[1]	NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. STRAIN=C57BL/6; TISSUE=Kidney; PubMed=11835629 [NCBI, ExPASy, EBI, Israel, Japan] Karoly E.D., Rose R.L.; "Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse."; J. Biochem. Mol. Toxicol. 15:300-308(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Czech II; TISSUE=Mammary tumor; 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. Shows catalytic activity towards methimazole, thiourea, trimethylamine, and the insecticide phorate.
CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
COFACTOR: Magnesium (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 10.5;
SUBCELLULAR LOCATION: Microsome membrane (By similarity). Endoplasmic reticulum membrane (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

AF184981; AAD56413.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031415; AAH31415.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_061369.2; -.

UniGene

Mm.10929

3D structure databases

ModBase

Q8K2I3.

Organism-specific databases

MGI

MGI:1916776; Fmo2.

Gene expression databases

ArrayExpress

Q8K2I3; -.

CleanEx

MM_FMO2; -.

GermOnline

ENSMUSG00000040170; Mus musculus.

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:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
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).
GO:0006800;	Biological process: oxygen and reactive oxygen species metabolic process (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002254; Flavin_mOase_2.
Graphical view of domain structure.

Pfam

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

PIRSF

PIRSF000332; FMO; 1.

PRINTS

PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01122; FMOXYGENASE2.

ProDom

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

ProtoNet

Q8K2I3.

Genome annotation databases

Ensembl

ENSMUSG00000040170; Mus musculus. [Contig view]

GeneID

55990; -.

KEGG

mmu:55990; -.

Phylogenomic databases

HOGENOM

Q8K2I3; -.

HOVERGEN

Q8K2I3; -.

Other

NextBio

311714; -.

SOURCE

Fmo2; Mus musculus.

UniRef

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

Keywords

Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Magnesium; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 535`	`534`	`Dimethylaniline monooxygenase [N-oxide-forming] 2.`	`PRO_0000147648`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`CONFLICT`	`169 169`		`Q -> R (in Ref. 1; AAD56413).`

Sequence information

Length: 535 AA [This is the length of the unprocessed precursor]

Molecular weight: 60974 Da [This is the MW of the unprocessed precursor]

CRC64: 705FAD9D8EADB1B1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKVVVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYRSVIT 

        70         80         90        100        110        120 
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA 

       130        140        150        160        170        180 
SSGQWEVYTQ SNGKEQRTVF DAVMVCSGHH IQPHLPLKSF PGIERFRGQY FHSREYKHPV 

       190        200        210        220        230        240 
GFEGKRILVV GIGNSAADIA SELSKTAAQV FVSTRHGSWV MSRISEDGYP WDMVFHTRFS 

       250        260        270        280        290        300 
SMLRNVLPRT VVKWMMEQQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK 

       310        320        330        340        350        360 
TRVKELTETA VVFEDGTVEE DVDIIVFATG YTFSFSFLED SLVKVEDNRV SLYKAMFPPH 

       370        380        390        400        410        420 
LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SETTMMADIV ERNEKRVNLF 

       430        440        450        460        470        480 
GKSQSQILQT NYVDYLDELA LEIGAKPDFV SLFFKDPKLA VKLYFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARNAILT QKQRILKPLK TRTLQSSDSA PVSFLLKILG LLAVVLAFFF QLQGF

Q8K2I3 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