NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Rutgers;
TISSUE=Abdomen;
DOI=10.1016/0965-1748(93)90051-S; PubMed=8508186 [NCBI, ExPASy, EBI, Israel, Japan]
Koener J.F., Carino F.A., Feyereisen R.;
"The cDNA and deduced protein sequence of house fly NADPH-cytochrome P450 reductase.";
Insect Biochem. Mol. Biol. 23:439-447(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.
DEVELOPMENTAL STAGE: Expressed throughout development, with high levels before metamorphosis and low levels in pupae.
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

L19897; AAA29295.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A56592; A56592.

3D structure databases

HSSP

P00388; 1AMO. [HSSP ENTRY / PDB]

ModBase

Q07994.

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

Q07994.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 671`	`671`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167603`
`DOMAIN`	`77 221`	`145`	`Flavodoxin-like.`
`DOMAIN`	`276 515`	`240`	`FAD-binding FR-type.`
`NP_BIND`	`167 198`	`32`	`FMN (By similarity).`
`NP_BIND`	`311 322`	`12`	`FAD (By similarity).`
`NP_BIND`	`448 458`	`11`	`FAD (By similarity).`
`NP_BIND`	`524 542`	`19`	`NADP (By similarity).`
`NP_BIND`	`618 634`	`17`	`NADP (By similarity).`

Sequence information

Length: 671 AA [This is the length of the unprocessed precursor]

Molecular weight: 76358 Da [This is the MW of the unprocessed precursor]

CRC64: A00A2C35DFD8D129 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAEHVEEVV SEEPFLGTLD IALLVVLLVG ATWYFMRSRK KEEAPIRSYS IQPTTVSTVS 

        70         80         90        100        110        120 
TTENSFIKKL KASGRSLVVF YGSQTGTAEE FAGRLAKEGL RYRMKGMVAD PEECDMEELL 

       130        140        150        160        170        180 
QMKDIPNSLA VFCLATYGEG DPTDNAMEFY EWITNGEVDL TGLNYAVFGL GNKTYEHYNK 

       190        200        210        220        230        240 
VAIYVDKRLE ELGATRVFEL GLGDDDANIE DDFITWKDRF WPSVCDFFGI EGSGEEVLMR 

       250        260        270        280        290        300 
QFRLLEQPDV QPDRIYTGEI ARLHSMQNQR PPFDAKNPFL ASVIVNRELH KGGGRSCMHI 

       310        320        330        340        350        360 
ELDIDGSKMR YDAGDHIAMY PINDKILVEK LGKLCDANLD TVFSLINTDT DSSKKHPFPC 

       370        380        390        400        410        420 
PTTYRTALTH YLEITAIPRT HILKELAEYC SDEKDKEFLR NMASITPEGK EKYQNWIQNS 

       430        440        450        460        470        480 
SRNIVHILED IKSCRPPIDH ICELLPRLQP RYYSISSSSK LYPTNVHITA VLVQYETPTG 

       490        500        510        520        530        540 
RVNKGVATSY MKEKNPSVGE VKVPVFIRKS QFRLPTKSEI PIIMVGPGTG LAPFRGFIQE 

       550        560        570        580        590        600 
RQFLRDGGKV VGDTILYFGC RKKDEDFIYR EELEQYVQNG TLTLKTAFSR DQQEKIYVTH 

       610        620        630        640        650        660 
LIEQDADLIW KVIGEQKGHF YICGDAKNMA VDVRNILVKI LSTKGNMNES DAVQYIKKME 

       670 
AQKRYSADVW S

Q07994 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