[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; Lattard V., Benoit E.; "Cloning, sequencing of flavin-containing monooxygenase 5 (FMO5) in the rat."; Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; 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).
[3]	METHYLATION AT ARG-5, AND MASS SPECTROMETRY. DOI=10.1091/mbc.E04-02-0101; PubMed=15047867 [NCBI, ExPASy, EBI, Israel, Japan] Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S., Yates J.R. III, Howell K.E.; "Organellar proteomics reveals Golgi arginine dimethylation."; Mol. Biol. Cell 15:2907-2919(2004).

Comments

FUNCTION: In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme (By similarity).
CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
COFACTOR: FAD.
SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane.
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

AF458413; AAM46761.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070883; AAH70883.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_653340.1; -.

UniGene

Rn.7038

3D structure databases

ModBase

Q8K4C0.

PTM databases

PhosphoSite

Q8K4C0; -.

Organism-specific databases

RGD

628602; Fmo5.

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.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002257; Flavin_mOase_5.
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.
PR01125; FMOXYGENASE5.

ProDom

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

Proteomics databases

PRIDE

Q8K4C0; -.

Genome annotation databases

Ensembl

ENSRNOG00000018076; Rattus norvegicus. [Contig view]

GeneID

246248; -.

KEGG

rno:246248; -.

Phylogenomic databases

HOVERGEN

Q8K4C0; -.

Other

623578; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 533`	`532`	`Dimethylaniline monooxygenase [N-oxide-forming] 5.`	`PRO_0000147668`
`NP_BIND`	`10 15`	`6`	`FAD (Potential).`
`NP_BIND`	`192 197`	`6`	`NADP (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`5 5`		`Omega-N-methylated arginine.`
`CONFLICT`	`34 34`		`R -> M (in Ref. 2; AAH70883).`
`CONFLICT`	`50 50`		`K -> E (in Ref. 2; AAH70883).`
`CONFLICT`	`136 136`		`Q -> E (in Ref. 2; AAH70883).`
`CONFLICT`	`228 228`		`R -> H (in Ref. 2; AAH70883).`

Sequence information

Length: 533 AA [This is the length of the unprocessed precursor]

Molecular weight: 60056 Da [This is the MW of the unprocessed precursor]

CRC64: A16A10779E91A8F8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKRIAVIG SGASGLTCIK CCLEEGLEPV CFERSDDIGG LWRYQENPEK GRASIYKSVI 

        70         80         90        100        110        120 
INTSKEMMCF SDYPIPDHYP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKQPDF 

       130        140        150        160        170        180 
STSGQWQVVT EHEGKQQVDV FDGVLVCTGH HTDPHLPLDS FPGIEKFKGK YFHSREYKNP 

       190        200        210        220        230        240 
VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKRGY PIDILLSSRI 

       250        260        270        280        290        300 
TNYLSKICGS ALKNRYMEKQ LNQRFDHEMF GLKPKHSALG QHPTINDDLP NRIISGLVKV 

       310        320        330        340        350        360 
KGNVKEFTET AAIFEDGSRE DDIDVVIFAT GYSFAFPFLE DSVKVVQNKV SLYKKVFPPN 

       370        380        390        400        410        420 
LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KTREEMAKRY 

       430        440        450        460        470        480 
VDSQRHTIQG DYIDTMEEIA DLVGVRPNLL SLAFTDPKLA FQLLVGPCTP VQYRLQGPGK 

       490        500        510        520        530 
WAGARKTILT TEDRIRKPLM TRVVERDSSG TSLVTVRVLM LAVTFLAVIL AYF

Q8K4C0 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