CP4E2_DROME
ID CP4E2_DROME Reviewed; 526 AA.
AC Q27606; Q24130; Q24291; Q9V4T4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cytochrome P450 4e2;
DE EC=1.14.-.-;
DE AltName: Full=CYPIVE2;
GN Name=Cyp4e2; ORFNames=CG2060;
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] OF 42-526.
RC TISSUE=Embryo;
RX PubMed=8972915; DOI=10.1016/s0378-1119(96)00378-2;
RA Pittendrigh B.R., Mocelin G., Andreev O., ffrench-Constant R.H.;
RT "The sequence of a Drosophila Cyp4e2 cytochrome P450-encoding cDNA.";
RL Gene 179:295-296(1996).
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=Embryo;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 42-444.
RC STRAIN=Raleigh DDTR;
RA Amichot M., Brun A., Cuany A., Lemouel T., Berge J.-B.;
RT "Cloning and expression study of CYP4E2 a novel P450 gene in Drosophila.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 312-435.
RC STRAIN=Haag-79;
RX PubMed=8676871; DOI=10.1007/bf02172519;
RA Dunkov B.C., Rodriguez-Arnaiz R., Pittendrigh B., ffrench-Constant R.H.,
RA Feyereisen R.;
RT "Cytochrome P450 gene clusters in Drosophila melanogaster.";
RL Mol. Gen. Genet. 251:290-297(1996).
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; U56957; AAC47424.1; -; mRNA.
DR EMBL; AE013599; AAF59091.1; -; Genomic_DNA.
DR EMBL; AY058518; AAL13747.1; -; mRNA.
DR EMBL; X86076; CAA60032.1; -; mRNA.
DR EMBL; U34332; AAA80666.1; -; mRNA.
DR PIR; JC5236; JC5236.
DR PIR; S57646; S57646.
DR PIR; S70622; S70622.
DR RefSeq; NP_001286196.1; NM_001299267.1.
DR RefSeq; NP_477117.2; NM_057769.4.
DR AlphaFoldDB; Q27606; -.
DR SMR; Q27606; -.
DR BioGRID; 61675; 5.
DR DIP; DIP-23009N; -.
DR IntAct; Q27606; 2.
DR STRING; 7227.FBpp0087824; -.
DR PaxDb; Q27606; -.
DR PRIDE; Q27606; -.
DR DNASU; 35822; -.
DR EnsemblMetazoa; FBtr0088745; FBpp0087824; FBgn0014469.
DR EnsemblMetazoa; FBtr0339278; FBpp0308387; FBgn0014469.
DR GeneID; 35822; -.
DR KEGG; dme:Dmel_CG2060; -.
DR CTD; 35822; -.
DR FlyBase; FBgn0014469; Cyp4e2.
DR VEuPathDB; VectorBase:FBgn0014469; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000165700; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q27606; -.
DR OMA; WWHQYGK; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q27606; -.
DR Reactome; R-DME-193144; Estrogen biosynthesis.
DR Reactome; R-DME-211976; Endogenous sterols.
DR BioGRID-ORCS; 35822; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35822; -.
DR PRO; PR:Q27606; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0014469; Expressed in adult Malpighian tubule (Drosophila) and 31 other tissues.
DR ExpressionAtlas; Q27606; baseline and differential.
DR Genevisible; Q27606; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..526
FT /note="Cytochrome P450 4e2"
FT /id="PRO_0000051841"
FT BINDING 307
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 444
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 256
FT /note="E -> K (in Ref. 5; CAA60032)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="S -> D (in Ref. 5; CAA60032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 60693 MW; A13DD43C4F4F4D52 CRC64;
MWFVLYIFLA LPLLLVAYLE LSTFRRRRVL NKFNGPRGLP LMGNAHQMGK NPSEILDTVF
SWWHQYGKDN FVFWIGTYSN VLVTSSKYLE FILSSQTLIT KSDIYQLTHP WLGLGLLTST
GSKWHKHRKM ITPAFHFNIL QDFHEVMNEN STKFIKHLKT VAAGDNIFDF QEQAHYLTLD
VICDTAMGVS INAMENRSSS IVQAFKDMCY NINMRAFHPL KRNELLYRLA PDYPAYSRTL
KTLQDFTNEI IAKRIEAHKS GAVSTNAGDE FTRKKMAFLD TLLSSTIDGR PLNSKELYEE
VSTFMFEGHD TTTSGVSFAV YLLSRHQDEQ RKLFKEQREV MGNSELGRDA TFQEISQMKY
LDLFIKEAQR VYPSVPFIGR FTEKDYVIDG DLVPKGTTLN LGLVMLGYNE KVFKDPHKFR
PERFELEKPG PFEYVPFSAG PRNCIGQKFA LLEIKTVVSK IIRNFEVLPA LDELVSKDGY
ISTTIGLPDA ERKKRDPYRH KYDPILSAVL TLKSENGLYI RLKERH
