ID   FMO1_MOUSE              Reviewed;         532 AA.
AC   P50285;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-DEC-2008, entry version 70.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE            EC=1.14.13.8;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 1;
DE            Short=FMO 1;
DE   AltName: Full=Dimethylaniline oxidase 1;
GN   Name=Fmo1; Synonyms=Fmo-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Itoh K., Nakamura K., Kimura T., Itoh S., Kamataki T.;
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Liver;
RX   MEDLINE=98241973; PubMed=9580872;
RA   Cherrington N.J., Falls J.G., Rose R.L., Clements K.M., Philpot R.M.,
RA   Levi P.E., Hodgson E.;
RT   "Molecular cloning, sequence, and expression of mouse flavin-
RT   containing monooxygenases 1 and 5 (FMO1 and FMO5).";
RL   J. Biochem. Mol. Toxicol. 12:205-212(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This protein is involved in the oxidative metabolism of
CC       a variety of xenobiotics such as drugs and pesticides. Form I
CC       catalyzes the N-oxygenation of secondary and tertiary amines.
CC   -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N-
CC       dimethylaniline N-oxide + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum
CC       membrane.
CC   -!- TISSUE SPECIFICITY: Liver (By similarity).
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; D16215; BAA03745.1; -; mRNA.
DR   EMBL; U87456; AAB47569.1; -; mRNA.
DR   EMBL; BC011229; AAH11229.1; -; mRNA.
DR   PIR; B61243; B61243.
DR   RefSeq; NP_034361.1; -.
DR   UniGene; Mm.976; -.
DR   PhosphoSite; P50285; -.
DR   Ensembl; ENSMUSG00000040181; Mus musculus.
DR   GeneID; 14261; -.
DR   KEGG; mmu:14261; -.
DR   MGI; MGI:1310002; Fmo1.
DR   HOGENOM; P50285; -.
DR   HOVERGEN; P50285; -.
DR   NextBio; 285603; -.
DR   ArrayExpress; P50285; -.
DR   CleanEx; MM_FMO1; -.
DR   GermOnline; ENSMUSG00000040181; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005792; C:microsome; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004499; F:flavin-containing monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002253; Flavin_mOase_1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01121; FMOXYGENASE1.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    532       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 1.
FT                                /FTId=PRO_0000147640.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   SITE        208    208       Important for substrate binding (By
FT                                similarity).
SQ   SEQUENCE   532 AA;  59915 MW;  C3CEDC7FC82DAC59 CRC64;
     MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSSDLGGL WRFTEHVEEG RASLYKSVVS
     NSSREMSCYP DFPFPEDYPN FVPNSLFLEY LKLYSTQFNL QRCIYFNTKV CSITKRPDFA
     VSGQWEVVTV TNGKQNSAIF DAVMVCTGFL TNPHLPLDSF PGILTFKGEY FHSRQYKHPD
     IFKDKRVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMIFMTRFQ
     NMLRNLLPTP IVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVFIK
     PSIKEVKENS VVFNNTPKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH
     LPKPTLAVIG LIKPLGSMVP TGETQARWVV QVLKGATTLP PPSVMMEEVN ERKKNKHSGF
     GLCYCKALQT DYITYIDDLL TSINAKPDLR AMLLTDPRLA LSIFFGPCTP YHFRLTGPGK
     WEGARKAILT QWDRTVKVTK TRTIQESPSS FETLLKLFSF LALLIAVFLI FL
//