Dimethylaniline monooxygenase [N-oxide-forming] 2

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Q8K2I3 (FMO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 2
EC=1.14.13.8

Alternative name(s):
Dimethylaniline oxidase 2
Pulmonary flavin-containing monooxygenase 2
Short name=FMO 2

Gene names

Name:

Fmo2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Shows catalytic activity towards methimazole, thiourea, trimethylamine, and the insecticide phorate.
Catalytic activity	N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
Cofactor	FAD By similarity. Magnesium By similarity.
Subcellular location	Microsome membrane By similarity. Endoplasmic reticulum membrane By similarity.
Sequence similarities	Belongs to the FMO family.
Biophysicochemical properties	pH dependence: Optimum pH is 10.5.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein Magnesium NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from sequence or structural similarity. Source: UniProtKB drug metabolic process Inferred from electronic annotation. Source: Compara organic acid metabolic process Inferred from electronic annotation. Source: Compara oxygen metabolic process Inferred from direct assay Ref.1. Source: MGI toxin metabolic process Inferred from electronic annotation. Source: Compara xenobiotic metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	N,N-dimethylaniline monooxygenase activity Inferred from electronic annotation. Source: EC NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 535

534

Dimethylaniline monooxygenase [N-oxide-forming] 2

PRO_0000147648

Regions

Nucleotide binding

9 – 14

FAD Potential

Nucleotide binding

191 – 196

NADP Potential

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Cross-link

492

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Experimental info

Sequence conflict

169

Q → R in AAD56413. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q8K2I3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 705FAD9D8EADB1B1
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FASTA

535

60,974

        10         20         30         40         50         60 
MAKKVVVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYRSVIT 

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

       130        140        150        160        170        180 
SSGQWEVYTQ SNGKEQRTVF DAVMVCSGHH IQPHLPLKSF PGIERFRGQY FHSREYKHPV 

       190        200        210        220        230        240 
GFEGKRILVV GIGNSAADIA SELSKTAAQV FVSTRHGSWV MSRISEDGYP WDMVFHTRFS 

       250        260        270        280        290        300 
SMLRNVLPRT VVKWMMEQQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK 

       310        320        330        340        350        360 
TRVKELTETA VVFEDGTVEE DVDIIVFATG YTFSFSFLED SLVKVEDNRV SLYKAMFPPH 

       370        380        390        400        410        420 
LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SETTMMADIV ERNEKRVNLF 

       430        440        450        460        470        480 
GKSQSQILQT NYVDYLDELA LEIGAKPDFV SLFFKDPKLA VKLYFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARNAILT QKQRILKPLK TRTLQSSDSA PVSFLLKILG LLAVVLAFFF QLQGF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse." Karoly E.D., Rose R.L. J. Biochem. Mol. Toxicol. 15:300-308(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Strain: C57BL/6. Tissue: Kidney.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF184981 mRNA. Translation: AAD56413.1. BC031415 mRNA. Translation: AAH31415.1.
IPI	IPI00322245.
RefSeq	NP_061369.2. NM_018881.3.
UniGene	Mm.10929.
3D structure databases
ProteinModelPortal	Q8K2I3.
SMR	Q8K2I3. Positions 3-215, 307-439.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000107135.
PTM databases
PhosphoSite	Q8K2I3.
Proteomic databases
PaxDb	Q8K2I3.
PRIDE	Q8K2I3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045902; ENSMUSP00000044405; ENSMUSG00000040170. ENSMUST00000111510; ENSMUSP00000107135; ENSMUSG00000040170.
GeneID	55990.
KEGG	mmu:55990.
UCSC	uc007dgz.1. mouse.
Organism-specific databases
CTD	2327.
MGI	MGI:1916776. Fmo2.
Phylogenomic databases
eggNOG	COG2072.
GeneTree	ENSGT00550000074292.
HOGENOM	HOG000076537.
HOVERGEN	HBG002037.
InParanoid	Q8K2I3.
KO	K00485.
OMA	PSERTMM.
OrthoDB	EOG48SGT0.
Gene expression databases
ArrayExpress	Q8K2I3.
Bgee	Q8K2I3.
CleanEx	MM_FMO2.
Genevestigator	Q8K2I3.
GermOnline	ENSMUSG00000040170. Mus musculus.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR012143. DiMe-aniline_mOase. IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. IPR002254. Flavin_mOase_2. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01122. FMOXYGENASE2.
ProtoNet	Search...
Other
ChiTaRS	FMO2. mouse.
NextBio	311714.
SOURCE	Search...

Entry information

Entry name

FMO2_MOUSE

Accession

Primary (citable) accession number: Q8K2I3
Secondary accession number(s): Q9QZF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents