ID   FMO2_MOUSE              Reviewed;         535 AA.
AC   Q8K2I3; Q9QZF7;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 48.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 2;
DE            EC=1.14.13.8;
DE   AltName: Full=Pulmonary flavin-containing monooxygenase 2;
DE            Short=FMO 2;
DE   AltName: Full=Dimethylaniline oxidase 2;
GN   Name=Fmo2;
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], AND CHARACTERIZATION.
RC   STRAIN=C57BL/6; TISSUE=Kidney;
RX   MEDLINE=21823878; PubMed=11835629;
RA   Karoly E.D., Rose R.L.;
RT   "Sequencing, expression, and characterization of cDNA expressed
RT   flavin-containing monooxygenase 2 from mouse.";
RL   J. Biochem. Mol. Toxicol. 15:300-308(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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. Shows
CC       catalytic activity towards methimazole, thiourea, trimethylamine,
CC       and the insecticide phorate.
CC   -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N-
CC       dimethylaniline N-oxide + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 10.5;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity).
CC       Endoplasmic reticulum membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; AF184981; AAD56413.1; -; mRNA.
DR   EMBL; BC031415; AAH31415.1; -; mRNA.
DR   RefSeq; NP_061369.2; -.
DR   UniGene; Mm.10929; -.
DR   Ensembl; ENSMUSG00000040170; Mus musculus.
DR   GeneID; 55990; -.
DR   KEGG; mmu:55990; -.
DR   MGI; MGI:1916776; Fmo2.
DR   HOGENOM; Q8K2I3; -.
DR   HOVERGEN; Q8K2I3; -.
DR   NextBio; 311714; -.
DR   ArrayExpress; Q8K2I3; -.
DR   CleanEx; MM_FMO2; -.
DR   GermOnline; ENSMUSG00000040170; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006800; P:oxygen and reactive oxygen species metaboli...; IDA:MGI.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002254; Flavin_mOase_2.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01122; FMOXYGENASE2.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Magnesium;
KW   Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    535       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 2.
FT                                /FTId=PRO_0000147648.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT    169    169       Q -> R (in Ref. 1; AAD56413).
SQ   SEQUENCE   535 AA;  60974 MW;  705FAD9D8EADB1B1 CRC64;
     MAKKVVVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYRSVIT
     NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA
     SSGQWEVYTQ SNGKEQRTVF DAVMVCSGHH IQPHLPLKSF PGIERFRGQY FHSREYKHPV
     GFEGKRILVV GIGNSAADIA SELSKTAAQV FVSTRHGSWV MSRISEDGYP WDMVFHTRFS
     SMLRNVLPRT VVKWMMEQQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK
     TRVKELTETA VVFEDGTVEE DVDIIVFATG YTFSFSFLED SLVKVEDNRV SLYKAMFPPH
     LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SETTMMADIV ERNEKRVNLF
     GKSQSQILQT NYVDYLDELA LEIGAKPDFV SLFFKDPKLA VKLYFGPCNS YQYRLVGPGQ
     WEGARNAILT QKQRILKPLK TRTLQSSDSA PVSFLLKILG LLAVVLAFFF QLQGF
//