ID   NCPR_DROME              Reviewed;         679 AA.
AC   Q27597; Q9VMF2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 91.
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
GN   Name=Cpr; ORFNames=CG11567;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Canton-S; TISSUE=Antenna;
RX   MEDLINE=97311413; PubMed=9168130; DOI=10.1016/S0378-1119(96)00851-7;
RA   Hovemann B.T., Sehlmeyer F., Malz J.;
RT   "Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase:
RT   pronounced expression in antennae may be related to odorant
RT   clearance.";
RL   Gene 189:213-219(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP
CC       to cytochrome p450 in microsomes. It can also provide electron
CC       transfer to heme oxygenase and cytochrome b5. May function to
CC       clear the olfactory organ (antennae) from accumulating chemicals.
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: FMN.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (By similarity). Note=Anchored to the ER membrane
CC       by its N-terminal hydrophobic region (By similarity).
CC   -!- TISSUE SPECIFICITY: High in antennae.
CC   -!- DEVELOPMENTAL STAGE: Embryos and adults.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X93090; CAA63639.1; -; mRNA.
DR   EMBL; AE014134; AAF52367.1; -; Genomic_DNA.
DR   EMBL; AY052000; AAK93424.1; -; mRNA.
DR   RefSeq; NP_477158.1; -.
DR   UniGene; Dm.6997; -.
DR   HSSP; P16435; 1B1C.
DR   DIP; DIP:19958N; -.
DR   IntAct; Q27597; 1.
DR   Ensembl; FBgn0015623; Drosophila melanogaster.
DR   GeneID; 33883; -.
DR   KEGG; dme:Dmel_CG11567; -.
DR   FlyBase; FBgn0015623; Cpr.
DR   HOGENOM; Q27597; -.
DR   OMA; Q27597; PEECDME.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-007638-MON; -.
DR   BRENDA; 1.6.2.4; 48.
DR   NextBio; 785740; -.
DR   ArrayExpress; Q27597; -.
DR   GermOnline; CG11567; Drosophila melanogaster.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR015702; NADPH_Cyt_P450_Rdtase.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   PANTHER; PTHR19384:SF17; NADPH_Cyt_Red; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; FMN;
KW   Membrane; NADP; Oxidoreductase.
FT   CHAIN         1    679       NADPH--cytochrome P450 reductase.
FT                                /FTId=PRO_0000167602.
FT   DOMAIN       84    228       Flavodoxin-like.
FT   DOMAIN      283    523       FAD-binding FR-type.
FT   NP_BIND     176    207       FMN (By similarity).
FT   NP_BIND     320    331       FAD (By similarity).
FT   NP_BIND     457    467       FAD (By similarity).
FT   NP_BIND     537    555       NADP (By similarity).
FT   NP_BIND     632    648       NADP (By similarity).
FT   CONFLICT     38     39       AA -> VT (in Ref. 1; CAA63639).
FT   CONFLICT     45     45       S -> T (in Ref. 1; CAA63639).
FT   CONFLICT    132    132       I -> T (in Ref. 1; CAA63639).
SQ   SEQUENCE   679 AA;  76347 MW;  C6387C111A0EDB4A CRC64;
     MASEQTIDGA AAIPSGGGDE PFLGLLDVAL LAVLIGGAAF YFLRSRKKEE EPTRSYSIQP
     TTVCTTSASD NSFIKKLKAS GRSLVVFYGS QTGTGEEFAG RLAKEGIRYR LKGMVADPEE
     CDMEELLQLK DIDNSLAVFC LATYGEGDPT DNAMEFYEWI TSGDVDLSGL NYAVFGLGNK
     TYEHYNKVAI YVDKRLEELG ANRVFELGLG DDDANIEDDF ITWKDRFWPA VCDHFGIEGG
     GEEVLIRQYR LLEQPDVQPD RIYTGEIARL HSIQNQRPPF DAKNPFLAPI KVNRELHKGG
     GRSCMHIELS IEGSKMRYDA GDHVAMFPVN DKSLVEKLGQ LCNADLDTVF SLINTDTDSS
     KKHPFPCPTT YRTALTHYLE ITAIPRTHIL KELAEYCTDE KEKELLRSMA SISPEGKEKY
     QSWIQDACRN IVHILEDIKS CRPPIDHVCE LLPRLQPRYY SISSSAKLHP TDVHVTAVLV
     EYKTPTGRIN KGVATTYLKN KQPQGSEEVK VPVFIRKSQF RLPTKPETPI IMVGPGTGLA
     PFRGFIQERQ FLRDEGKTVG ESILYFGCRK RSEDYIYESE LEEWVKKGTL NLKAAFSRDQ
     GKKVYVQHLL EQDADLIWNV IGENKGHFYI CGDAKNMAVD VRNILVKILS TKGNMSEADA
     VQYIKKMEAQ KRYSADVWS
//