[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3919392 [NCBI, ExPASy, EBI, Israel, Japan] Porter T.D., Kasper C.B.; "Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains."; Proc. Natl. Acad. Sci. U.S.A. 82:973-977(1985).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3082610 [NCBI, ExPASy, EBI, Israel, Japan] Murakami H., Yabusaki Y., Ohkawa H.; "Expression of rat NADPH-cytochrome P-450 reductase cDNA in Saccharomyces cerevisiae."; DNA 5:1-10(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Wistar; TISSUE=Liver; DOI=10.1021/bi00494a009; PubMed=2125483 [NCBI, ExPASy, EBI, Israel, Japan] Porter T.D., Beck T.W., Kasper C.B.; "NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein."; Biochemistry 29:9814-9818(1990).
[4]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1073/pnas.94.16.8411; PubMed=9237990 [NCBI, ExPASy, EBI, Israel, Japan] Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S., Kim J.-J.P.; "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes."; Proc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997).
[5]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS. DOI=10.1074/jbc.M101731200; PubMed=11371558 [NCBI, ExPASy, EBI, Israel, Japan] Hubbard P.A., Shen A.L., Paschke R., Kasper C.B., Kim J.-J.P.; "NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer."; J. Biol. Chem. 276:29163-29170(2001).

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

M10068; AAA41064.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12516; AAA41067.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58937; AAA41683.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58932; AAA41683.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58933; AAA41683.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58934; AAA41683.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58935; AAA41683.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58936; AAA41683.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A36073; RDRTO4.

NP_113764.1; -.

3D structure databases

PDB

1AMO; X-ray; 2.60 A; A/B=64-678.	[ExPASy / RCSB / EBI]
1J9Z; X-ray; 2.70 A; A/B=57-678.	[ExPASy / RCSB / EBI]
1JA0; X-ray; 2.60 A; A/B=57-676.	[ExPASy / RCSB / EBI]
1JA1; X-ray; 1.80 A; A/B=57-678.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AMO; -.
1J9Z; -.
1JA0; -.
1JA1; -.

ModBase

P00388.

Organism-specific databases

RGD

68335; Por.

Gene expression databases

ArrayExpress

P00388; -.

GermOnline

ENSRNOG00000001442; Rattus norvegicus.

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:0019899;	Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
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

P00388.

Genome annotation databases

Ensembl

ENSRNOG00000001442; Rattus norvegicus. [Contig view]

GeneID

29441; -.

KEGG

rno:29441; -.

NMPDR

fig|10116.3.peg.8387; -.

Phylogenomic databases

HOVERGEN

P00388; -.

Other

LinkHub

P00388; -.

NextBio

609193; -.

UniRef

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

Keywords

3D-structure; 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_0000167600`
`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).`
`CONFLICT`	`255 255`		`V -> A (in Ref. 3; AAA41683).`
`HELIX`	`69 76`	`8`
`STRAND`	`80 85`	`6`
`STRAND`	`87 89`	`3`
`HELIX`	`90 101`	`12`
`HELIX`	`102 105`	`4`
`STRAND`	`109 112`	`4`
`HELIX`	`114 116`	`3`
`HELIX`	`119 127`	`9`
`STRAND`	`132 140`	`9`
`TURN`	`141 143`	`3`
`HELIX`	`147 149`	`3`
`HELIX`	`150 158`	`9`
`STRAND`	`167 174`	`8`
`STRAND`	`176 180`	`5`
`HELIX`	`183 194`	`12`
`STRAND`	`198 201`	`4`
`STRAND`	`204 207`	`4`
`TURN`	`208 210`	`3`
`HELIX`	`212 231`	`20`
`STRAND`	`244 249`	`6`
`HELIX`	`255 257`	`3`
`STRAND`	`258 261`	`4`
`STRAND`	`263 265`	`3`
`TURN`	`266 270`	`5`
`STRAND`	`282 291`	`10`
`STRAND`	`294 298`	`5`
`STRAND`	`300 306`	`7`
`STRAND`	`319 322`	`4`
`HELIX`	`328 337`	`10`
`STRAND`	`345 351`	`7`
`STRAND`	`360 366`	`7`
`HELIX`	`367 373`	`7`
`HELIX`	`383 389`	`7`
`HELIX`	`390 392`	`3`
`HELIX`	`396 403`	`8`
`HELIX`	`404 406`	`3`
`STRAND`	`408 410`	`3`
`HELIX`	`411 419`	`9`
`TURN`	`420 424`	`5`
`HELIX`	`427 433`	`7`
`HELIX`	`441 447`	`7`
`STRAND`	`454 457`	`4`
`TURN`	`462 464`	`3`
`STRAND`	`468 474`	`7`
`STRAND`	`477 479`	`3`
`STRAND`	`483 487`	`5`
`HELIX`	`489 496`	`8`
`STRAND`	`508 514`	`7`
`STRAND`	`528 531`	`4`
`HELIX`	`534 537`	`4`
`HELIX`	`538 552`	`15`
`STRAND`	`560 567`	`8`
`TURN`	`569 571`	`3`
`HELIX`	`576 584`	`9`
`STRAND`	`587 595`	`9`
`STRAND`	`598 601`	`4`
`HELIX`	`605 611`	`7`
`HELIX`	`613 621`	`9`
`STRAND`	`626 632`	`7`
`TURN`	`633 635`	`3`
`HELIX`	`636 651`	`16`
`HELIX`	`656 668`	`13`
`STRAND`	`671 677`	`7`

Sequence information

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

Molecular weight: 76963 Da [This is the MW of the unprocessed precursor]

CRC64: AF3087E4D7A352D6 [This is a checksum on the sequence]

        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

P00388 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