ID CP6A2_DROME Reviewed; 506 AA.
AC P33270; P91669; Q5U1C1; Q9V9A2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 24-JAN-2024, entry version 178.
DE RecName: Full=Cytochrome P450 6a2;
DE EC=1.14.-.-;
DE AltName: Full=CYPVIA2;
DE AltName: Full=Cytochrome P450-B1;
GN Name=Cyp6a2; Synonyms=CYT-P450-B1; ORFNames=CG9438;
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 [GENOMIC DNA].
RC STRAIN=91-C;
RX PubMed=1317576; DOI=10.1073/pnas.89.11.4855;
RA Waters L.C., Zelhof A.C., Shaw B.J., Ch'Ang L.-Y.;
RT "Possible involvement of the long terminal repeat of transposable element
RT 17.6 in regulating expression of an insecticide resistance-associated P450
RT gene in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4855-4859(1992).
RN [2]
RP ERRATUM OF PUBMED:1317576.
RX PubMed=1465460; DOI=10.1073/pnas.89.24.12209-c;
RA Waters L.C., Zelhof A.C., Shaw B.J., Ch'Ang L.-Y.;
RL Proc. Natl. Acad. Sci. U.S.A. 89:12209-12209(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Iso-1;
RA Dunkov B.C., Feyereisen R.;
RT "Drosophila melanogaster Cyp6a2 gene.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Canton-S;
RX PubMed=9407006; DOI=10.1089/dna.1997.16.1345;
RA Dunkov B.C., Guzov V.M., Mocelin G., Shotkoski F., Brun A., Amichot M.,
RA ffrench-Constant R.H., Feyereisen R.;
RT "The Drosophila cytochrome P450 gene Cyp6a2: structure, localization,
RT heterologous expression, and induction by phenobarbital.";
RL DNA Cell Biol. 16:1345-1356(1997).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-383.
RX PubMed=8625948;
RX DOI=10.1002/(sici)1098-2280(1996)27:1<46::aid-em7>3.0.co;2-c;
RA Saner C., Weibel B., Wurgler F.E., Sengstag C.;
RT "Metabolism of promutagens catalyzed by Drosophila melanogaster CYP6A2
RT enzyme in Saccharomyces cerevisiae.";
RL Environ. Mol. Mutagen. 27:46-58(1996).
CC -!- FUNCTION: Is involved in the breakdown of synthetic insecticides and
CC may be involved in the metabolism of insect hormones.
CC {ECO:0000269|PubMed:9407006}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M88009; AAA28438.1; -; Genomic_DNA.
DR EMBL; S51248; AAB24525.1; -; mRNA.
DR EMBL; U78088; AAB36782.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70832.1; -; Genomic_DNA.
DR EMBL; BT015971; AAV36856.1; -; mRNA.
DR EMBL; S81983; AAB36460.1; -; Genomic_DNA.
DR PIR; A45378; A47198.
DR RefSeq; NP_523628.1; NM_078904.2.
DR AlphaFoldDB; P33270; -.
DR SMR; P33270; -.
DR BioGRID; 61483; 1.
DR STRING; 7227.FBpp0085466; -.
DR PaxDb; 7227-FBpp0085466; -.
DR DNASU; 35587; -.
DR EnsemblMetazoa; FBtr0086133; FBpp0085466; FBgn0000473.
DR GeneID; 35587; -.
DR KEGG; dme:Dmel_CG9438; -.
DR AGR; FB:FBgn0000473; -.
DR CTD; 35587; -.
DR FlyBase; FBgn0000473; Cyp6a2.
DR VEuPathDB; VectorBase:FBgn0000473; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00940000165972; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; P33270; -.
DR OMA; PLKYTPM; -.
DR OrthoDB; 1611592at2759; -.
DR PhylomeDB; P33270; -.
DR BioGRID-ORCS; 35587; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35587; -.
DR PRO; PR:P33270; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000473; Expressed in capitellum (Drosophila) and 22 other cell types or tissues.
DR ExpressionAtlas; P33270; baseline and differential.
DR Genevisible; P33270; 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 GO; GO:0031000; P:response to caffeine; IDA:FlyBase.
DR GO; GO:0046680; P:response to DDT; IMP:FlyBase.
DR CDD; cd11056; CYP6-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24292:SF100; CYP6A16, ISOFORM B-RELATED; 1.
DR PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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..506
FT /note="Cytochrome P450 6a2"
FT /id="PRO_0000051866"
FT BINDING 451
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 31
FT /note="V -> L (in Ref. 1; AAA28438/AAB24525)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> R (in Ref. 1; AAA28438/AAB24525, 3; AAB36782
FT and 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 283..284
FT /note="RV -> SSF (in Ref. 1; AAA28438/AAB24525 and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 58685 MW; D6FFDE4AA81CD660 CRC64;
MFVLIYLLIA ISSLLAYLYH RNFNYWNRRG VPHDAPHPLY GNMVGFRKNR VMHDFFYDYY
NKYRKSGFPF VGFYFLHKPA AFIVDTQLAK NILIKDFSNF ADRGQFHNGR DDPLTQHLFN
LDGKKWKDMR QRLTPTFTSG KMKFMFPTVI KVSEEFVKVI TEQVPAAQNG AVLEIKELMA
RFTTDVIGTC AFGIECNTLR TPVSDFRTMG QKVFTDMRHG KLLTMFVFSF PKLASRLRMR
MMPEDVHQFF MRLVNDTIAL RERENFKRND FMNLLIELKQ KGRVTLDNGE VIEGMDIGEL
AAQVFVFYVA GFETSSSTMS YCLYELAQNQ DIQDRLRNEI QTVLEEQEGQ LTYESIKAMT
YLNQVISETL RLYTLVPHLE RKALNDYVVP GHEKLVIEKG TQVIIPACAY HRDEDLYPNP
ETFDPERFSP EKVAARESVE WLPFGDGPRN CIGMRFGQMQ ARIGLAQIIS RFRVSVCDTT
EIPLKYSPMS IVLGTVGGIY LRVERI
//
