[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=3029050 [NCBI, ExPASy, EBI, Israel, Japan] Katagiri M., Murakami H., Yabusaki Y., Sugiyama T., Okamoto M., Yamano T., Ohkawa H.; "Molecular cloning and sequence analysis of full-length cDNA for rabbit liver NADPH-cytochrome P-450 reductase mRNA."; J. Biochem. 100:945-954(1986).
[2]	PARTIAL PROTEIN SEQUENCE OF 1-81. TISSUE=Liver; PubMed=6802823 [NCBI, ExPASy, EBI, Israel, Japan] Black S.D., Coon M.J.; "Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region."; J. Biol. Chem. 257:5929-5938(1982).

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

D00101; BAA00063.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04610; CAA28279.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25505; A25505.

3D structure databases

HSSP

P16435; 1B1C. [HSSP ENTRY / PDB]

SMR

P00389; 65-679.

ModBase

P00389.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
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).

BLOCKS

P00389.

Phylogenomic databases

HOVERGEN

P00389; -.

Other

ProtoNet

P00389.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 679`	`679`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167599`
`DOMAIN`	`81 225`	`145`	`Flavodoxin-like.`
`DOMAIN`	`280 522`	`243`	`FAD-binding FR-type.`
`NP_BIND`	`171 202`	`32`	`FMN (By similarity).`
`NP_BIND`	`315 326`	`12`	`FAD (By similarity).`
`NP_BIND`	`452 462`	`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-acetylalanine.`
`MOD_RES`	`576 576`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`40 41`		`YW -> NY (in Ref. 2; AA sequence).`
`CONFLICT`	`53 53`		`E -> N (in Ref. 2; AA sequence).`

Sequence information

Length: 679 AA [This is the length of the unprocessed precursor]

Molecular weight: 76588 Da [This is the MW of the unprocessed precursor]

CRC64: B1A163FA53A5988B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADSHGDTGA TMPEAAAQEA SVFSMTDVVL FSLIVGLITY WFLFRKKKEE VPEFTKIQAP 

        70         80         90        100        110        120 
TSSSVKESSF VEKMKKTGRN IVVFYGSQTG TAEEFANRLS KDAHRYGMRG MAADPEEYDL 

       130        140        150        160        170        180 
ADLSSLPEIN NALAVFCMAT YGEGDPTDNA QDFYDWLQET DVDLSGVKYA VFGLGNKTYE 

       190        200        210        220        230        240 
HFNAMGKYVD QRLEQLGAQR IFELGMGDDD ANLEEDFITW REQFWPAVCE HFGVEATGEE 

       250        260        270        280        290        300 
SSIRQYELVL HTDIDVAKVY QGEMGRLKSY ENQKPPFDAK NPFLATVTTN RKLNQGTERH 

       310        320        330        340        350        360 
LMHLELDISD SKIRYESGDH VAVYPANDSA LVNQLGEILG ADLDVVMSLN NLDEESNKKH 

       370        380        390        400        410        420 
PFPCPTSYRT ALTYYLDITN PPRTNVLYEL AQYAADPAEQ EQLRKMASSS GEGKELYLSW 

       430        440        450        460        470        480 
VVEARRHILA ILQDYPSLRP PIDHLCELLP RLQARYYSIA SSSKVHPNSV HICAVAVEYE 

       490        500        510        520        530        540 
TKAGRLNKGV ATSWLRAKEP AGENGGRALV PMFVRKSQFR LPFKATTPVI MVGPGTGVAP 

       550        560        570        580        590        600 
FIGFIQERAW LRQQGKEVGE TLLYYGCRRA AEDYLYREEL AGFQKDGTLS QLNVAFSREQ 

       610        620        630        640        650        660 
AQKVYVQHLL RRDKEHLWRL IHEGGAHIYV CGDARNMARD VQNTFYDIVA ELGAMEHAQA 

       670 
VDYVKKLMTK GRYSLDVWS

P00389 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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