NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Hartley;
TISSUE=Lung;
PubMed=1306120 [NCBI, ExPASy, EBI, Israel, Japan]
Nikbakht K.N., Lawton M.P., Philpot R.M.;
"Guinea pig or rabbit lung flavin-containing monooxygenases with distinct mobilities in SDS-PAGE are allelic variants that differ at only two positions.";
Pharmacogenetics 2:207-216(1992).

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 (By similarity).
COFACTOR: Magnesium (By similarity).
SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane.
TISSUE SPECIFICITY: Lung.
POLYMORPHISM: There are two allelic forms (A and B).
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

L10037; AAB59631.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P36366.

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).
QuickGo view.

Family and domain databases

InterPro

IPR012143; dManiline_mOase.
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

PR00370; FMOXYGENASE.
PR01122; FMOXYGENASE2.

ProDom

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

ProtoNet

P36366.

Phylogenomic databases

HOVERGEN

P36366; -.

Other

UniRef

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

Keywords

Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Magnesium; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; 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_0000147644`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`VARIANT`	`522 522`	`1`	`V -> L (in B form).`
`VARIANT`	`530 530`	`1`	`S -> F (in B form).`

Sequence information

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

Molecular weight: 60942 Da [This is the MW of the unprocessed precursor]

CRC64: 10D9DDA06EB58DA2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYKSVIT 

        70         80         90        100        110        120 
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRLFAKKFDL LKYIQFQTTV LTVKKHPDFS 

       130        140        150        160        170        180 
SSGQWEVVTQ SDGKEQSAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPA 

       190        200        210        220        230        240 
GFEGKRILVI GIGNSASDIA SELSKNAAQV FISTRNGSWV MSRISEDGYP WDMVFHTRFK 

       250        260        270        280        290        300 
SMLRNILPRT VSKWMMEQQL NRWFNHANYS LEPKNKYLMK EPILNDDLPS RILYGAVKVK 

       310        320        330        340        350        360 
SRVTQLTETS ALFEDGTVEE DIDVIVFATG YTFSFPFLEE SLVKIEHNMV SLYKYMFPPQ 

       370        380        390        400        410        420 
LEKPTLTCMG LIQPLGSIFP TVELQARWAT RVFKGLCHLP SEKTMMEDII KRNEKRIDLF 

       430        440        450        460        470        480 
GESQSQIVQT NYVDYLDELA LEIGAKPDLI SFLLKDPELA VKLCFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARRAILT QKQRILKPLK TRSVKAAPNL SASFLMKILA LVAVFVAFFS QLYGF

P36366 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