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P00388 (NCPR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase

Short name=CPR
Short name=P450R
EC=1.6.2.4
Gene names
Name:Por
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length678 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

FAD.

FMN.

Subcellular location

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

Sequence similarities

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

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   LigandFAD
Flavoprotein
FMN
NADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarnitine metabolic process

Inferred from expression pattern PubMed 16616465. Source: RGD

cellular organofluorine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to follicle-stimulating hormone stimulus

Inferred from expression pattern PubMed 19077323. Source: RGD

cellular response to gonadotropin stimulus

Inferred from expression pattern PubMed 19077323. Source: RGD

cellular response to peptide hormone stimulus

Inferred from expression pattern PubMed 19077323. Source: RGD

demethylation

Inferred from direct assay PubMed 19171935. Source: RGD

fatty acid oxidation

Inferred from direct assay PubMed 17400174. Source: RGD

flavonoid metabolic process

Inferred from expression pattern PubMed 18803703. Source: RGD

internal peptidyl-lysine acetylation

Inferred from direct assay PubMed 18194664. Source: RGD

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 19264869. Source: RGD

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 19264869. Source: RGD

negative regulation of lipase activity

Inferred from direct assay PubMed 18801337. Source: RGD

nitrate catabolic process

Inferred from direct assay PubMed 16527817. Source: RGD

nitric oxide catabolic process

Inferred from direct assay PubMed 19152507. Source: RGD

oxidation-reduction process

Inferred from direct assay PubMed 19171935. Source: BHF-UCL

positive regulation of cholesterol biosynthetic process

Inferred from mutant phenotype PubMed 19264869. Source: RGD

positive regulation of chondrocyte differentiation

Inferred from mutant phenotype PubMed 19264869. Source: RGD

positive regulation of monooxygenase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of smoothened signaling pathway

Inferred from mutant phenotype PubMed 19264869. Source: RGD

positive regulation of steroid hormone biosynthetic process

Inferred from direct assay PubMed 2495435. Source: RGD

regulation of cholesterol metabolic process

Inferred from mutant phenotype PubMed 19264869. Source: RGD

regulation of growth plate cartilage chondrocyte proliferation

Inferred from mutant phenotype PubMed 19264869. Source: RGD

response to drug

Inferred from expression pattern PubMed 19265259. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 17392395. Source: RGD

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 9774150. Source: RGD

membrane

Inferred from direct assay PubMed 19152507. Source: RGD

mitochondrion

Inferred from direct assay PubMed 9774150. Source: RGD

   Molecular_functionFMN binding

Inferred from mutant phenotype PubMed 16928691. Source: RGD

NADP binding

Inferred from direct assay PubMed 9774150. Source: RGD

NADPH-hemoprotein reductase activity

Inferred from direct assay PubMed 19171935. Source: BHF-UCL

cytochrome-b5 reductase activity, acting on NAD(P)H

Inferred from direct assay PubMed 16055078. Source: RGD

electron carrier activity

Inferred from direct assay PubMed 19171935. Source: RGD

enzyme binding

Inferred from physical interaction PubMed 15516695PubMed 15680923. Source: BHF-UCL

flavin adenine dinucleotide binding

Inferred from mutant phenotype PubMed 16928691. Source: RGD

hydrolase activity

Inferred from direct assay PubMed 16226717. Source: RGD

iron ion binding

Inferred from electronic annotation. Source: InterPro

iron-cytochrome-c reductase activity

Inferred from direct assay PubMed 15823091. Source: RGD

nitric oxide dioxygenase activity

Inferred from direct assay PubMed 19152507. Source: RGD

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

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 678677NADPH--cytochrome P450 reductase
PRO_0000167600

Regions

Domain80 – 224145Flavodoxin-like
Domain279 – 521243FAD-binding FR-type
Nucleotide binding170 – 20132FMN By similarity
Nucleotide binding314 – 32512FAD By similarity
Nucleotide binding451 – 46111FAD By similarity
Nucleotide binding530 – 54819NADP By similarity
Nucleotide binding625 – 64117NADP By similarity

Amino acid modifications

Modified residue21N-acetylglycine By similarity

Experimental info

Sequence conflict2551V → A in AAA41683. Ref.3

Secondary structure

.................................................................................................................... 678
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00388 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AF3087E4D7A352D6

FASTA67876,963
        10         20         30         40         50         60 
MGDSHEDTSA TMPEAVAEEV SLFSTTDMVL FSLIVGVLTY WFIFRKKKEE IPEFSKIQTT 

        70         80         90        100        110        120 
APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA 

       130        140        150        160        170        180 
DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH 

       190        200        210        220        230        240 
FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES 

       250        260        270        280        290        300 
SIRQYELVVH EDMDVAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTANR KLNQGTERHL 

       310        320        330        340        350        360 
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQIGEILGA DLDVIMSLNN LDEESNKKHP 

       370        380        390        400        410        420 
FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV 

       430        440        450        460        470        480 
VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA 

       490        500        510        520        530        540 
KSGRVNKGVA TSWLRAKEPA GENGGRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGIAPF 

       550        560        570        580        590        600 
MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA 

       610        620        630        640        650        660 
HKVYVQHLLK RDREHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV 

       670 
DYVKKLMTKG RYSLDVWS 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10068 mRNA. Translation: AAA41064.1.
M12516 mRNA. Translation: AAA41067.1.
M58937 expand/collapse EMBL AC list , M58932, M58933, M58934, M58935, M58936 Genomic DNA. Translation: AAA41683.1.
PIRRDRTO4. A36073.
RefSeqNP_113764.1. NM_031576.1.
UniGeneRn.11359.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP00388.
SMRP00388. Positions 63-678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248088. 1 interaction.
MINTMINT-4564101.
STRING10116.ENSRNOP00000001961.

Chemistry

ChEMBLCHEMBL2817.

Proteomic databases

PaxDbP00388.
PRIDEP00388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001961; ENSRNOP00000001961; ENSRNOG00000001442.
GeneID29441.
KEGGrno:29441.
UCSCRGD:68335. rat.

Organism-specific databases

CTD5447.
RGD68335. Por.

Phylogenomic databases

eggNOGCOG0369.
GeneTreeENSGT00620000087711.
HOGENOMHOG000282027.
HOVERGENHBG000432.
InParanoidP00388.
KOK00327.
OMAKITGRHS.
OrthoDBEOG7HQN7J.
PhylomeDBP00388.
TreeFamTF105719.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14290.
SABIO-RKP00388.

Gene expression databases

GenevestigatorP00388.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000208. P450R. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00388.
NextBio609193.
PROP00388.

Entry information

Entry nameNCPR_RAT
AccessionPrimary (citable) accession number: P00388
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references