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UniProtKB/Swiss-Prot entry Q27597


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NCPR_DROME
Primary accession number Q27597
Secondary accession number Q9VMF2
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 84)
Name and origin of the protein
Protein name NADPH--cytochrome P450 reductase
Synonyms CPR
P450R
EC 1.6.2.4
Gene name
Name: Cpr
ORFNames: CG11567
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Canton-S;
TISSUE=Antenna;
DOI=10.1016/S0378-1119(96)00851-7; PubMed=9168130 [NCBI, ExPASy, EBI, Israel, Japan]
Hovemann B.T., Sehlmeyer F., Malz J.;
"Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: pronounced expression in antennae may be related to odorant clearance.";
Gene 189:213-219(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X93090; CAA63639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAF52367.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY052000; AAK93424.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_477158.1; -.
UniGene Dm.6997
3D structure databases
HSSP P16435; 1B1C. [HSSP ENTRY / PDB]
ModBase Q27597.
Protein-protein interaction databases
DIP DIP:19958N; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-007638-MON; -.
Organism-specific databases
FlyBase FBgn0015623; Cpr.
Gene expression databases
ArrayExpress Q27597; -.
GermOnline CG11567; Drosophila melanogaster.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
PANTHER PTHR19384:SF17; NADPH_Cyt_Red; 1.
Pfam PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00369; FLAVODOXIN.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q27597.
Genome annotation databases
Ensembl CG11567; Drosophila melanogaster. [Contig view]
GeneID 33883; -.
KEGG dme:Dmel_CG11567; -.
Phylogenomic databases
HOGENOM Q27597; -.
Other
ProtoNet Q27597.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   679  679     NADPH--cytochrome P450 reductase. PRO_0000167602
DOMAIN   84   228  145     Flavodoxin-like. 
DOMAIN   283   523  241     FAD-binding FR-type. 
NP_BIND   176   207  32     FMN (By similarity). 
NP_BIND   320   331  12     FAD (By similarity). 
NP_BIND   457   467  11     FAD (By similarity). 
NP_BIND   537   555  19     NADP (By similarity). 
NP_BIND   632   648  17     NADP (By similarity). 
CONFLICT   38    39        AA -> VT (in Ref. 1; CAA63639). 
CONFLICT   45    45        S -> T (in Ref. 1; CAA63639). 
CONFLICT   132   132        I -> T (in Ref. 1; CAA63639). 
Sequence information
Length: 679 AA [This is the length of the unprocessed precursor] Molecular weight: 76347 Da [This is the MW of the unprocessed precursor] CRC64: C6387C111A0EDB4A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASEQTIDGA AAIPSGGGDE PFLGLLDVAL LAVLIGGAAF YFLRSRKKEE EPTRSYSIQP 

        70         80         90        100        110        120 
TTVCTTSASD NSFIKKLKAS GRSLVVFYGS QTGTGEEFAG RLAKEGIRYR LKGMVADPEE 

       130        140        150        160        170        180 
CDMEELLQLK DIDNSLAVFC LATYGEGDPT DNAMEFYEWI TSGDVDLSGL NYAVFGLGNK 

       190        200        210        220        230        240 
TYEHYNKVAI YVDKRLEELG ANRVFELGLG DDDANIEDDF ITWKDRFWPA VCDHFGIEGG 

       250        260        270        280        290        300 
GEEVLIRQYR LLEQPDVQPD RIYTGEIARL HSIQNQRPPF DAKNPFLAPI KVNRELHKGG 

       310        320        330        340        350        360 
GRSCMHIELS IEGSKMRYDA GDHVAMFPVN DKSLVEKLGQ LCNADLDTVF SLINTDTDSS 

       370        380        390        400        410        420 
KKHPFPCPTT YRTALTHYLE ITAIPRTHIL KELAEYCTDE KEKELLRSMA SISPEGKEKY 

       430        440        450        460        470        480 
QSWIQDACRN IVHILEDIKS CRPPIDHVCE LLPRLQPRYY SISSSAKLHP TDVHVTAVLV 

       490        500        510        520        530        540 
EYKTPTGRIN KGVATTYLKN KQPQGSEEVK VPVFIRKSQF RLPTKPETPI IMVGPGTGLA 

       550        560        570        580        590        600 
PFRGFIQERQ FLRDEGKTVG ESILYFGCRK RSEDYIYESE LEEWVKKGTL NLKAAFSRDQ 

       610        620        630        640        650        660 
GKKVYVQHLL EQDADLIWNV IGENKGHFYI CGDAKNMAVD VRNILVKILS TKGNMSEADA 

       670 
VQYIKKMEAQ KRYSADVWS 

Q27597 in FASTA format

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