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P00389

- NCPR_RABIT

UniProt

P00389 - NCPR_RABIT

Protein

NADPH--cytochrome P450 reductase

Gene

POR

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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 bindingi171 – 20232FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi315 – 32612FADBy similarityAdd
    BLAST
    Nucleotide bindingi452 – 46211FADBy similarityAdd
    BLAST
    Nucleotide bindingi530 – 54819NADPBy similarityAdd
    BLAST
    Nucleotide bindingi625 – 64117NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. FMN binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. NADPH-hemoprotein reductase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14302.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase (EC:1.6.2.4)
    Short name:
    CPR
    Short name:
    P450R
    Cleaved into the following chain:
    Gene namesi
    Name:POR
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 679679NADPH--cytochrome P450 reductasePRO_0000167599Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 679678NADPH--cytochrome P450 reductase, N-terminally processedPRO_0000421789Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000020921.

    Structurei

    3D structure databases

    ProteinModelPortaliP00389.
    SMRiP00389. Positions 65-679.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 225145Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini280 – 522243FAD-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.
    HOGENOMiHOG000282027.
    HOVERGENiHBG000432.

    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.

    P00389-1 [UniParc]FASTAAdd to Basket

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    MADSHGDTGA TMPEAAAQEA SVFSMTDVVL FSLIVGLITY WFLFRKKKEE    50
    VPEFTKIQAP TSSSVKESSF VEKMKKTGRN IVVFYGSQTG TAEEFANRLS 100
    KDAHRYGMRG MAADPEEYDL ADLSSLPEIN NALAVFCMAT YGEGDPTDNA 150
    QDFYDWLQET DVDLSGVKYA VFGLGNKTYE HFNAMGKYVD QRLEQLGAQR 200
    IFELGMGDDD ANLEEDFITW REQFWPAVCE HFGVEATGEE SSIRQYELVL 250
    HTDIDVAKVY QGEMGRLKSY ENQKPPFDAK NPFLATVTTN RKLNQGTERH 300
    LMHLELDISD SKIRYESGDH VAVYPANDSA LVNQLGEILG ADLDVVMSLN 350
    NLDEESNKKH PFPCPTSYRT ALTYYLDITN PPRTNVLYEL AQYAADPAEQ 400
    EQLRKMASSS GEGKELYLSW VVEARRHILA ILQDYPSLRP PIDHLCELLP 450
    RLQARYYSIA SSSKVHPNSV HICAVAVEYE TKAGRLNKGV ATSWLRAKEP 500
    AGENGGRALV PMFVRKSQFR LPFKATTPVI MVGPGTGVAP FIGFIQERAW 550
    LRQQGKEVGE TLLYYGCRRA AEDYLYREEL AGFQKDGTLS QLNVAFSREQ 600
    AQKVYVQHLL RRDKEHLWRL IHEGGAHIYV CGDARNMARD VQNTFYDIVA 650
    ELGAMEHAQA VDYVKKLMTK GRYSLDVWS 679
    Length:679
    Mass (Da):76,588
    Last modified:July 21, 1986 - v1
    Checksum:iB1A163FA53A5988B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 412YW → NY AA sequence (PubMed:6802823)Curated
    Sequence conflicti53 – 531E → N AA sequence (PubMed:6802823)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00101 mRNA. Translation: BAA00063.1.
    X04610 mRNA. Translation: CAA28279.1.
    PIRiA25505.
    RefSeqiNP_001153762.1. NM_001160290.1.
    UniGeneiOcu.2197.

    Genome annotation databases

    GeneIDi100301554.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00101 mRNA. Translation: BAA00063.1 .
    X04610 mRNA. Translation: CAA28279.1 .
    PIRi A25505.
    RefSeqi NP_001153762.1. NM_001160290.1.
    UniGenei Ocu.2197.

    3D structure databases

    ProteinModelPortali P00389.
    SMRi P00389. Positions 65-679.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000020921.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100301554.

    Organism-specific databases

    CTDi 5447.

    Phylogenomic databases

    eggNOGi COG0369.
    HOGENOMi HOG000282027.
    HOVERGENi HBG000432.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14302.

    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. "Molecular cloning and sequence analysis of full-length cDNA for rabbit liver NADPH-cytochrome P-450 reductase mRNA."
      Katagiri M., Murakami H., Yabusaki Y., Sugiyama T., Okamoto M., Yamano T., Ohkawa H.
      J. Biochem. 100:945-954(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region."
      Black S.D., Coon M.J.
      J. Biol. Chem. 257:5929-5938(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-81.
      Tissue: Liver.

    Entry informationi

    Entry nameiNCPR_RABIT
    AccessioniPrimary (citable) accession number: P00389
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3