ID   FMO4_RABIT              Reviewed;         555 AA.
AC   P36367;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2008, entry version 59.
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=FMO 1E1;
DE   AltName: Full=Dimethylaniline oxidase 4;
GN   Name=FMO4;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   MEDLINE=94245761; PubMed=8188717;
RA   Burnett V.L., Lawton M.P., Philpot R.M.;
RT   "Cloning and sequencing of flavin-containing monooxygenases FMO3 and
RT   FMO4 from rabbit and characterization of FMO3.";
RL   J. Biol. Chem. 269:14314-14322(1994).
CC   -!- FUNCTION: This protein is involved in the oxidative metabolism of
CC       a variety of xenobiotics such as drugs and pesticides.
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: Kidney and liver.
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; L10392; AAA21177.1; -; mRNA.
DR   PIR; A54096; A54096.
DR   RefSeq; NP_001076253.1; -.
DR   UniGene; Ocu.1822; -.
DR   Ensembl; ENSOCUG00000002795; Oryctolagus cuniculus.
DR   GeneID; 100009582; -.
DR   HOVERGEN; P36367; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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    555       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 4.
FT                                /FTId=PRO_0000147662.
FT   TRANSMEM    518    532       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   555 AA;  62992 MW;  5A7219CAD1DEB3A2 CRC64;
     MAKKVAVIGA GVSGLTSIKC CLDEDLEPTC FERSNDIGGL WKYTETSKDG MTRIYWSLVT
     NVCKEMSCYS DFPFQEDYPN FMSHSKFWNY LQEFAEHFDL LKYIQFKTTV CSVTKRPDFS
     KTGQWDVVTE TEGKQHRAVF DAVMVCTGKF LNPRLPLESF PGILKFRGQI LHCQEYKIPE
     GFRGQRVLVI GLGNSGGDVA VELSRVAAQV LLSTRTGTWV ISRSSNGGYP FNMMITRRCL
     NVIEQVLPSC FLRWINERQM NKRFNHENYG LSITKGKNPK FIVNDELPTC ILCGTVTVKT
     SVKEFTETSA IFEDGTVEEN IDSVIFTTGY VFSFPFLEEP LRSLCMKKMF LYKHVFPSNL
     ERASMAIIGL ISLKGSILTG TELQARWATR VFKGLCKIPP PQQLMAEVTK KEELIKRGVI
     KDTSEEKLSY IPYMDDLAAC IGTKPNIPLL FLKDPRLAWE VFFGPCTPYQ YRLMGPGKWD
     GARNAILTQW DRTLKPLKTR TVSSDSSKSA SLSHYLKVWG APLLLASVLL ICKSSHFLKS
     VRDKLQNRIF PYLVL
//