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Reviewed, UniProtKB/Swiss-Prot P00388 (NCPR_RAT)

Last modified November 3, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

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

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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.

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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
Modified residue5751Phosphotyrosine By similarity

Experimental info

Sequence conflict2551V → A in AAA41683. Ref.3

Secondary structure

1 ................................................................................................................ 678
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00388-1 [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

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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: 3919392] [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: 3082610] [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: 2125483] [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: 9237990] [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: 11371558] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00231200.
PIRRDRTO4. A36073.
RefSeqNP_113764.1.
UniGeneRn.11359

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP00388.

Proteomic databases

PRIDEP00388.

Genome annotation databases

EnsemblENSRNOT00000001961; ENSRNOP00000001961; ENSRNOG00000001442; Rattus norvegicus. [Genome view]
GeneID29441.
KEGGrno:29441.
NMPDRfig|10116.3.peg.8387.
UCSCNM_031576. rat.

Organism-specific databases

CTD29441.
RGD68335. Por.

Phylogenomic databases

HOVERGENP00388.
OMAFHKDGAL.

Enzyme and pathway databases

BRENDA1.6.2.4. 248.

Gene expression databases

ArrayExpressP00388.
GenevestigatorP00388.
GermOnlineENSRNOG00000001442. Rattus norvegicus.

Family and domain databases

InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015702. NADPH_Cyt_P450_Rdtase.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PANTHERPTHR19384:SF17. NADPH_Cyt_Red. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio609193.

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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: November 3, 2009
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents