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Q27597

- NCPR_DROME

UniProt

Q27597 - NCPR_DROME

Protein

NADPH--cytochrome P450 reductase

Gene

Cpr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    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 – 20732FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi320 – 33112FADBy similarityAdd
    BLAST
    Nucleotide bindingi457 – 46711FADBy similarityAdd
    BLAST
    Nucleotide bindingi537 – 55519NADPBy similarityAdd
    BLAST
    Nucleotide bindingi632 – 64817NADPBy 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

    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 By similarity; 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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    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

    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:
    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

    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: October 1, 2014
    This is version 129 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