[1]	NUCLEOTIDE SEQUENCE [MRNA]. Itoh K., Nakamura K., Kimura T., Itoh S., Kamataki T.; Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CD-1; TISSUE=Liver; PubMed=9580872 [NCBI, ExPASy, EBI, Israel, Japan] Cherrington N.J., Falls J.G., Rose R.L., Clements K.M., Philpot R.M., Levi P.E., Hodgson E.; "Molecular cloning, sequence, and expression of mouse flavin-containing monooxygenases 1 and 5 (FMO1 and FMO5)."; J. Biochem. Mol. Toxicol. 12:205-212(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Liver; 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).

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 (By similarity).
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

D16215; BAA03745.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U87456; AAB47569.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011229; AAH11229.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B61243; B61243.

NP_034361.1; -.

3D structure databases

ModBase

P50285.

PTM databases

PhosphoSite

P50285; -.

Organism-specific databases

MGI

MGI:1310002; Fmo1.

Gene expression databases

ArrayExpress

P50285; -.

CleanEx

MM_FMO1; -.

GermOnline

ENSMUSG00000040181; Mus musculus.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
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.
PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01121; FMOXYGENASE1.

ProDom

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

BLOCKS

P50285.

Genome annotation databases

Ensembl

ENSMUSG00000040181; Mus musculus. [Contig view]

GeneID

14261; -.

KEGG

mmu:14261; -.

Phylogenomic databases

HOGENOM

P50285; -.

HOVERGEN

P50285; -.

Other

Fmo1; Mus musculus.

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

Keywords

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_0000147640`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`SITE`	`208 208`	`1`	`Important for substrate binding (By similarity).`

Sequence information

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

Molecular weight: 59915 Da [This is the MW of the unprocessed precursor]

CRC64: C3CEDC7FC82DAC59 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSSDLGGL WRFTEHVEEG RASLYKSVVS 

        70         80         90        100        110        120 
NSSREMSCYP DFPFPEDYPN FVPNSLFLEY LKLYSTQFNL QRCIYFNTKV CSITKRPDFA 

       130        140        150        160        170        180 
VSGQWEVVTV TNGKQNSAIF DAVMVCTGFL TNPHLPLDSF PGILTFKGEY FHSRQYKHPD 

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

       250        260        270        280        290        300 
NMLRNLLPTP IVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVFIK 

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

       370        380        390        400        410        420 
LPKPTLAVIG LIKPLGSMVP TGETQARWVV QVLKGATTLP PPSVMMEEVN ERKKNKHSGF 

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

       490        500        510        520        530 
WEGARKAILT QWDRTVKVTK TRTIQESPSS FETLLKLFSF LALLIAVFLI FL

P50285 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