[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1016/0167-4781(93)90177-F; PubMed=8504165 [NCBI, ExPASy, EBI, Israel, Japan] Itoh K., Kimura T., Yokoi T., Itoh S., Kamataki T.; "Rat liver flavin-containing monooxygenase (FMO): cDNA cloning and expression in yeast."; Biochim. Biophys. Acta 1173:165-171(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pituitary; 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]	PROTEIN SEQUENCE OF 34-42 AND 52-56. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1016/S0092-8674(00)80191-9; PubMed=9094723 [NCBI, ExPASy, EBI, Israel, Japan] Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.; "Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells."; Cell 89:149-158(1997).

Comments

FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.
CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
COFACTOR: FAD.
SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane.
TISSUE SPECIFICITY: Liver.
SIMILARITY: Belongs to the FMO family.

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

M84719; AAA41165.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061567; AAH61567.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S33758; S33758.

NP_036924.1; -.

3D structure databases

ModBase

P36365.

Organism-specific databases

RGD

2622; Fmo1.

Gene expression databases

ArrayExpress

P36365; -.

GermOnline

ENSRNOG00000034191; Rattus norvegicus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031227;	Cellular component: intrinsic to endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004499;	Molecular function: flavin-containing monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR012143; dManiline_mOase.
IPR000960; Flavin_mOase.
IPR002253; Flavin_mOase_1.
Graphical view of domain structure.

Pfam

PF00743; FMO-like; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000332; FMO; 1.

PRINTS

PR00419; ADXRDTASE.
PR00370; FMOXYGENASE.
PR01121; FMOXYGENASE1.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

ProtoNet

P36365.

Genome annotation databases

Ensembl

ENSRNOG00000034191; Rattus norvegicus. [Contig view]

GeneID

25256; -.

KEGG

rno:25256; -.

Phylogenomic databases

HOVERGEN

P36365; -.

Other

NextBio

605891; -.

UniRef

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

Keywords

Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 532`	`532`	`Dimethylaniline monooxygenase [N-oxide-forming] 1.`	`PRO_0000147643`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`SITE`	`208 208`	`1`	`Important for substrate binding (By similarity).`
`CONFLICT`	`141 141`		`D -> A (in Ref. 1; AAA41165).`

Sequence information

Length: 532 AA [This is the length of the unprocessed precursor]

Molecular weight: 59825 Da [This is the MW of the unprocessed precursor]

CRC64: 188EABAF96653977 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSCDLGGL WRFTEHVEEG RASLYNSVVS 

        70         80         90        100        110        120 
NSSKEMSCYS DFPFPEDYPN FVPNSLFLEY LQLYATQFNL LRCIYFNTKV CSITKRPDFA 

       130        140        150        160        170        180 
VSGQWEVVTV CQGKQSSDTF DAVMVCTGFL TNPHLPLDSF PGIQTFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
VFKDKRVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMIFMTRFQ 

       250        260        270        280        290        300 
NMLRNLLPTP VVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVLIK 

       310        320        330        340        350        360 
PSIKEVKENS VVFNNTPKEE PIDVIVFATG YSFAFPFLDE SIVKVEDGQA SLYKYIFPAH 

       370        380        390        400        410        420 
LPKPTLAVIG LIKPLGSMIP TGETQARWVV QVLKGATTLP PPSVMMKEVN ERKKNKHSGF 

       430        440        450        460        470        480 
GLCYCKALQS DYITYIDDLL TSINAKPDLR AMLLTDPRLA LSIFFGPCTP YHFRLTGPGK 

       490        500        510        520        530 
WEGARKAILT QWDRTVNVTK TRTVQETPST FETLLKLFSF LALLVAVFFI FL

P36365 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