CP9H1_DROME
ID CP9H1_DROME Reviewed; 518 AA.
AC Q9V6H1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable cytochrome P450 9h1;
DE EC=1.14.-.-;
DE AltName: Full=CYPIXH1;
GN Name=Cyp9h1; ORFNames=CG17577;
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 [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 [2]
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).
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; AE013599; AAF58453.1; -; Genomic_DNA.
DR RefSeq; NP_610820.1; NM_136976.2.
DR AlphaFoldDB; Q9V6H1; -.
DR SMR; Q9V6H1; -.
DR IntAct; Q9V6H1; 1.
DR STRING; 7227.FBpp0086933; -.
DR PaxDb; Q9V6H1; -.
DR PRIDE; Q9V6H1; -.
DR DNASU; 36412; -.
DR EnsemblMetazoa; FBtr0087820; FBpp0086933; FBgn0033775.
DR GeneID; 36412; -.
DR KEGG; dme:Dmel_CG17577; -.
DR UCSC; CG17577-RA; d. melanogaster.
DR CTD; 36412; -.
DR FlyBase; FBgn0033775; Cyp9h1.
DR VEuPathDB; VectorBase:FBgn0033775; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00940000165057; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q9V6H1; -.
DR OMA; RRKDNEF; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; Q9V6H1; -.
DR BioGRID-ORCS; 36412; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36412; -.
DR PRO; PR:Q9V6H1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033775; Expressed in second segment of antenna (Drosophila) and 18 other tissues.
DR ExpressionAtlas; Q9V6H1; baseline and differential.
DR Genevisible; Q9V6H1; 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 3: Inferred from homology;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..518
FT /note="Probable cytochrome P450 9h1"
FT /id="PRO_0000051921"
FT BINDING 462
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"
SQ SEQUENCE 518 AA; 60045 MW; A3585251AA179421 CRC64;
MDQSMIALAL FIILLVLLYK WSVAKYDVFS ERGVSHEKPW PLIGNIPLKA MIGGMPVLKK
MIELHTKHTG SPVYGIYALR DAVFFVRDPE LIKLIGIKEF DHFVNHNSMH NNIQESILSK
SLISLRDGRW KEMRNILTPA FTGSKMRIMY DLIQSCSEEG VIHIQEQLEL SQDASIELEM
KDYFTRFAND VIATVAFGIS INSFRRKDNE FFRIGQAMSR ISAWSVVKAM LYALFPRLMK
VLRIQVLDTK NIDYFSSLVT AAMRYRQEHK VVRPDMIHLL MEAKQQRLAD LSDKSKDELY
YSEFTADDLL AQCLLFFFAG FEIISSSLCF LTHELCLNPT VQDRLYEEII SVHEELKGQP
LTYDKLTKMK YLDMVVLEAL RKWPPSISTD RECRQDIDLF DENGQKLFSA RKGDVLQIPI
FSLHHDPENF EDPEFFNPER FADGHALESR VYMPFGVGPR NCIGNRMALM ELKSIVYQLL
LNFKLLPAKR TSRDLLNDIR GHGLKPKNGF WLKFEARQ
