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P00388

- NCPR_RAT

UniProt

P00388 - NCPR_RAT

Protein

NADPH--cytochrome P450 reductase

Gene

Por

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.

    Catalytic activityi

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

    Cofactori

    FAD.
    FMN.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi170 – 20132FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi314 – 32512FADBy similarityAdd
    BLAST
    Nucleotide bindingi451 – 46111FADBy similarityAdd
    BLAST
    Nucleotide bindingi530 – 54819NADPBy similarityAdd
    BLAST
    Nucleotide bindingi625 – 64117NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: RGD
    2. electron carrier activity Source: RGD
    3. enzyme binding Source: BHF-UCL
    4. flavin adenine dinucleotide binding Source: RGD
    5. FMN binding Source: RGD
    6. hydrolase activity Source: RGD
    7. iron-cytochrome-c reductase activity Source: RGD
    8. iron ion binding Source: InterPro
    9. NADP binding Source: RGD
    10. NADPH-hemoprotein reductase activity Source: BHF-UCL
    11. nitric oxide dioxygenase activity Source: RGD
    12. 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

    GO - Biological processi

    1. carnitine metabolic process Source: RGD
    2. cellular organofluorine metabolic process Source: Ensembl
    3. cellular response to follicle-stimulating hormone stimulus Source: RGD
    4. cellular response to gonadotropin stimulus Source: RGD
    5. cellular response to peptide hormone stimulus Source: RGD
    6. demethylation Source: RGD
    7. fatty acid oxidation Source: RGD
    8. flavonoid metabolic process Source: RGD
    9. internal peptidyl-lysine acetylation Source: RGD
    10. negative regulation of apoptotic process Source: RGD
    11. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
    12. negative regulation of lipase activity Source: RGD
    13. nitrate catabolic process Source: RGD
    14. nitric oxide catabolic process Source: RGD
    15. oxidation-reduction process Source: BHF-UCL
    16. positive regulation of cholesterol biosynthetic process Source: RGD
    17. positive regulation of chondrocyte differentiation Source: RGD
    18. positive regulation of monooxygenase activity Source: Ensembl
    19. positive regulation of smoothened signaling pathway Source: RGD
    20. positive regulation of steroid hormone biosynthetic process Source: RGD
    21. regulation of cholesterol metabolic process Source: RGD
    22. regulation of growth plate cartilage chondrocyte proliferation Source: RGD
    23. response to drug Source: RGD
    24. response to nutrient Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14290.
    SABIO-RKP00388.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase (EC:1.6.2.4)
    Short name:
    CPR
    Short name:
    P450R
    Gene namesi
    Name:Por
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 12

    Organism-specific databases

    RGDi68335. Por.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. intracellular membrane-bounded organelle Source: RGD
    4. membrane Source: RGD
    5. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 678677NADPH--cytochrome P450 reductasePRO_0000167600Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00388.
    PRIDEiP00388.

    Expressioni

    Gene expression databases

    GenevestigatoriP00388.

    Interactioni

    Protein-protein interaction databases

    BioGridi248088. 1 interaction.
    MINTiMINT-4564101.
    STRINGi10116.ENSRNOP00000001961.

    Structurei

    Secondary structure

    1
    678
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi69 – 768
    Beta strandi80 – 856
    Beta strandi87 – 893
    Helixi90 – 10112
    Helixi102 – 1054
    Beta strandi109 – 1124
    Helixi114 – 1163
    Helixi119 – 1279
    Beta strandi132 – 1409
    Turni141 – 1433
    Helixi147 – 1493
    Helixi150 – 1589
    Beta strandi167 – 1748
    Beta strandi176 – 1805
    Helixi183 – 19412
    Beta strandi198 – 2014
    Beta strandi204 – 2074
    Turni208 – 2103
    Helixi212 – 23120
    Beta strandi244 – 2496
    Helixi255 – 2573
    Beta strandi258 – 2614
    Beta strandi263 – 2653
    Turni266 – 2705
    Beta strandi278 – 2803
    Beta strandi282 – 29110
    Beta strandi294 – 2985
    Beta strandi300 – 3067
    Turni308 – 3114
    Beta strandi319 – 3224
    Helixi328 – 33710
    Beta strandi345 – 3517
    Beta strandi360 – 3667
    Helixi367 – 3737
    Helixi383 – 3897
    Helixi390 – 3923
    Beta strandi393 – 3953
    Helixi396 – 4038
    Helixi404 – 4063
    Beta strandi408 – 4103
    Helixi411 – 4199
    Turni420 – 4245
    Helixi427 – 4337
    Helixi441 – 4477
    Beta strandi454 – 4574
    Turni462 – 4643
    Beta strandi468 – 4747
    Beta strandi477 – 4793
    Beta strandi483 – 4875
    Helixi489 – 4968
    Beta strandi508 – 5147
    Beta strandi528 – 5314
    Helixi534 – 5374
    Helixi538 – 55215
    Beta strandi560 – 5678
    Turni569 – 5713
    Helixi576 – 5849
    Beta strandi587 – 5959
    Beta strandi598 – 6014
    Helixi605 – 6117
    Helixi613 – 6219
    Beta strandi626 – 6327
    Turni633 – 6353
    Helixi636 – 65116
    Helixi656 – 66813
    Beta strandi671 – 6777

