[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=New Zealand white; PubMed=2318837 [NCBI, ExPASy, EBI, Israel, Japan] Lawton M.P., Gasser R., Tynes R.E., Hodgson E., Philpot R.M.; "The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes."; J. Biol. Chem. 265:5855-5861(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=New Zealand white; 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).
[3]	PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2. TISSUE=Lung; DOI=10.1021/bi00105a012; PubMed=1911780 [NCBI, ExPASy, EBI, Israel, Japan] Guan S., Falick A.M., Williams D.E., Cashman J.R.; "Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin."; Biochemistry 30:9892-9900(1991).

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 (By similarity).
TISSUE SPECIFICITY: Lung.
POLYMORPHISM: There are two allelic forms.
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

M32029; AAA31442.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

B35182; B35182.

NP_001075753.1; -.

3D structure databases

ModBase

P17635.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
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]

Genome annotation databases

Ensembl

ENSOCUG00000005177; Oryctolagus cuniculus. [Contig view]

GeneID

100009119; -.

Phylogenomic databases

HOVERGEN

P17635; -.

Other

UniRef

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

Keywords

Acetylation; Direct protein sequencing; 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.`
`CHAIN`	`2 535`	`534`	`Dimethylaniline monooxygenase [N-oxide-forming] 2.`	`PRO_0000147650`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`VARIANT`	`120 120`	`1`	`A -> S (in PFMO-2 and PFMO-4).`
`VARIANT`	`136 136`	`1`	`Q -> E (in PFMO-2 and PFMO-4).`

Sequence information

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

Molecular weight: 61144 Da [This is the MW of the unprocessed precursor]

CRC64: D51910BDA41C55C2 [This is a checksum on the sequence]

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

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

       130        140        150        160        170        180 
SSGQWEVVTQ SNSKQQSAVF DAVMVCSGHH ILPNIPLKSF PGIEKFKGQY FHSRQYKHPA 

       190        200        210        220        230        240 
GLEGKRILVI GIGNSASDIA VELSKKAAQV YISTRKGSWV MSRISEDGYP WDMVFHTRFS 

       250        260        270        280        290        300 
SMLRNVLPRM IVKWMMEQQM NRWFNHENYG LAPENKYLMK EPVLNDDLPS RILYGTIKVK 

       310        320        330        340        350        360 
RRVKELTESA AIFEDGTVEE DIDVIVFATG YTFAFPFLEE SLVKIEDNMV SLYKYMFPPQ 

       370        380        390        400        410        420 
LEKSTFACLG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SKETMMADII KRNENRIALF 

       430        440        450        460        470        480 
GESLSQKLQT NYIDYLDELA LEIGAKPDLV SFLFKDPKLA VKLYFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARNAIFT QKQRILKPLK TRTLKASSNF PVSFLLKFLG LFALVLAFLF QLQWF

P17635 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