ID CP4D1_DROME Reviewed; 512 AA.
AC P33269; O18644; O18653; O18664; Q9W515; Q9W516;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Cytochrome P450 4d1;
DE EC=1.14.-.-;
DE AltName: Full=CYPIVD1;
GN Name=Cyp4d1; Synonyms=CYT-P450-D1; ORFNames=CG3656;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1605861; DOI=10.1089/dna.1992.11.397;
RA Gandhi R., Varak E., Goldberg M.L.;
RT "Molecular analysis of a cytochrome P450 gene of family 4 on the Drosophila
RT X chromosome.";
RL DNA Cell Biol. 11:397-404(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAM-1, CAM-12, CAM-14, CAM-19, CAM-2, CAM-3, CAM-38, CAM-41, CAM-42,
RC CAM-44, CAM-48, CAM-8, and CAM-9;
RA Phillips K.S., Begun D.J., Aquadro C.F.;
RT "Evidence for non-neutral evolution around the cytochrome p450 gene cluster
RT on the Drosophila melanogaster X chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
CC -!- FUNCTION: Involved in the metabolism of insect hormones and in the
CC breakdown of synthetic insecticides.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P33269-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P33269-2; Sequence=VSP_000614;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with the highest
CC levels occurring during late larval stages, then falling drastically
CC during pupariation. {ECO:0000269|PubMed:1605861}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X67645; CAA47887.1; -; mRNA.
DR EMBL; AF016992; AAB71155.1; -; Genomic_DNA.
DR EMBL; AF016993; AAB71156.1; -; Genomic_DNA.
DR EMBL; AF016994; AAB71157.1; -; Genomic_DNA.
DR EMBL; AF016995; AAB71158.1; -; Genomic_DNA.
DR EMBL; AF016996; AAB71159.1; -; Genomic_DNA.
DR EMBL; AF016997; AAB71160.1; -; Genomic_DNA.
DR EMBL; AF016998; AAB71161.1; -; Genomic_DNA.
DR EMBL; AF016999; AAB71162.1; -; Genomic_DNA.
DR EMBL; AF017000; AAB71163.1; -; Genomic_DNA.
DR EMBL; AF017001; AAB71164.1; -; Genomic_DNA.
DR EMBL; AF017002; AAB71165.1; -; Genomic_DNA.
DR EMBL; AF017003; AAB71166.1; -; Genomic_DNA.
DR EMBL; AF017004; AAB71167.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45736.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45737.1; -; Genomic_DNA.
DR EMBL; Z98269; CAB10972.1; -; Genomic_DNA.
DR PIR; S25707; S25707.
DR PIR; T13611; T13611.
DR RefSeq; NP_476907.2; NM_057559.4.
DR RefSeq; NP_726797.1; NM_166932.2.
DR AlphaFoldDB; P33269; -.
DR SMR; P33269; -.
DR IntAct; P33269; 1.
DR STRING; 7227.FBpp0070412; -.
DR PaxDb; 7227-FBpp0070412; -.
DR PeptideAtlas; P33269; -.
DR DNASU; 31188; -.
DR GeneID; 31188; -.
DR KEGG; dme:Dmel_CG3656; -.
DR AGR; FB:FBgn0005670; -.
DR CTD; 31188; -.
DR FlyBase; FBgn0005670; Cyp4d1.
DR VEuPathDB; VectorBase:FBgn0005670; -.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; P33269; -.
DR OrthoDB; 1611592at2759; -.
DR PhylomeDB; P33269; -.
DR Reactome; R-DME-193144; Estrogen biosynthesis.
DR Reactome; R-DME-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-DME-211916; Vitamins.
DR Reactome; R-DME-211976; Endogenous sterols.
DR Reactome; R-DME-2453902; The canonical retinoid cycle in rods (twilight vision).
DR BioGRID-ORCS; 31188; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Cyp4d1; fly.
DR GenomeRNAi; 31188; -.
DR PRO; PR:P33269; -.
DR Proteomes; UP000000803; Chromosome X.
DR ExpressionAtlas; P33269; baseline and differential.
DR Genevisible; P33269; 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 CDD; cd20628; CYP4; 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; PTHR24291:SF197; CYTOCHROME P450 4D1-RELATED; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 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 Alternative splicing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..512
FT /note="Cytochrome P450 4d1"
FT /id="PRO_0000051832"
FT BINDING 316
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 456
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..186
FT /note="MFLVIGAILASALFVGLLLYHLKFKRLIDLISYMPGPPVLPLVGHGHHFIGK
FT PPHEMVKKIFEFMETYSKDQVLKVWLGPELNVLMGNPKDVEVVLGTLRFNDKAGEYKAL
FT EPWLKEGLLVSRGRKWHKRRKIITPAFHFKILDQFVEVFEKGSRDLLRNMEQDRLKHGE
FT SGFSLYDWINLCTMDT -> MWLLLSLVLLLAIIALEMRRFLRNMRTIPGPLPLPLLGN
FT AHIFLGLTPAEACLKIGELAERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQ
FT EYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRI
FT SRGQERINLGEAIHLCALDA (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_000614"
FT VARIANT 170
FT /note="E -> D (in strain: CAM-2, CAM-3, CAM-8, CAM-12, CAM-
FT 41, CAM-44, CAM-48 and Berkeley)"
FT VARIANT 426
FT /note="S -> I (in strain: CAM-8, CAM-44, CAM-48 and
FT Berkeley)"
FT CONFLICT 68
FT /note="Y -> I (in Ref. 1; CAA47887)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="E -> K (in Ref. 1; CAA47887)"
FT /evidence="ECO:0000305"
FT CONFLICT 468..509
FT /note="AIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLMFKVRE -> PSWPMC
FT SGTTRLTLWATSFGTTRADRRTYSAYQGPLSSRCG (in Ref. 1; CAA47887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58691 MW; F7B089734231A6A3 CRC64;
MFLVIGAILA SALFVGLLLY HLKFKRLIDL ISYMPGPPVL PLVGHGHHFI GKPPHEMVKK
IFEFMETYSK DQVLKVWLGP ELNVLMGNPK DVEVVLGTLR FNDKAGEYKA LEPWLKEGLL
VSRGRKWHKR RKIITPAFHF KILDQFVEVF EKGSRDLLRN MEQDRLKHGE SGFSLYDWIN
LCTMDTICET AMGVSINAQS NADSEYVQAV KTISMVLHKR MFNILYRFDL TYMLTPLARA
EKKALNVLHQ FTEKIIVQRR EELIREGSSQ ESSNDDADVG AKRKMAFLDI LLQSTVDERP
LSNLDIREEV DTFMFEGHDT TSSALMFFFY NIATHPEAQK KCFEEIRSVV GNDKSTPVSY
ELLNQLHYVD LCVKETLRMY PSVPLLGRKV LEDCEINGKL IPAGTNIGIS PLYLGRREEL
FSEPNSFKPE RFDVVTTAEK LNPYAYIPFS AGPRNCIGQK FAMLEIKAIV ANVLRHYEVD
FVGDSSEPPV LIAELILRTK EPLMFKVRER VY
//