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AMOX-ray2.60A/B64-678[»]
    1J9ZX-ray2.70A/B57-676[»]
    1JA0X-ray2.60A/B57-676[»]
    1JA1X-ray1.80A/B57-678[»]
    3ES9X-ray3.40A/B/C57-678[»]
    3OJWX-ray2.20A62-678[»]
    3OJXX-ray2.50A57-678[»]
    3WKTX-ray4.30A/B58-678[»]
    ProteinModelPortaliP00388.
    SMRiP00388. Positions 63-678.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00388.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 224145Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini279 – 521243FAD-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.
    HOGENOMiHOG000282027.
    HOVERGENiHBG000432.
    InParanoidiP00388.
    KOiK00327.
    OMAiVYSENSI.
    OrthoDBiEOG7HQN7J.
    PhylomeDBiP00388.
    TreeFamiTF105719.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00388-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDSHEDTSA TMPEAVAEEV SLFSTTDMVL FSLIVGVLTY WFIFRKKKEE    50
    IPEFSKIQTT APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK 100
    DAHRYGMRGM SADPEEYDLA DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ 150
    DFYDWLQETD VDLTGVKFAV FGLGNKTYEH FNAMGKYVDQ RLEQLGAQRI 200
    FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES SIRQYELVVH 250
    EDMDVAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTANR KLNQGTERHL 300
    MHLELDISDS KIRYESGDHV AVYPANDSAL VNQIGEILGA DLDVIMSLNN 350
    LDEESNKKHP FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE 400
    HLHKMASSSG EGKELYLSWV VEARRHILAI LQDYPSLRPP IDHLCELLPR 450
    LQARYYSIAS SSKVHPNSVH ICAVAVEYEA KSGRVNKGVA TSWLRAKEPA 500
    GENGGRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGIAPF MGFIQERAWL 550
    REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA 600
    HKVYVQHLLK RDREHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE 650
    FGPMEHTQAV DYVKKLMTKG RYSLDVWS 678
    Length:678
    Mass (Da):76,963
    Last modified:January 23, 2007 - v3
    Checksum:iAF3087E4D7A352D6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551V → A in AAA41683. (PubMed:2125483)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10068 mRNA. Translation: AAA41064.1.
    M12516 mRNA. Translation: AAA41067.1.
    M58937
    , M58932, M58933, M58934, M58935, M58936 Genomic DNA. Translation: AAA41683.1.
    PIRiA36073. RDRTO4.
    RefSeqiNP_113764.1. NM_031576.1.
    UniGeneiRn.11359.

    Genome annotation databases

    EnsembliENSRNOT00000001961; ENSRNOP00000001961; ENSRNOG00000001442.
    GeneIDi29441.
    KEGGirno:29441.
    UCSCiRGD:68335. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10068 mRNA. Translation: AAA41064.1 .
    M12516 mRNA. Translation: AAA41067.1 .
    M58937
    , M58932 , M58933 , M58934 , M58935 , M58936 Genomic DNA. Translation: AAA41683.1 .
    PIRi A36073. RDRTO4.
    RefSeqi NP_113764.1. NM_031576.1.
    UniGenei Rn.11359.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AMO X-ray 2.60 A/B 64-678 [» ]
    1J9Z X-ray 2.70 A/B 57-676 [» ]
    1JA0 X-ray 2.60 A/B 57-676 [» ]
    1JA1 X-ray 1.80 A/B 57-678 [» ]
    3ES9 X-ray 3.40 A/B/C 57-678 [» ]
    3OJW X-ray 2.20 A 62-678 [» ]
    3OJX X-ray 2.50 A 57-678 [» ]
    3WKT X-ray 4.30 A/B 58-678 [» ]
    ProteinModelPortali P00388.
    SMRi P00388. Positions 63-678.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248088. 1 interaction.
    MINTi MINT-4564101.
    STRINGi 10116.ENSRNOP00000001961.

    Chemistry

    ChEMBLi CHEMBL2817.

    Proteomic databases

    PaxDbi P00388.
    PRIDEi P00388.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000001961 ; ENSRNOP00000001961 ; ENSRNOG00000001442 .
    GeneIDi 29441.
    KEGGi rno:29441.
    UCSCi RGD:68335. rat.

    Organism-specific databases

    CTDi 5447.
    RGDi 68335. Por.

    Phylogenomic databases

    eggNOGi COG0369.
    GeneTreei ENSGT00620000087711.
    HOGENOMi HOG000282027.
    HOVERGENi HBG000432.
    InParanoidi P00388.
    KOi K00327.
    OMAi VYSENSI.
    OrthoDBi EOG7HQN7J.
    PhylomeDBi P00388.
    TreeFami TF105719.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14290.
    SABIO-RK P00388.

    Miscellaneous databases

    EvolutionaryTracei P00388.
    NextBioi 609193.
    PROi P00388.

    Gene expression databases

    Genevestigatori P00388.

    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. "Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains."
      Porter T.D., Kasper C.B.
      Proc. Natl. Acad. Sci. U.S.A. 82:973-977(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression of rat NADPH-cytochrome P-450 reductase cDNA in Saccharomyces cerevisiae."
      Murakami H., Yabusaki Y., Ohkawa H.
      DNA 5:1-10(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein."
      Porter T.D., Beck T.W., Kasper C.B.
      Biochemistry 29:9814-9818(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Wistar.
      Tissue: Liver.
    4. "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes."
      Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S., Kim J.-J.P.
      Proc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    5. "NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer."
      Hubbard P.A., Shen A.L., Paschke R., Kasper C.B., Kim J.-J.P.
      J. Biol. Chem. 276:29163-29170(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS.

    Entry informationi

    Entry nameiNCPR_RAT
    AccessioniPrimary (citable) accession number: P00388
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3