CP314_DROME
ID CP314_DROME Reviewed; 540 AA.
AC Q9VUF8; Q8T483;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ecdysone 20-monooxygenase;
DE Short=E20MO;
DE EC=1.14.99.22;
DE AltName: Full=CYPCCCXIVA1;
DE AltName: Full=Cytochrome P450 314a1, mitochondrial;
DE AltName: Full=Protein shade;
DE Flags: Precursor;
GN Name=shd; Synonyms=CYP314A1; ORFNames=CG13478;
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] (ISOFORM B), FUNCTION, ENZYME ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-225.
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).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Testis;
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 [5]
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).
CC -!- FUNCTION: Required for CNS development; midline glial cells. Involved
CC in the metabolism of insect hormones; responsible for all ecdysone 20-
CC monooxygenase activity during embryonic, larval and adult stages. May
CC be involved in the breakdown of synthetic insecticides.
CC {ECO:0000269|PubMed:12676319, ECO:0000269|PubMed:14610274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ecdysone + O2 = 20-hydroxyecdysone + A + H2O;
CC Xref=Rhea:RHEA:14021, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16587, ChEBI:CHEBI:16688,
CC ChEBI:CHEBI:17499; EC=1.14.99.22;
CC Evidence={ECO:0000269|PubMed:14610274};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- PATHWAY: Steroid biosynthesis; ecdysteroid biosynthesis.
CC {ECO:0000269|PubMed:14610274}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14610274}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9VUF8-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q9VUF8-2; Sequence=VSP_009267;
CC -!- TISSUE SPECIFICITY: Strong expression by embryonic stage 10 in
CC epidermis, decreases significantly in older embryos. Third instar
CC larvae show expression in the midgut copper cells, Malpighian tubules
CC and fat body. In the adult ovaries, expression is seen in both nurse
CC cells and centripetally migrating follicle cells.
CC {ECO:0000269|PubMed:14610274}.
CC -!- MISCELLANEOUS: Member of the Halloween gene group.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF484414; AAQ05972.1; -; mRNA.
DR EMBL; AE014296; AAS65010.1; -; Genomic_DNA.
DR EMBL; AY089309; AAL90047.1; -; mRNA.
DR RefSeq; NP_001261843.1; NM_001274914.1. [Q9VUF8-1]
DR RefSeq; NP_648709.2; NM_140452.2. [Q9VUF8-2]
DR RefSeq; NP_996074.1; NM_206352.2. [Q9VUF8-1]
DR AlphaFoldDB; Q9VUF8; -.
DR SMR; Q9VUF8; -.
DR BioGRID; 64922; 2.
DR IntAct; Q9VUF8; 1.
DR STRING; 7227.FBpp0089324; -.
DR PaxDb; Q9VUF8; -.
DR DNASU; 39592; -.
DR EnsemblMetazoa; FBtr0075676; FBpp0089324; FBgn0003388. [Q9VUF8-1]
DR EnsemblMetazoa; FBtr0304700; FBpp0293243; FBgn0003388. [Q9VUF8-2]
DR EnsemblMetazoa; FBtr0333031; FBpp0305245; FBgn0003388. [Q9VUF8-1]
DR GeneID; 39592; -.
DR KEGG; dme:Dmel_CG13478; -.
DR UCSC; CG13478-RA; d. melanogaster. [Q9VUF8-1]
DR CTD; 56961; -.
DR FlyBase; FBgn0003388; shd.
DR VEuPathDB; VectorBase:FBgn0003388; -.
DR eggNOG; KOG0159; Eukaryota.
DR InParanoid; Q9VUF8; -.
DR OMA; CALHRHK; -.
DR PhylomeDB; Q9VUF8; -.
DR BioCyc; MetaCyc:MON-7726; -.
DR BRENDA; 1.14.99.22; 1994.
DR UniPathway; UPA00765; -.
DR BioGRID-ORCS; 39592; 0 hits in 1 CRISPR screen.
DR ChiTaRS; N; fly.
DR GenomeRNAi; 39592; -.
DR PRO; PR:Q9VUF8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003388; Expressed in arthropod fat body and 18 other tissues.
DR ExpressionAtlas; Q9VUF8; baseline and differential.
DR Genevisible; Q9VUF8; DM.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0004501; F:ecdysone 20-monooxygenase 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:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0045456; P:ecdysteroid biosynthetic process; IDA:FlyBase.
DR GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; IMP:FlyBase.
DR GO; GO:0035074; P:pupation; 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 1: Evidence at protein level;
KW Alternative splicing; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..540
FT /note="Ecdysone 20-monooxygenase"
FT /id="PRO_0000003630"
FT BINDING 488
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 VAR_SEQ 1..107
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009267"
FT MUTAGEN 225
FT /note="E->K: In allele shd-Z383; failure of head
FT involution. Defects in dorsal closure and aberrant gut
FT looping."
FT /evidence="ECO:0000269|PubMed:14610274"
FT CONFLICT 14
FT /note="G -> V (in Ref. 1; AAQ05972)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="I -> T (in Ref. 1; AAQ05972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 61690 MW; E6B007B6A6D99E58 CRC64;
MAVILLLALA LVLGCYCALH RHKLADIYLR PLLKNTLLED FYHAELIQPE APKRRRRGIW
DIPGPKRIPF LGTKWIFLLF FRRYKMTKLH EVYADLNRQY GDIVLEVMPS NVPIVHLYNR
DDLEKVLKYP SKYPFRPPTE IIVMYRQSRP DRYASVGIVN EQGPMWQRLR SSLTSSITSP
RVLQNFLPAL NAVCDDFIEL LRARRDPDTL VVPNFEELAN LMGLEAVCTL MLGRRMGFLA
IDTKQPQKIS QLAAAVKQLF ISQRDSYYGL GLWKYFPTKT YRDFARAEDL IYDVISEIID
HELEELKKSA ACEDDEAAGL RSIFLNILEL KDLDIRDKKS AIIDFIAAGI ETLANTLLFV
LSSVTGDPGA MPRILSEFCE YRDTNILQDA LTNATYTKAC IQESYRLRPT AFCLARILEE
DMELSGYSLN AGTVVLCQNM IACHKDSNFQ GAKQFTPERW IDPATENFTV NVDNASIVVP
FGVGRRSCPG KRFVEMEVVL LLAKMVLAFD VSFVKPLETE FEFLLAPKTP LSLRLSDRVF
