CP132_DROME
ID CP132_DROME Reviewed; 493 AA.
AC Q9VGB4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable cytochrome P450 313a2;
DE EC=1.14.-.-;
DE AltName: Full=CYPCCCXIIIA2;
GN Name=Cyp313a2; ORFNames=CG10094;
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; AAF54769.4; -; Genomic_DNA.
DR RefSeq; NP_650169.3; NM_141912.3.
DR AlphaFoldDB; Q9VGB4; -.
DR SMR; Q9VGB4; -.
DR IntAct; Q9VGB4; 4.
DR STRING; 7227.FBpp0300785; -.
DR PaxDb; Q9VGB4; -.
DR EnsemblMetazoa; FBtr0308561; FBpp0300785; FBgn0038006.
DR GeneID; 41487; -.
DR KEGG; dme:Dmel_CG10094; -.
DR UCSC; CG10094-RA; d. melanogaster.
DR CTD; 41487; -.
DR FlyBase; FBgn0038006; Cyp313a2.
DR VEuPathDB; VectorBase:FBgn0038006; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000167150; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q9VGB4; -.
DR OMA; FPEHQEM; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q9VGB4; -.
DR SignaLink; Q9VGB4; -.
DR BioGRID-ORCS; 41487; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41487; -.
DR PRO; PR:Q9VGB4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; Q9VGB4; differential.
DR Genevisible; Q9VGB4; 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..493
FT /note="Probable cytochrome P450 313a2"
FT /id="PRO_0000052324"
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 493 AA; 56651 MW; 808769F4D0627262 CRC64;
MIVIQLLIAA SLILWIRFLW SRRKLYMLMM QLPGRMGLPL LGNSVRYLII SRGRMSSRTT
YMDKHGSTYM AWIGTTPIVI TRDPKIAEKV LTSPFCINRS SQTTNALALS MGYGLLTLQG
SKWMARRKHM NPAFKHSVLL SFLPIFNAET DLLVSVFDSF VGQGEKDVLS DLIRWSFAIA
TQTTLGTDVT KDDNFENDAI LKTYQSMLRL TIINIFVPFV QNKIVSKLFG LEWLRRRDAS
AINKMINNIL DKKLNSNPEN YCESELKTVI HRAIELFRND EMSLMELGAE CSSMVLAAFE
TSAHTVYYAL VLLAMFPEHQ EMVFNEIKEH FPLAKGIEVT HTDLQQLVYL DRVLNETLRL
MPSVPFSSRE TLEDLRLSNG VVIPKGMTIS IDIFNTQRNT DYWGSEAAQF NPENFLPEKI
HDRHPYAFIP FSKGKRNCIG WRYGLMSSKL ALVKILRNYK LKTSFPYENL EFVDHMVIKL
AQSPQLAFER RTL
