ID   FMO4_MOUSE              Reviewed;         560 AA.
AC   Q8VHG0;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 4;
DE            EC=1.14.13.8;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 4;
DE            Short=FMO 4;
DE   AltName: Full=Dimethylaniline oxidase 4;
GN   Name=Fmo4;
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].
RC   STRAIN=129/Sv; TISSUE=Kidney;
RA   Hernandez D., Janmohamed A., Chandan P., Phillips I.R., Shephard E.A.;
RT   "The mouse flavin-containing monooxygenase gene cluster.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AF461145; AAL66366.1; -; mRNA.
DR   IPI; IPI00128288; -.
DR   RefSeq; NP_659127.1; -.
DR   UniGene; Mm.155164; -.
DR   PhosphoSite; Q8VHG0; -.
DR   PRIDE; Q8VHG0; -.
DR   Ensembl; ENSMUSG00000026692; Mus musculus.
DR   GeneID; 226564; -.
DR   KEGG; mmu:226564; -.
DR   MGI; MGI:2429497; Fmo4.
DR   HOGENOM; Q8VHG0; -.
DR   HOVERGEN; Q8VHG0; -.
DR   OMA; Q8VHG0; PLKSLCT.
DR   BRENDA; 1.14.13.8; 244.
DR   NextBio; 378238; -.
DR   ArrayExpress; Q8VHG0; -.
DR   Bgee; Q8VHG0; -.
DR   CleanEx; MM_FMO4; -.
DR   GermOnline; ENSMUSG00000026692; 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:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004499; F:flavin-containing monooxygenase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002256; Flavin_mOase_4.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01124; FMOXYGENASE4.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Microsome; Monooxygenase; NADP; Oxidoreductase; Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    560       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 4.
FT                                /FTId=PRO_0000147661.
FT   TRANSMEM    516    530       Potential.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   560 AA;  63792 MW;  75C3AEE53693B7AD CRC64;
     MAKKVAVIGA GVSGLSSIKC CLDENLEPTC FERTSDFGGL WKFADTSEDG MTRVYRSLVT
     NVCKEMSCYS DFPFREDYPN FMSHEKFWDY LREFAEHFGL LRYIRFKTTV LSVTKRPDFS
     ETGQWDVVTE TEGKRDRAVF DAVMVCTGQF LSPHLPLESF PGIHKFKGQI LHSQEYRIPD
     AFRGKRILVV GLGNTGGDIA VELSEIAAQV FLSTRTGTWV LSRSSPGGYP FNMIQTRWLN
     FLVRVLPSRF INWTHERKMN KILNHENYGL SIAKGKKPKF IVNDELPTCI LCGKVTMKTS
     VKDFTESSVI FEDGTTEANI DVVIFTTGYE FSFPFFEEPL KSLCTKKIIL YKRVFPPNLE
     RATLAIIGLI SLNGSILVGT EFQARWATRV FKGLCSIPPS QKLMAEATKT EQLIKRGVIK
     DTSQDKLDFI TYMDELTQCI GAKPSIPLLF IKDPRLAWEV FFGPCTPYQY RLVGPGRWDG
     ARNAILTQWD RTLKPLKTRI VPKSPEPTSL SHYLIAWGAP VLLVSLLLIY KSSHFLELVQ
     GKLPRRFPPY RLLWYMPQNS
//