位置:首页 > 蛋白库 > CP6A9_DROME
CP6A9_DROME
ID   CP6A9_DROME             Reviewed;         504 AA.
AC   Q27594; Q8MRY8; Q9V772;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Cytochrome P450 6a9;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPVIA9;
GN   Name=Cyp6a9; ORFNames=CG10246;
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 FUNCTION.
RC   STRAIN=91-R;
RX   PubMed=8973362; DOI=10.1016/s0378-1119(96)00446-5;
RA   Maitra S., Dombrowski S.M., Waters L.C., Ganguly R.;
RT   "Three second chromosome-linked clustered Cyp6 genes show differential
RT   constitutive and barbital-induced expression in DDT-resistant and
RT   susceptible strains of Drosophila melanogaster.";
RL   Gene 180:165-171(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).
CC   -!- FUNCTION: Involved in the metabolism of insect hormones and in the
CC       breakdown of synthetic insecticides. {ECO:0000269|PubMed:8973362}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB46609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L46860; AAB46609.1; ALT_INIT; mRNA.
DR   EMBL; AE013599; AAF58188.2; -; Genomic_DNA.
DR   EMBL; AY119196; AAM51056.1; -; mRNA.
DR   PIR; JC5321; JC5321.
DR   RefSeq; NP_523748.2; NM_079024.3.
DR   AlphaFoldDB; Q27594; -.
DR   SMR; Q27594; -.
DR   BioGRID; 62405; 6.
DR   IntAct; Q27594; 5.
DR   STRING; 7227.FBpp0289405; -.
DR   PaxDb; Q27594; -.
DR   PRIDE; Q27594; -.
DR   EnsemblMetazoa; FBtr0300128; FBpp0289405; FBgn0013771.
DR   GeneID; 36663; -.
DR   KEGG; dme:Dmel_CG10246; -.
DR   CTD; 36663; -.
DR   FlyBase; FBgn0013771; Cyp6a9.
DR   VEuPathDB; VectorBase:FBgn0013771; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   GeneTree; ENSGT00940000165972; -.
DR   HOGENOM; CLU_001570_5_2_1; -.
DR   InParanoid; Q27594; -.
DR   OrthoDB; 467733at2759; -.
DR   PhylomeDB; Q27594; -.
DR   SignaLink; Q27594; -.
DR   BioGRID-ORCS; 36663; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36663; -.
DR   PRO; PR:Q27594; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0013771; Expressed in adult Malpighian tubule (Drosophila) and 22 other tissues.
DR   Genevisible; Q27594; 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Cytochrome P450 6a9"
FT                   /id="PRO_0000051868"
FT   BINDING         449
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        137
FT                   /note="Y -> S (in Ref. 1; AAB46609 and 4; AAM51056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        376
FT                   /note="V -> D (in Ref. 1; AAB46609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424..434
FT                   /note="DNFSPERVKER -> IFFARTSEGS (in Ref. 1; AAB46609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="N -> L (in Ref. 1; AAB46609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="S -> I (in Ref. 4; AAM51056)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  58005 MW;  3B0C875DAC3D4290 CRC64;
     MGVYSVLLAI VVVLVGYLLL KWRRALHYWQ NLDIPCEEPH ILMGSLTGVQ TSRSFSAIWM
     DYYNKFRGTG PFAGFYWFQR PGILVLDISL AKLILIKEFN KFTDRGFYHN TEDDPLSGQL
     FLLDGQKWKS MRSKLSYTFT SGKMKYMFPT VVKVGHEFIE VFGQAMEKSP IVEVRDILAR
     FTTDVIGTCA FGIECSSLKD PEAEFRVMGR RAIFEQRHGP IGIAFINSFQ NLARRLHMKI
     TLEEAEHFFL RIVRETVAFR EKNNIRRNDF MDQLIDLKNS PLTKSESGES VNLTIEEMAA
     QAFVFFGAGF ETSSTTMGFA LYELAQHQDI QDRVRKECQE VIGKYNGEIT YESMKDMVYL
     DQVISETLRL YTVLPVLNRE CLEDYEVPGH PKYVIKKGMP VLIPCGAMHR DEKLYANPNT
     FNPDNFSPER VKERDSVEWL PFGDGPRNCI GMRFGQMQAR SGLALLINRF KFSVCEQTTI
     PIVYSKKTFL ISSETGIFLK VERV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024