEQV HKSHGSLPFA IGQRSCIGRR VALKQLHSLL
GRCAAQFEMS CLNEMPVDSV LRMVTVPDRT LRLALRPRTE
