CP133_DROME
ID CP133_DROME Reviewed; 492 AA.
AC Q9VGB3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable cytochrome P450 313a3;
DE EC=1.14.-.-;
DE AltName: Full=CYPCCCXIIIA3;
GN Name=Cyp313a3; ORFNames=CG10093;
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 [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 [2]
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: May be involved in the metabolism of insect hormones and in
CC the breakdown of synthetic insecticides. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF54770.3; -; Genomic_DNA.
DR RefSeq; NP_650170.2; NM_141913.3.
DR AlphaFoldDB; Q9VGB3; -.
DR SMR; Q9VGB3; -.
DR IntAct; Q9VGB3; 1.
DR STRING; 7227.FBpp0082086; -.
DR PaxDb; Q9VGB3; -.
DR DNASU; 41488; -.
DR EnsemblMetazoa; FBtr0082617; FBpp0082086; FBgn0038007.
DR GeneID; 41488; -.
DR KEGG; dme:Dmel_CG10093; -.
DR UCSC; CG10093-RA; d. melanogaster.
DR CTD; 41488; -.
DR FlyBase; FBgn0038007; Cyp313a3.
DR VEuPathDB; VectorBase:FBgn0038007; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000167150; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q9VGB3; -.
DR OMA; GWKYGLM; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q9VGB3; -.
DR BioGRID-ORCS; 41488; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41488; -.
DR PRO; PR:Q9VGB3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038007; Expressed in spermathecum and 1 other tissue.
DR ExpressionAtlas; Q9VGB3; baseline and differential.
DR Genevisible; Q9VGB3; DM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..492
FT /note="Probable cytochrome P450 313a3"
FT /id="PRO_0000052325"
FT BINDING 438
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"
SQ SEQUENCE 492 AA; 56195 MW; 2836D13953C3B4DC CRC64;
MDTFQLLLAV GVCFWIYFLW SRRRLYMMHF KIPGPMGLPI LGIAFEYLIT YKRKMSIRTK
YMDIYGSTCL VWVGPTPFVI TRDPKIAEEI FLSPECLNRS SIFSKPVNSC TGDGLLSLEA
SKWVDRRKNL NPAFKQNVLL SFLPIFNSEA KTLVAFLDSL VGQGEKKVRD DIVRWSFRIA
TQTTVGTDVK KDASFKNDSV LKSYETFMKI IVMNVLLPFT HNKIFSTLGG FETQKALAKS
NVNKMIGTIV DKKLMTKPES GSQPEITSVI NKAIELHRNG EMSREEVQSE CCSFVVAAFE
TTGDTVYHAL ILLAMFPEHQ DTVYQELKEL FPVAGDFEVT YDDLQRMVFL ERVVNETLRL
IPSVPFTPRE TIRDFRLSSG VVIPKGVGIG IDIFATHRNR DHWGTDPSSF NPDHFLPDNV
RDRHPYAYIP FSKGRRNCIG WKYGLMSSKL ALSKILRNCK VSTSFRYEDL EFVDNIGMEL
AQSPGLEFHR RT