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P97501 (FMO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 3

EC=1.14.13.8
Alternative name(s):
Dimethylaniline oxidase 3
Hepatic flavin-containing monooxygenase 3
Short name=FMO 3
Trimethylamine monooxygenase
EC=1.14.13.148
Gene names
Name:Fmo3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.3

Catalytic activity

N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.

N,N,N-trimethylamine + NADPH + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O.

Cofactor

FAD By similarity.

Subcellular location

Microsome membrane. Endoplasmic reticulum membrane By similarity.

Tissue specificity

Liver.

Induction

Expression is specifically repressed in male mice after puberty, preventing trimethylamine degradation. Trimethylamine is present at high concentration in the urine of male mice after puberty and acts as an attractant. Ref.3

Miscellaneous

Trimethylamine is a bacterial metabolite found in some animal odors, and is a repulsive odor associated with bad breath and spoiled food for most organisms, except for M.musculus, where it acts as an attractant (Ref.3).

Sequence similarities

Belongs to the FMO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 534533Dimethylaniline monooxygenase [N-oxide-forming] 3
PRO_0000147656

Regions

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

Amino acid modifications

Modified residue4011Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P97501 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: F72F7993C01AF9C9

FASTA53460,516
        10         20         30         40         50         60 
MKKKVAIIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHIEEG RASIYQSVFT 

        70         80         90        100        110        120 
NSSKEMMCFP DFPYPDDFPN FMHHSKLQEY ITSFAKEKNL LKYIQFETPV TSINKCPNFS 

       130        140        150        160        170        180 
TTGKWEVTTE KHGKKETAVF DATMICSGHH IFPHVPKDSF PGLNRFKGKC FHSRDYKEPG 

       190        200        210        220        230        240 
IWKGKRVLVI GLGNSGCDIA AELSHVAQKV TISSRSGSWV MSRVWDDGYP WDMVVLTRFQ 

       250        260        270        280        290        300 
TFLKNNLPTA ISDWWYTRQM NARFKHENYG LVPLNRTLRK EPVFNDELPA RILCGMVTIK 

       310        320        330        340        350        360 
PNVKEFTETS AVFEDGTMFE AIDCVIFATG YGYAYPFLDD SIIKSRNNEV TLYKGVFPPQ 

       370        380        390        400        410        420 
LEKPTMAVIG LVQSLGATIP ITDLQARWAA QVIKGTCTLP SVNDMMDDID EKMGEKFKWY 

       430        440        450        460        470        480 
GNSTTIQTDY IVYMDELASF IGAKPNLLWL FLKDPRLAVE VFFGPCSPYQ FRLVGPGKWS 

       490        500        510        520        530 
GARNAILTQW DRSLKPMKTR VVSKVQKSCS HFYSRLLRLL AVPVLLIALF LVLI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): comparison with the human isoform."
Falls J.G., Cherrington N.J., Clements K.M., Philpot R.M., Levi P.E., Rose R.L., Hodgson E.
Arch. Biochem. Biophys. 347:9-18(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Liver.
[2]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[3]"Synchronous evolution of an odor biosynthesis pathway and behavioral response."
Li Q., Korzan W.J., Ferrero D.M., Chang R.B., Roy D.S., Buchi M., Lemon J.K., Kaur A.W., Stowers L., Fendt M., Liberles S.D.
Curr. Biol. 23:11-20(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U87147 mRNA. Translation: AAB47541.1.
CCDSCCDS15426.1.
RefSeqNP_032056.1. NM_008030.1.
UniGeneMm.2900.

3D structure databases

ProteinModelPortalP97501.
SMRP97501. Positions 2-208, 310-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97501. 3 interactions.
MINTMINT-4095189.
STRING10090.ENSMUSP00000028010.

PTM databases

PhosphoSiteP97501.

Proteomic databases

MaxQBP97501.
PaxDbP97501.
PRIDEP97501.

Protocols and materials databases

DNASU14262.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028010; ENSMUSP00000028010; ENSMUSG00000026691.
GeneID14262.
KEGGmmu:14262.
UCSCuc007dhe.1. mouse.

Organism-specific databases

CTD2328.
MGIMGI:1100496. Fmo3.

Phylogenomic databases

eggNOGCOG2072.
HOGENOMHOG000076537.
HOVERGENHBG002037.
InParanoidP97501.
KOK00485.
OMAFMHNSKL.
OrthoDBEOG7GXPB6.
PhylomeDBP97501.
TreeFamTF105285.

Gene expression databases

ArrayExpressP97501.
BgeeP97501.
CleanExMM_FMO3.
GenevestigatorP97501.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFPIRSF000332. FMO. 1 hit.
PRINTSPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
ProtoNetSearch...

Other

NextBio285607.
PROP97501.
SOURCESearch...

Entry information

Entry nameFMO3_MOUSE
AccessionPrimary (citable) accession number: P97501
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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