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P04175

- NCPR_PIG

UniProt

P04175 - NCPR_PIG

Protein

NADPH--cytochrome P450 reductase

Gene

POR

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (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 bindingi529 – 54719NADPBy similarityAdd
    BLAST
    Nucleotide bindingi624 – 64017NADPBy 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

    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: 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
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 678677NADPH--cytochrome P450 reductasePRO_0000167598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP04175.

    Structurei

    3D structure databases

    ProteinModelPortaliP04175.
    SMRiP04175. Positions 64-678.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    HOVERGENiHBG000432.
    KOiK00327.

    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.

    P04175-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDSNVDTGT TTSEMVAEEV SLFSATDMVL FSLIVGLLTY WFIFRKKKDE    50
    VPEFSKIETT TSSVKDSSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK 100
    DAHRYGMRGM AADPEEYDLS DLSSLPEIEN ALAVFCMATY GEGDPTDNAQ 150
    DFYDWLQEAD VDLTGVKYAV FGLGNKTYEH FNAMGKYVDK RLEQLGAQRI 200
    FDLGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES SIRQYELVVH 250
    TDMDTAVVYT GEMGRLKSYE NQKPPFDAKN PFLAVVTTNR KLNQGTERHL 300
    MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGEILGT DLDIVMSLNN 350
    LDEESNKRHP FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE 400
    QLRKMASSSG EGKELYLSWV VEARRHILAI LQDYPSLRPP IDHLCERLPR 450
    LQARYYSIAS SSKVHPNSVH ICAVVVEYET KSGRVNKGVA TSWLRAKEPA 500
    GENGRRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF IGFIQERAWL 550
    QEQGKEVGET LLYYGCRRSD EDYLYREELA QFHAKGALTR LSVAFSREQP 600
    QKVYVQHLLK RDKEHLWKLI HDGGAHIYIC GDARNMARDV QNTFCDIVAE 650
    QGPMEHAQAV DYVKKLMTKG RYSLDVWS 678
    Length:678
    Mass (Da):76,833
    Last modified:January 23, 2007 - v2
    Checksum:i206079E13CA6E0A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551S → T in AAA85368. 1 PublicationCurated
    Sequence conflicti164 – 1641T → S in AAA85368. 1 PublicationCurated
    Sequence conflicti175 – 1751N → D AA sequence (PubMed:3098240)Curated
    Sequence conflicti340 – 3401T → A AA sequence (PubMed:3098240)Curated
    Sequence conflicti379 – 3791N → D AA sequence (PubMed:3098240)Curated
    Sequence conflicti401 – 4011Q → E AA sequence (PubMed:3098240)Curated
    Sequence conflicti447 – 4471R → L in AAA85368. 1 PublicationCurated
    Sequence conflicti503 – 5031N → D AA sequence (PubMed:3098240)Curated
    Sequence conflicti509 – 5091V → L AA sequence (PubMed:3099837)Curated
    Sequence conflicti509 – 5091V → L AA sequence (PubMed:3098240)Curated
    Sequence conflicti675 – 6751D → N AA sequence (PubMed:3098240)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33893 mRNA. Translation: AAA85368.1.
    PIRiA25584. RDPGO4.
    RefSeqiNP_001123431.1. NM_001129959.1.
    UniGeneiSsc.50299.

    Genome annotation databases

    GeneIDi100170114.
    KEGGissc:100170114.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33893 mRNA. Translation: AAA85368.1 .
    PIRi A25584. RDPGO4.
    RefSeqi NP_001123431.1. NM_001129959.1.
    UniGenei Ssc.50299.

    3D structure databases

    ProteinModelPortali P04175.
    SMRi P04175. Positions 64-678.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P04175.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100170114.
    KEGGi ssc:100170114.

    Organism-specific databases

    CTDi 5447.

    Phylogenomic databases

    HOVERGENi HBG000432.
    KOi K00327.

    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. Amborn J., Preiss B., Stender B., Viale M., Repp R.Z., Lampert F., Kroger M., Lumper L.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete amino acid sequence of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes."
      Haniu M., Iyanagi T., Miller P., Lee T.D., Shively J.E.
      Biochemistry 25:7906-7911(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-678, ACETYLATION AT GLY-2.
    3. "Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase."
      Vogel F., Lumper L.
      Biochem. J. 236:871-878(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 57-678.

    Entry informationi

    Entry nameiNCPR_PIG
    AccessioniPrimary (citable) accession number: P04175
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 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