[1]	NUCLEOTIDE SEQUENCE [MRNA]. 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]	PROTEIN SEQUENCE OF 2-535. TISSUE=Liver; PubMed=2355001 [NCBI, ExPASy, EBI, Israel, Japan] Ozols J.; "Covalent structure of liver microsomal flavin-containing monooxygenase form 1."; J. Biol. Chem. 265:10289-10299(1990).
[3]	PROTEIN SEQUENCE OF 4-33 AND 224-247. TISSUE=Liver; DOI=10.1016/0006-291X(89)92097-4; PubMed=2505769 [NCBI, ExPASy, EBI, Israel, Japan] Ozols J.; "Liver microsomes contain two distinct NADPH-Monooxygenases with NH2-terminal segments homologous to the flavin containing NADPH-monooxygenase of Pseudomonas fluorescens."; Biochem. Biophys. Res. Commun. 163:49-55(1989).

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.
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

M32030; AAA31278.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35182; A35182.
A35427; A35427.

RefSeq

NP_001075754.1; -.

UniGene

Ocu.1887

3D structure databases

ModBase

P17636.

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]

BLOCKS

P17636.

Genome annotation databases

GeneID

100009120; -.

Phylogenomic databases

HOVERGEN

P17636; -.

Other

ProtoNet

P17636.

UniRef

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

Keywords

Acetylation; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; 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] 1.`	`PRO_0000147642`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`SITE`	`208 208`	`1`	`Important for substrate binding (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`CONFLICT`	`20 20`		`C -> S (in Ref. 2 and 3).`
`CONFLICT`	`27 27`		`E -> K (in Ref. 2 and 3).`
`CONFLICT`	`99 99`		`S -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`103 103`		`S -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`116 116`		`C -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`126 126`		`E -> K (in Ref. 2; AA sequence).`
`CONFLICT`	`279 279`		`L -> M (in Ref. 2; AA sequence).`
`CONFLICT`	`340 340`		`F -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`406 406`		`S -> C (in Ref. 2; AA sequence).`
`CONFLICT`	`455 455`		`L -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`457 457`		`L -> G (in Ref. 2; AA sequence).`
`CONFLICT`	`535 535`		`L -> LES (in Ref. 2; AA sequence).`

Sequence information

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

Molecular weight: 60183 Da [This is the MW of the unprocessed precursor]

CRC64: 8EE95683FC3E43D5 [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 
NSCKEMSCYS DFPFPEDYPN YVPNSQFLDY LKMYADRFSL LKSIQFKTTV FSITKCQDFN 

       130        140        150        160        170        180 
VSGQWEVVTL HEGKQESAIF DAVMVCTGFL TNPHLPLGCF PGIKTFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
IFKDKRVLVV GMGNSGTDIA VEASHVAKKV FLSTTGGAWV ISRVFDSGYP WDMVFTTRFQ 

       250        260        270        280        290        300 
NFIRNSLPTP IVTWLVAKKM NSWFNHANYG LVPKDRIQLK EPVLNDELPG RIITGKVFIR 

       310        320        330        340        350        360 
PSIKEVKENS VVFGNAHNTP SEEPIDVIVF ATGYTFAFPF LDESVVKVED GQASLYKYIF 

       370        380        390        400        410        420 
PAHLQKPTLA VIGLIKPLGS MLPTGETQAR YTVQVFKGVI KLPPTSVMIK EVNERKENKH 

       430        440        450        460        470        480 
NGFGLCYCKA LQADYITYID DLLTSINAKP NLFSLLLTDP LLALTMFFGP YSPYQFRLTG 

       490        500        510        520        530 
PGKWKGARNA IMTQWDRTFK VTKTRIVQES SSPFESLLKL FAVLALLVSV FLIFL

P17636 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