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Reviewed, UniProtKB/Swiss-Prot Q8K2I3 (FMO2_MOUSE)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 2
    EC=1.14.13.8
Alternative name(s):
    Pulmonary flavin-containing monooxygenase 2
      Short name=FMO 2
    Dimethylaniline oxidase 2
Gene names
Name: Fmo2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 535534Dimethylaniline monooxygenase [N-oxide-forming] 2
PRO_0000147648

Regions

Nucleotide binding9 – 146FAD Potential
Nucleotide binding191 – 1966NADP Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict1691Q → R in AAD56413. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8K2I3-1 [UniParc].

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

FASTA53560,974
        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' 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: 11835629] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF184981 mRNA. Translation: AAD56413.1.
BC031415 mRNA. Translation: AAH31415.1.
IPIIPI00322245.
RefSeqNP_061369.2.
UniGeneMm.10929

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000040170. Mus musculus. [Contig view]
GeneID55990.
KEGGmmu:55990.

Organism-specific databases

MGIMGI:1916776. Fmo2.

Phylogenomic databases

HOGENOMQ8K2I3.
HOVERGENQ8K2I3.
OMAQ8K2I3. NYVDYLD.

Enzyme and pathway databases

BRENDA1.14.13.8. 244.

Gene expression databases

ArrayExpressQ8K2I3.
BgeeQ8K2I3.
CleanExMM_FMO2.
GermOnlineENSMUSG00000040170. Mus musculus.

Family and domain databases

InterProIPR012143. dManiline_mOase.
IPR000960. Flavin_mOase.
IPR002254. Flavin_mOase_2.
[Graphical view]
PfamPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFPIRSF000332. FMO. 1 hit.
PRINTSPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other Resources

NextBio311714.
SOURCESearch...

Entry information

Entry nameFMO2_MOUSE
AccessionPrimary (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: June 16, 2009
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents