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P37040 (NCPR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarnitine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular organofluorine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to follicle-stimulating hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

demethylation

Inferred from electronic annotation. Source: Ensembl

fatty acid oxidation

Inferred from electronic annotation. Source: Ensembl

flavonoid metabolic process

Inferred from electronic annotation. Source: Ensembl

internal peptidyl-lysine acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipase activity

Inferred from electronic annotation. Source: Ensembl

nitrate catabolic process

Inferred from electronic annotation. Source: Ensembl

nitric oxide catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of monooxygenase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of steroid hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of growth plate cartilage chondrocyte proliferation

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: Ensembl

NADP binding

Inferred from electronic annotation. Source: Ensembl

NADPH-hemoprotein reductase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

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

Inferred from electronic annotation. Source: Ensembl

electron carrier activity

Inferred from electronic annotation. Source: Ensembl

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: Ensembl

hydrolase activity

Inferred from electronic annotation. Source: Ensembl

iron ion binding

Inferred from electronic annotation. Source: InterPro

iron-cytochrome-c reductase activity

Inferred from electronic annotation. Source: Ensembl

nitric oxide dioxygenase activity

Inferred from electronic annotation. Source: Ensembl

oxidoreductase activity

Inferred from mutant phenotype PubMed 11742006. Source: MGI

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_0000167597

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

Sequences

Sequence LengthMass (Da)Tools
P37040 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 060282A7A55483AF

FASTA67877,044
        10         20         30         40         50         60 
MGDSHEDTSA TVPEAVAEEV SLFSTTDIVL FSLIVGVLTY WFIFKKKKEE 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 EDMDTAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL 

       310        320        330        340        350        360 
MHLELDISDS KIRYESGDHV AVYPANDSTL 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 TSWLRTKEPA GENGRRALVP MFVRKSQFRL PFKPTTPVIM VGPGTGVAPF 

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

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

       670 
DYVKKLMTKG RYSLDVWS 

« Hide

References

« Hide 'large scale' references
[1]"Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and functional expression in yeast."
Ohgiya S., Ishizaki K., Kamataki T., Shinriki N.
Biochim. Biophys. Acta 1186:137-141(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ddY.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17571 mRNA. Translation: BAA04496.1.
BC031463 mRNA. Translation: AAH31463.1.
RefSeqNP_032924.1. NM_008898.1.
XP_006504461.1. XM_006504398.1.
XP_006504462.1. XM_006504399.1.
UniGeneMm.3863.

3D structure databases

ProteinModelPortalP37040.
SMRP37040. Positions 63-678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202299. 1 interaction.
IntActP37040. 6 interactions.
MINTMINT-1863828.
STRING10090.ENSMUSP00000005651.

PTM databases

PhosphoSiteP37040.

2D gel databases

SWISS-2DPAGEP37040.

Proteomic databases

PaxDbP37040.
PRIDEP37040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005651; ENSMUSP00000005651; ENSMUSG00000005514.
GeneID18984.
KEGGmmu:18984.
UCSCuc008zyt.1. mouse.

Organism-specific databases

CTD5447.
MGIMGI:97744. Por.

Phylogenomic databases

eggNOGCOG0369.
GeneTreeENSGT00620000087711.
HOGENOMHOG000282027.
HOVERGENHBG000432.
InParanoidP37040.
KOK00327.
OMAYLPHITD.
OrthoDBEOG7HQN7J.
PhylomeDBP37040.
TreeFamTF105719.

Gene expression databases

ArrayExpressP37040.
BgeeP37040.
CleanExMM_POR.
GenevestigatorP37040.

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

ChiTaRSPOR. mouse.
NextBio295354.
PROP37040.
SOURCESearch...

Entry information

Entry nameNCPR_MOUSE
AccessionPrimary (citable) accession number: P37040
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 123 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot