[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Hartley; DOI=10.1016/0167-4781(92)90147-R; PubMed=1420354 [NCBI, ExPASy, EBI, Israel, Japan] Ohgiya S., Goda T., Ishizaki K., Kamataki T., Shinriki N.; "Molecular cloning and sequence analysis of guinea-pig NADPH-cytochrome P-450 oxidoreductase."; Biochim. Biophys. Acta 1171:103-105(1992).
[2]	ERRATUM. PubMed=8373812 [NCBI, ExPASy, EBI, Israel, Japan] Ohgiya S., Goda T., Ishizaki K., Kamataki T., Shinriki N.; Biochim. Biophys. Acta 1174:313-313(1993).

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.
CAUTION: Was originally (Ref.1) thought to originate from mouse.

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

D10498; BAA01385.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S27158; S27158.

3D structure databases

HSSP

P00388; 1AMO. [HSSP ENTRY / PDB]

SMR

P37039; 64-678.

ModBase

P37039.

Ontologies

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

P37039.

Phylogenomic databases

HOVERGEN

P37039; -.

Other

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_0000167595`
`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 (By similarity).`

Sequence information

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

Molecular weight: 76782 Da [This is the MW of the unprocessed precursor]

CRC64: 4AC01B1825F0946F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDSHVDTGA TSTEAVAEEV SLFSMTDMIL LSVLVGFLTY FFLFRKKKEE IPEFTKISTT 

        70         80         90        100        110        120 
TSSVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM AADPEEYDLA 

       130        140        150        160        170        180 
DLSSLPEIDN SLAVFCMATY GEGDPTDNAQ DFYDWLQETD LDLSGVKYAV FGLGNKTYEH 

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

       250        260        270        280        290        300 
SIRQYELVLH ADTDPAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL 

       310        320        330        340        350        360 
MHLELDISDS KIRYESGDHV AVYPANDSNL VNQLGKILGA DLDVVMSLKN LDEESNKKHP 

       370        380        390        400        410        420 
FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE QLHKMASSSG EGKELYLTWV 

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

       490        500        510        520        530        540 
KSGRINKGVA TSWLQAKDPA GENGRRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGVAPF 

       550        560        570        580        590        600 
IGFIQERAWL QQQGKEVGET LLYYGCRRSD EDYLYREELA QFHKDGTLTQ LNVAFSREQA 

       610        620        630        640        650        660 
QKVYVQHLLK RDQEHLWKLI HEDGAHIYVC GDARNMARDV QNTFCNIAAE LGGMEHTQAV 

       670 
DYVKKLMTKG RYSLDVWS

P37039 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