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UniProtKB/Swiss-Prot entry Q9EQ76

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FMO3_RAT
Primary accession number Q9EQ76
Secondary accession number Q5PQV6
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 45)
Name and origin of the protein
Protein name Dimethylaniline monooxygenase [N-oxide-forming] 3
Synonyms EC 1.14.13.8
Hepatic flavin-containing monooxygenase 3
FMO 3
Dimethylaniline oxidase 3
Gene name
Name: Fmo3
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
DOI=10.1006/abbi.2001.2317; PubMed=11414682 [NCBI, ExPASy, EBI, Israel, Japan]
Lattard V., Buronfosse T., Lachuer J., Longin-Sauvageon C., Moulin C., Benoit E.;
"Cloning, sequencing, tissue distribution, and heterologous expression of rat flavin-containing monooxygenase 3.";
Arch. Biochem. Biophys. 391:30-40(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
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.
  • 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
AF286595; AAG44891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC087008; AAH87008.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_445885.2; -.
UniGene Rn.163228
3D structure databases
ModBase Q9EQ76.
Organism-specific databases
RGD 619761; Fmo3.
Gene expression databases
ArrayExpress Q9EQ76; -.
GermOnline ENSRNOG00000003620; Rattus norvegicus.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002255; Flavin_mOase_3.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.
Pfam PF00743; FMO-like; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000332; FMO; 1.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01123; FMOXYGENASE3.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q9EQ76.
Genome annotation databases
Ensembl ENSRNOG00000003620; Rattus norvegicus. [Contig view]
GeneID 84493; -.
KEGG rno:84493; -.
Phylogenomic databases
HOVERGEN Q9EQ76; -.
Other
ProtoNet Q9EQ76.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   531  531     Dimethylaniline monooxygenase [N-oxide-forming] 3. PRO_0000147659
NP_BIND   9    14  6     FAD (Potential). 
NP_BIND   191   196  6     NADP (Potential). 
CONFLICT   501   501        V -> D (in Ref. 2; AAH87008). 
Sequence information
Length: 531 AA [This is the length of the unprocessed precursor] Molecular weight: 59960 Da [This is the MW of the unprocessed precursor] CRC64: 35A89988323B311F [This is a checksum on the sequence] 
        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
Q9EQ76 in FASTA format

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