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UniProtKB/Swiss-Prot entry P32417

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

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Entry information
Entry name FMO3_RABIT
Primary accession number P32417
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 63)
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
FMO form 2
FMO II
FMO 1D1
Dimethylaniline oxidase 3
Gene name
Name: FMO3
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white;
TISSUE=Liver;
PubMed=8188717 [NCBI, ExPASy, EBI, Israel, Japan]
Burnett V.L., Lawton M.P., Philpot R.M.;
"Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3.";
J. Biol. Chem. 269:14314-14322(1994).
[2]
 PROTEIN SEQUENCE OF 2-531.
DOI=10.1016/0003-9861(91)90596-B; PubMed=1898080 [NCBI, ExPASy, EBI, Israel, Japan]
Ozols J.;
"Multiple forms of liver microsomal flavin-containing monooxygenases: complete covalent structure of form 2.";
Arch. Biochem. Biophys. 290:103-115(1991).
[3]
 PROTEIN SEQUENCE OF 2-33.
TISSUE=Liver;
DOI=10.1016/0006-291X(89)92097-4; PubMed=2505769 [NCBI, ExPASy, EBI, Israel, Japan]
Ozols J.;
"Liver microsomes contain two distinct NADPH-Monooxygenases with NH2-terminal segments homologous to the flavin containing NADPH-monooxygenase of Pseudomonas fluorescens.";
Biochem. Biophys. Res. Commun. 163:49-55(1989).
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.
  • CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
  • COFACTOR: FAD.
  • SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane.
  • TISSUE SPECIFICITY: Liver.
  • 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
L10391; AAA21178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B54096; B54096.
S18380; S18380.
RefSeq NP_001075715.1; -.
UniGene Ocu.1821
3D structure databases
ModBase P32417.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031227; Cellular component: intrinsic to endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0005792; Cellular component: microsome (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004499; Molecular function: flavin-containing monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002255; Flavin_mOase_3.
Graphical view of domain structure.
Pfam PF00743; FMO-like; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000332; FMO; 1.
PRINTS PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01123; FMOXYGENASE3.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
ProtoNet P32417.
Genome annotation databases
GeneID 100009065; -.
Phylogenomic databases
HOVERGEN P32417; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   531  530     Dimethylaniline monooxygenase [N-oxide-forming] 3. PRO_0000147658
NP_BIND   9    14  6     FAD (Potential). 
NP_BIND   191   196  6     NADP (Potential). 
VARIANT   279   279  1     R -> M. 
VARIANT   405   405  1     M -> V. 
CONFLICT   76    76        D -> P (in Ref. 2; AA sequence). 
CONFLICT   81    81        F -> N (in Ref. 2; AA sequence). 
CONFLICT   128   130        STE -> ATC (in Ref. 2; AA sequence). 
CONFLICT   172   173        HS -> RQ (in Ref. 2; AA sequence). 
CONFLICT   197   197        C -> E (in Ref. 2; AA sequence). 
CONFLICT   306   306        F -> FKEF (in Ref. 2; AA sequence). 
CONFLICT   419   419        W -> T (in Ref. 2; AA sequence). 
CONFLICT   423   423        S -> W (in Ref. 2; AA sequence). 
CONFLICT   514   516        WLK -> ELW (in Ref. 2; AA sequence). 
Sequence information
Length: 531 AA [This is the length of the unprocessed precursor] Molecular weight: 59815 Da [This is the MW of the unprocessed precursor] CRC64: A4505481077C6CC8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGKKVAIIGA GISGLASIRS CLEEGLEPTC FEMSDDIGGL WKFSDHAEEG RASIYQSVFT 

        70         80         90        100        110        120 
NSSKEMMCFP DFPFPDDFPN FMHNSKLQEY ITTFAREKNL LKYIQFKTLV SSIKKHPDFS 

       130        140        150        160        170        180 
VTGQWYVSTE RNGKKETAVF DAVMICSGHH VYPNLPKDSF PGLKHFKGKS FHSREYKEPG 

       190        200        210        220        230        240 
IFKGKRVLVI GLGNSGCDIA TELSHTAEQV VISSRSGSWV MSRVWDDGYP WDMLYVTRFQ 

       250        260        270        280        290        300 
TFLKNNLPTA ISDWWYVKQM NAKFKHENYS LMPLNGTLRK EPVFNDDLPA RILCGTVSIK 

       310        320        330        340        350        360 
PNVKEFTETS AIFEDGTVFE AIDSVIFATG YGYAYPFLDD SIIKSENNKV TLFKGIFPPQ 

       370        380        390        400        410        420 
LEKPTMAVIG LVQSLGAAIP TTDLQARWAA QVIKGTCTLP PVKDMMNDIH EKMGTKLKWF 

       430        440        450        460        470        480 
GKSETIQTDY INYMDELASF IGVKLNIPWL FLTDPRLALE VFFGPCSPYQ FRLVGPGKWP 

       490        500        510        520        530 
GARQAILTQW DRSLKPMKTR AVGHLQKPAL FSPWLKLLAI AVLLIAAVLV F
P32417 in FASTA format

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