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Q27597

- NCPR_DROME

UniProt

Q27597 - NCPR_DROME

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Protein

NADPH--cytochrome P450 reductase

Gene
Cpr, CG11567
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 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. May function to clear the olfactory organ (antennae) from accumulating chemicals.1 Publication

Catalytic activityi

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

Cofactori

FAD.
FMN.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi176 – 20732FMN By similarityAdd
BLAST
Nucleotide bindingi320 – 33112FAD By similarityAdd
BLAST
Nucleotide bindingi457 – 46711FAD By similarityAdd
BLAST
Nucleotide bindingi537 – 55519NADP By similarityAdd
BLAST
Nucleotide bindingi632 – 64817NADP By similarityAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. NADPH-hemoprotein reductase activity Source: UniProtKB-EC
  4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Short name:
CPR
Short name:
P450R
Gene namesi
Name:Cpr
ORF Names:CG11567
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0015623. Cpr.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity
Note: Anchored to the ER membrane by its N-terminal hydrophobic region By similarity.

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. 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.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ27597.
SMRiQ27597. Positions 71-679.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 228145Flavodoxin-likeAdd
BLAST
Domaini283 – 523241FAD-binding FR-typeAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Phylogenomic databases

eggNOGiCOG0369.
GeneTreeiENSGT00620000087711.
InParanoidiQ27597.
KOiK00327.
OMAiLWQLIHE.
OrthoDBiEOG7HQN7J.
PhylomeDBiQ27597.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
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

MASEQTIDGA AAIPSGGGDE PFLGLLDVAL LAVLIGGAAF YFLRSRKKEE    50
EPTRSYSIQP TTVCTTSASD NSFIKKLKAS GRSLVVFYGS QTGTGEEFAG 100
RLAKEGIRYR LKGMVADPEE CDMEELLQLK DIDNSLAVFC LATYGEGDPT 150
DNAMEFYEWI TSGDVDLSGL NYAVFGLGNK TYEHYNKVAI YVDKRLEELG 200
ANRVFELGLG DDDANIEDDF ITWKDRFWPA VCDHFGIEGG GEEVLIRQYR 250
LLEQPDVQPD RIYTGEIARL HSIQNQRPPF DAKNPFLAPI KVNRELHKGG 300
GRSCMHIELS IEGSKMRYDA GDHVAMFPVN DKSLVEKLGQ LCNADLDTVF 350
SLINTDTDSS KKHPFPCPTT YRTALTHYLE ITAIPRTHIL KELAEYCTDE 400
KEKELLRSMA SISPEGKEKY QSWIQDACRN IVHILEDIKS CRPPIDHVCE 450
LLPRLQPRYY SISSSAKLHP TDVHVTAVLV EYKTPTGRIN KGVATTYLKN 500
KQPQGSEEVK VPVFIRKSQF RLPTKPETPI IMVGPGTGLA PFRGFIQERQ 550
FLRDEGKTVG ESILYFGCRK RSEDYIYESE LEEWVKKGTL NLKAAFSRDQ 600
GKKVYVQHLL EQDADLIWNV IGENKGHFYI CGDAKNMAVD VRNILVKILS 650
TKGNMSEADA VQYIKKMEAQ KRYSADVWS 679
Length:679
Mass (Da):76,347
Last modified:December 1, 2000 - v2
Checksum:iC6387C111A0EDB4A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392AA → VT in CAA63639. 1 Publication
Sequence conflicti45 – 451S → T in CAA63639. 1 Publication
Sequence conflicti132 – 1321I → T in CAA63639. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X93090 mRNA. Translation: CAA63639.1 .
AE014134 Genomic DNA. Translation: AAF52367.1 .
AY052000 mRNA. Translation: AAK93424.1 .
RefSeqi NP_001260128.1. NM_001273199.1.
NP_001260129.1. NM_001273200.1.
NP_477158.1. NM_057810.4.
UniGenei Dm.6997.

3D structure databases

ProteinModelPortali Q27597.
SMRi Q27597. Positions 71-679.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60040. 1 interaction.
DIPi DIP-19958N.
MINTi MINT-863368.

Proteomic databases

PaxDbi Q27597.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0079250 ; FBpp0078880 ; FBgn0015623 .
FBtr0331223 ; FBpp0303665 ; FBgn0015623 .
FBtr0331224 ; FBpp0303666 ; FBgn0015623 .
GeneIDi 33883.
KEGGi dme:Dmel_CG11567.

Organism-specific databases

CTDi 33883.
FlyBasei FBgn0015623. Cpr.

Phylogenomic databases

eggNOGi COG0369.
GeneTreei ENSGT00620000087711.
InParanoidi Q27597.
KOi K00327.
OMAi LWQLIHE.
OrthoDBi EOG7HQN7J.
PhylomeDBi Q27597.

Miscellaneous databases

GenomeRNAii 33883.
NextBioi 785740.
PROi Q27597.

Gene expression databases

Bgeei Q27597.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000208. P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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: July 9, 2014
This is version 128 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

External Data

Dasty 3

Similar proteinsi