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Protein

NADPH--cytochrome P450 reductase

Gene

Cpr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

This enzyme is required for electron transfer from NADP to cytochrome p450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome b5 (By similarity). May function to clear the olfactory organ (antennae) from accumulating chemicals.UniRule annotation1 Publication

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotationNote: Binds 1 FAD per monomer.UniRule annotation
  • FMNUniRule annotationNote: Binds 1 FMN per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei212 – 2121FMNUniRule annotation
Binding sitei302 – 3021NADPUniRule annotation
Binding sitei482 – 4821FADUniRule annotation
Binding sitei537 – 5371NADPUniRule annotation
Binding sitei640 – 6401NADPUniRule annotation
Binding sitei678 – 6781FADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 956FMNUniRule annotation
Nucleotide bindingi142 – 1454FMNUniRule annotation
Nucleotide bindingi177 – 18610FMNUniRule annotation
Nucleotide bindingi458 – 4614FADUniRule annotation
Nucleotide bindingi476 – 4783FADUniRule annotation
Nucleotide bindingi492 – 4954FADUniRule annotation
Nucleotide bindingi597 – 5982NADPUniRule annotation
Nucleotide bindingi603 – 6075NADPUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

ReactomeiR-DME-211897. Cytochrome P450 - arranged by substrate type.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation)
Short name:
CPRUniRule annotation
Short name:
P450RUniRule annotation
Gene namesi
Name:Cpr
ORF Names:CG11567
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0015623. Cpr.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121LumenalUniRule annotationAdd
BLAST
Transmembranei22 – 4221HelicalUniRule annotationAdd
BLAST
Topological domaini43 – 679637CytoplasmicUniRule annotationAdd
BLAST

GO - Cellular componenti

  • endomembrane system Source: FlyBase
  • endoplasmic reticulum Source: FlyBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lipid particle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 679679NADPH--cytochrome P450 reductasePRO_0000167602Add
BLAST

Proteomic databases

PaxDbiQ27597.

Expressioni

Tissue specificityi

High in antennae.1 Publication

Developmental stagei

Embryos and adults.

Gene expression databases

BgeeiQ27597.
ExpressionAtlasiQ27597. differential.
GenevisibleiQ27597. DM.

Interactioni

Protein-protein interaction databases

BioGridi60040. 1 interaction.
DIPiDIP-19958N.
MINTiMINT-863368.
STRINGi7227.FBpp0078880.

