Reviewed, UniProtKB/Swiss-Prot Q9EQ76 (FMO3_RAT)

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 3
    EC=1.14.13.8
Alternative name(s):
    Hepatic flavin-containing monooxygenase 3
      Short name=FMO 3
    Dimethylaniline oxidase 3

Gene names

Name:

Fmo3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Acts on TMA to produce TMA-N-oxide. Has activities of methimazole S-oxidation and NADPH oxidation associated with the N- or S-oxidation of trimethylamine and thioacetamide.
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.
Tissue specificity	Expressed in kidney and liver. Weakly expressed in lung. Does not seem to be expressed in brain, adipose tissue, or muscle. Ref.1
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	drug metabolic process Inferred from direct assay. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro microsome Ref.1 Inferred from direct assay. Source: RGD
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from physical interaction. Source: RGD amino acid binding Inferred from physical interaction. Source: RGD flavin-containing monooxygenase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Dimethylaniline monooxygenase [N-oxide-forming] 3		PRO_0000147659
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Amino acid modifications
	Modified residue	401	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	501	1	V → D in AAH87008. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9EQ76-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 35A89988323B311F	FASTA	531	59,960
	10 20 30 40 50 60 MKRKVAVIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHTEEG RASIYQSVFT 70 80 90 100 110 120 NSSKEMMCFP DFPYPDDFPN FMHNSKLQEY ITSFATEKNL LKYIQFETLV TRINKCPDFS 130 140 150 160 170 180 TTGKWEVTTE KNSKKETAVF DAVMICSGHH VYPHLPKDSF PGLNRFKGKC FHSRDYKEPG 190 200 210 220 230 240 TWKGKRVLVI GLGNSGCDIA AELSHVAQQV IISSRSGSWV MSRVWNDGYP WDMVVITRFQ 250 260 270 280 290 300 TFLKNNLPTA ISDWWYMKQM NARFKHENYG LMPLNGTLRK EPVFNDELPA RILCGTVSIK 310 320 330 340 350 360 PNVKEFTETS AVFEDGTVFE GIDCVIFATG YGYAYPFLDD SIIKSRNNEV TLYKGIFPPQ 370 380 390 400 410 420 LEKPTMAVIG LVQSLGAAIP TTDLQARWAA QVIRGTCILP SVNDMMDDID EKMGKKLKWF 430 440 450 460 470 480 GNSTTIQTDY IVYMDELASF IGAKPNILWL FLKDPRLAIE VFFGPCSPYQ FRLVGPGKWS 490 500 510 520 530 GARNAILTQW DRSLKPMKTR VVGGIQKPCL YSHFLRLLAV PVLIALFLVL I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, tissue distribution, and heterologous expression of rat flavin-containing monooxygenase 3." Lattard V., Buronfosse T., Lachuer J., Longin-Sauvageon C., Moulin C., Benoit E. Arch. Biochem. Biophys. 391:30-40(2001) [PubMed: 11414682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY. Strain: Sprague-Dawley.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF286595 mRNA. Translation: AAG44891.1. BC087008 mRNA. Translation: AAH87008.1.
IPI	IPI00565267.
RefSeq	NP_445885.2.
UniGene	Rn.163228
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000003620. Rattus norvegicus. [Contig view]
GeneID	84493.
KEGG	rno:84493.
Organism-specific databases
RGD	619761. Fmo3.
Phylogenomic databases
HOVERGEN	Q9EQ76.
Enzyme and pathway databases
BRENDA	1.14.13.8. 248.
Gene expression databases
ArrayExpress	Q9EQ76.
GermOnline	ENSRNOG00000003620. Rattus norvegicus.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR000960. Flavin_mOase. IPR002255. Flavin_mOase_3. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01123. FMOXYGENASE3.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	617057.

Entry information

Entry name

FMO3_RAT

Accession

Primary (citable) accession number: Q9EQ76
Secondary accession number(s): Q5PQV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)