[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 137-151 AND 309-318. TISSUE=Liver; DOI=10.1021/bi00453a014; PubMed=2322534 [NCBI, ExPASy, EBI, Israel, Japan] Gasser R., Tynes R.E., Lawton M.P., Korsmeyer K.K., Ziegler D.M., Philpot R.M.; "The flavin-containing monooxygenase expressed in pig liver: primary sequence, distribution, and evidence for a single gene."; Biochemistry 29:119-124(1990).
[2]	PROTEIN SEQUENCE OF 2-14 AND 185-202, AND ACETYLATION AT ALA-2. TISSUE=Liver; DOI=10.1016/0006-291X(90)92181-X; PubMed=2383273 [NCBI, ExPASy, EBI, Israel, Japan] Guan S.H., Falick A.M., Cashman J.R.; "N-terminus determination: FAD and NADP binding domain mapping of hog liver flavin-containing monooxygenase by tandem mass spectrometry."; Biochem. Biophys. Res. Commun. 170:937-943(1990).
[3]	PROTEIN SEQUENCE OF 186-208. TISSUE=Liver; PubMed=7758472 [NCBI, ExPASy, EBI, Israel, Japan] Wu R.-F., Ichikawa Y.; "An essential lysyl residue (Lys208) in the substrate-binding site of porcine FAD-containing monooxygenase."; Eur. J. Biochem. 229:749-753(1995).
[4]	GLYCOSYLATION AT ASN-120. DOI=10.1021/tx980117p; PubMed=9778310 [NCBI, ExPASy, EBI, Israel, Japan] Korsmeyer K.K., Guan S., Yang Z.C., Falick A.M., Ziegler D.M., Cashman J.R.; "N-glycosylation of pig flavin-containing monooxygenase form 1: determination of the site of protein modification by mass spectrometry."; Chem. Res. Toxicol. 11:1145-1153(1998).

Comments

FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.
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

M32031; AAA31033.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A33768; A33768.

NP_999229.1; -.

3D structure databases

ModBase

P16549.

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: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

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

PR00370; FMOXYGENASE.
PR01121; FMOXYGENASE1.

ProDom

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

ProtoNet

P16549.

Genome annotation databases

GeneID

397132; -.

KEGG

ssc:397132; -.

Phylogenomic databases

HOVERGEN

P16549; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 532`	`531`	`Dimethylaniline monooxygenase [N-oxide-forming] 1.`	`PRO_0000147641`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`SITE`	`208 208`	`1`	`Important for substrate binding.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`CARBOHYD`	`120 120`		`N-linked (GlcNAc...) (high mannose).`

Sequence information

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

Molecular weight: 59952 Da [This is the MW of the unprocessed precursor]

CRC64: 5E475E7F2F3B8A67 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS 

        70         80         90        100        110        120 
NSCKEMSCYP DFPFPEDYPN YVPNSHFLEY LRMYANQFNL LKCIQFKTKV CSVTKHEDFN 

       130        140        150        160        170        180 
TTGQWDVVTL CEGKQESAVF DAVMVCTGFL TNPYLPLDSF PGINTFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
IFKDKSVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMVFMTRFQ 

       250        260        270        280        290        300 
NMFRNSLPTP IVNWLIAKKM NSWFNHANYG LIPEDRIQLR EPVLNDELPG RIITGKVLIK 

       310        320        330        340        350        360 
PSIKEVKENS VVFNSSPEEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH 

       370        380        390        400        410        420 
LQKPTLAVIG LIKPLGSLLP TGDTQARWAV RVLKGVNKLP PSSVMIQEVN TRKENKPSGF 

       430        440        450        460        470        480 
GLCYCKALQS DYIAYIDELL TYIDAKPNMF SLLLTDPHLA LTIFFGPCTP YQFRLTGPGK 

       490        500        510        520        530 
WEGARNAIMT QWDRTFKVTK TRIVKESPSP FASLLKLFSF LALLVAIFQI FL

P16549 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