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CP4D1_DROME
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   03-AUG-2022, entry version 165.
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; P33269; -.
DR   PeptideAtlas; P33269; -.
DR   PRIDE; P33269; -.
DR   DNASU; 31188; -.
DR   GeneID; 31188; -.
DR   KEGG; dme:Dmel_CG3656; -.
DR   CTD; 31188; -.
DR   FlyBase; FBgn0005670; Cyp4d1.
DR   VEuPathDB; VectorBase:FBgn0005670; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   InParanoid; P33269; -.
DR   PhylomeDB; P33269; -.
DR   Reactome; R-DME-193144; Estrogen biosynthesis.
DR   Reactome; R-DME-211976; Endogenous sterols.
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   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   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
 
 
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