ID   FMO2_RAT                Reviewed;         535 AA.
AC   Q6IRI9;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 41.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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 (By
CC       similarity).
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   -!- 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; BC070904; AAH70904.1; -; mRNA.
DR   RefSeq; NP_653338.2; -.
DR   UniGene; Rn.3928; -.
DR   Ensembl; ENSRNOG00000003510; Rattus norvegicus.
DR   GeneID; 246245; -.
DR   KEGG; rno:246245; -.
DR   RGD; 628600; Fmo2.
DR   HOVERGEN; Q6IRI9; -.
DR   NextBio; 623556; -.
DR   ArrayExpress; Q6IRI9; -.
DR   GermOnline; ENSRNOG00000003510; Rattus norvegicus.
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   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   2: Evidence at transcript 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_0000147651.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   MOD_RES       2      2       N-acetylvaline (By similarity).
SQ   SEQUENCE   535 AA;  60899 MW;  4BDABD847733F639 CRC64;
     MVKKVAVIGA GVSGLISLKG CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYHSVIT
     NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA
     SSGQWDVYVQ SNGKEQRAVF DAVMVCSGHH IQPHLPLKSF PGIERFQGQY FHSRQYKHPV
     GYEGKRILVV GIGNSAADIA SELSKRAAQV FVSTRHGSWV LSRISEDGYP WDMVFHTRFS
     SMLRNVLPRT VVKWMMERQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK
     TRVKELTETA VVFEDGTVEE DVDVIVFATG YTFSFPFLED SLVKVEDNKV SLYKAMFPPH
     LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGVCRLP SETTMMADIA ERNEKRIDLF
     GKSQSQILQT NYIDYLDELA LEIGAKPDFI SLLFKDPKLA VKLYFGPCNS YQYRLVGPGQ
     WEGARNAILT QKQRILKPLK TRTLQTSASA PVSFLIKVLG LLAIVLAFFF KLHGF
//