Structurei

3D structure databases

ProteinModelPortaliQ27597.
SMRiQ27597. Positions 71-679.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 228145Flavodoxin-likeUniRule annotationAdd
BLAST
Domaini283 – 523241FAD-binding FR-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation
In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Contains 1 FAD-binding FR-type domain.UniRule annotation
Contains 1 flavodoxin-like domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
GeneTreeiENSGT00840000129950.
InParanoidiQ27597.
KOiK00327.
OMAiYEWITSG.
OrthoDBiEOG7HQN7J.
PhylomeDBiQ27597.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27597-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEQTIDGA AAIPSGGGDE PFLGLLDVAL LAVLIGGAAF YFLRSRKKEE
60 70 80 90 100
EPTRSYSIQP TTVCTTSASD NSFIKKLKAS GRSLVVFYGS QTGTGEEFAG
110 120 130 140 150
RLAKEGIRYR LKGMVADPEE CDMEELLQLK DIDNSLAVFC LATYGEGDPT
160 170 180 190 200
DNAMEFYEWI TSGDVDLSGL NYAVFGLGNK TYEHYNKVAI YVDKRLEELG
210 220 230 240 250
ANRVFELGLG DDDANIEDDF ITWKDRFWPA VCDHFGIEGG GEEVLIRQYR
260 270 280 290 300
LLEQPDVQPD RIYTGEIARL HSIQNQRPPF DAKNPFLAPI KVNRELHKGG
310 320 330 340 350
GRSCMHIELS IEGSKMRYDA GDHVAMFPVN DKSLVEKLGQ LCNADLDTVF
360 370 380 390 400
SLINTDTDSS KKHPFPCPTT YRTALTHYLE ITAIPRTHIL KELAEYCTDE
410 420 430 440 450
KEKELLRSMA SISPEGKEKY QSWIQDACRN IVHILEDIKS CRPPIDHVCE
460 470 480 490 500
LLPRLQPRYY SISSSAKLHP TDVHVTAVLV EYKTPTGRIN KGVATTYLKN
510 520 530 540 550
KQPQGSEEVK VPVFIRKSQF RLPTKPETPI IMVGPGTGLA PFRGFIQERQ
560 570 580 590 600
FLRDEGKTVG ESILYFGCRK RSEDYIYESE LEEWVKKGTL NLKAAFSRDQ
610 620 630 640 650
GKKVYVQHLL EQDADLIWNV IGENKGHFYI CGDAKNMAVD VRNILVKILS
660 670
TKGNMSEADA VQYIKKMEAQ KRYSADVWS
Length:679
Mass (Da):76,347
Last modified:December 1, 2000 - v2
Checksum:iC6387C111A0EDB4A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392AA → VT in CAA63639 (PubMed:9168130).Curated
Sequence conflicti45 – 451S → T in CAA63639 (PubMed:9168130).Curated
Sequence conflicti132 – 1321I → T in CAA63639 (PubMed:9168130).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93090 mRNA. Translation: CAA63639.1.
AE014134 Genomic DNA. Translation: AAF52367.1.
AY052000 mRNA. Translation: AAK93424.1.
RefSeqiNP_001260128.1. NM_001273199.1.
NP_001260129.1. NM_001273200.1.
NP_477158.1. NM_057810.4.
UniGeneiDm.6997.

Genome annotation databases

EnsemblMetazoaiFBtr0079250; FBpp0078880; FBgn0015623.
FBtr0331223; FBpp0303665; FBgn0015623.
FBtr0331224; FBpp0303666; FBgn0015623.
GeneIDi33883.
KEGGidme:Dmel_CG11567.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93090 mRNA. Translation: CAA63639.1.
AE014134 Genomic DNA. Translation: AAF52367.1.
AY052000 mRNA. Translation: AAK93424.1.
RefSeqiNP_001260128.1. NM_001273199.1.
NP_001260129.1. NM_001273200.1.
NP_477158.1. NM_057810.4.
UniGeneiDm.6997.

3D structure databases

ProteinModelPortaliQ27597.
SMRiQ27597. Positions 71-679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60040. 1 interaction.
DIPiDIP-19958N.
MINTiMINT-863368.
STRINGi7227.FBpp0078880.

Proteomic databases

PaxDbiQ27597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079250; FBpp0078880; FBgn0015623.
FBtr0331223; FBpp0303665; FBgn0015623.
FBtr0331224; FBpp0303666; FBgn0015623.
GeneIDi33883.
KEGGidme:Dmel_CG11567.

Organism-specific databases

CTDi33883.
FlyBaseiFBgn0015623. Cpr.

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
GeneTreeiENSGT00840000129950.
InParanoidiQ27597.
KOiK00327.
OMAiYEWITSG.
OrthoDBiEOG7HQN7J.
PhylomeDBiQ27597.

Enzyme and pathway databases

ReactomeiR-DME-211897. Cytochrome P450 - arranged by substrate type.

Miscellaneous databases

GenomeRNAii33883.
PROiQ27597.

Gene expression databases

BgeeiQ27597.
ExpressionAtlasiQ27597. differential.
GenevisibleiQ27597. DM.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: pronounced expression in antennae may be related to odorant clearance."
    Hovemann B.T., Sehlmeyer F., Malz J.
    Gene 189:213-219(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Canton-S.
    Tissue: Antenna.
  2. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    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.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiNCPR_DROME
AccessioniPrimary (citable) accession number: Q27597
Secondary accession number(s): Q9VMF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.