[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ddY; DOI=10.1016/0005-2728(94)90146-5; PubMed=8011664 [NCBI, ExPASy, EBI, Israel, Japan] Ohgiya S., Ishizaki K., Kamataki T., Shinriki N.; "Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and functional expression in yeast."; Biochim. Biophys. Acta 1186:137-141(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-575, AND MASS SPECTROMETRY. DOI=10.1021/pr070122r; PubMed=17622165 [NCBI, ExPASy, EBI, Israel, Japan] Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."; J. Proteome Res. 6:3174-3186(2007).

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.
COFACTOR: FMN.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Anchored to the ER membrane by its N-terminal hydrophobic region.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D17571; BAA04496.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031463; AAH31463.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_032924.1; -.

UniGene

Mm.3863

3D structure databases

HSSP

P00388; 1AMO. [HSSP ENTRY / PDB]

SMR

P37040; 63-678.

ModBase

P37040.

Protein-protein interaction databases

IntAct

P37040; -.

PTM databases

PhosphoSite

P37040; -.

2D gel databases

SWISS-2DPAGE

P37040; -.

Organism-specific databases

MGI

MGI:97744; Por.

Gene expression databases

CleanEx

MM_POR; -.

GermOnline

ENSMUSG00000005514; Mus musculus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from direct assay from MGI).
GO:0005625;	Cellular component: soluble fraction (inferred from direct assay from MGI).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0003958;	Molecular function: NADPH-hemoprotein reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

PANTHER

PTHR19384:SF17; NADPH_Cyt_Red; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P37040.

Genome annotation databases

Ensembl

ENSMUSG00000005514; Mus musculus. [Contig view]

GeneID

18984; -.

KEGG

mmu:18984; -.

Phylogenomic databases

HOGENOM

P37040; -.

HOVERGEN

P37040; -.

Other

NextBio

295354; -.

SOURCE

Por; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 678`	`677`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167597`
`DOMAIN`	`80 224`	`145`	`Flavodoxin-like.`
`DOMAIN`	`279 521`	`243`	`FAD-binding FR-type.`
`NP_BIND`	`170 201`	`32`	`FMN (By similarity).`
`NP_BIND`	`314 325`	`12`	`FAD (By similarity).`
`NP_BIND`	`451 461`	`11`	`FAD (By similarity).`
`NP_BIND`	`530 548`	`19`	`NADP (By similarity).`
`NP_BIND`	`625 641`	`17`	`NADP (By similarity).`
`MOD_RES`	`2 2`		`N-acetylglycine (By similarity).`
`MOD_RES`	`575 575`		`Phosphotyrosine.`

Sequence information

Length: 678 AA [This is the length of the unprocessed precursor]

Molecular weight: 77044 Da [This is the MW of the unprocessed precursor]

CRC64: 060282A7A55483AF [This is a checksum on the sequence]

        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

P37040 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools