[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; Lattard V., Longin-Sauvageon C., Benoit E.; "Cloning, sequencing and tissue distribution of rat flavin-containing monooxygenase 4. Two different FMO4 are produced by tissue specific alternative splicing."; Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; 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 (By similarity).
CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
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

AF458416; AAM46764.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081721; AAH81721.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_653147.1; -.

UniGene

Rn.216582

3D structure databases

ModBase

Q8K4B7.

Organism-specific databases

RGD

628601; Fmo4.

Gene expression databases

ArrayExpress

Q8K4B7; -.

GermOnline

ENSRNOG00000003400; Rattus norvegicus.

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: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.
IPR002256; Flavin_mOase_4.
Graphical view of domain structure.

Pfam

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

PIRSF

PIRSF000332; FMO; 1.

PRINTS

PR00370; FMOXYGENASE.
PR01124; FMOXYGENASE4.

ProDom

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

ProtoNet

Q8K4B7.

Genome annotation databases

Ensembl

ENSRNOG00000003400; Rattus norvegicus. [Contig view]

GeneID

246247; -.

KEGG

rno:246247; -.

Phylogenomic databases

HOVERGEN

Q8K4B7; -.

Other

NextBio

623572; -.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 560`	`559`	`Dimethylaniline monooxygenase [N-oxide-forming] 4.`	`PRO_0000147663`
`TRANSMEM`	`516 530`	`15`	`Potential.`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`CONFLICT`	`244 244`		`Q -> R (in Ref. 1; AAM46764).`

Sequence information

Length: 560 AA [This is the length of the unprocessed precursor]

Molecular weight: 63660 Da [This is the MW of the unprocessed precursor]

CRC64: 9A7A77C41A328EFB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKVAVIGA GVSGLSSIKC CLDENLEPTC FERSSDFGGL WKFAEASEDG MTRVYRSLVT 

        70         80         90        100        110        120 
NVCKEMSCYS DFPFHEDYPN FMSHEKFWDY LREFAEHFGL LKYIRFKTTV RSVTKRPDFS 

       130        140        150        160        170        180 
ETGQWEVVTE TEGKQDRAVF DAVMVCTGQF LSPRLPLESF PGIHKFKGQI LHSQEYRIPD 

       190        200        210        220        230        240 
AFRGKRILVV GLGNTGGDVA VELSGIAAQV FLSTRTGAWV RSRSSVGGYP LNMMQTRWRN 

       250        260        270        280        290        300 
FLAQVLPSRF VSWNQERQMN KIFNHENYGL SIAKGKKPKF IVNDELPTCI LCGKITMKTS 

       310        320        330        340        350        360 
VKDFTESSIV FEDGTIEANI DVVIFTTGYE FSFPFFEEPL KSLCTKKVIL YKRVFPPNLE 

       370        380        390        400        410        420 
RSTLAIIGLI SLTGSILVGT EFQARWATRV FKGLCNIPPS QKLMAEAIKK EELIKRGVIK 

       430        440        450        460        470        480 
DTSQDKLDFI SYMDELTQCI GAKPNIPLLF LKDPRLAWEV FFGPCTPYQY RLMGPGRWDG 

       490        500        510        520        530        540 
ARNAILTQWD RTVKPLKTRT VPKSQEPASL SRYLKTWGAP VLIVSLLLIY KSSLFLELVQ 

       550        560 
SKLQGRFSPS RILWYIPQNS

Q8K4B7 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