ID   FMO4_RAT                Reviewed;         560 AA.
AC   Q8K4B7; Q66HR6;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 52.
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   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 [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Lattard V., Longin-Sauvageon C., Benoit E.;
RT   "Cloning, sequencing and tissue distribution of rat flavin-containing
RT   monooxygenase 4. Two different FMO4 are produced by tissue specific
RT   alternative splicing.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity).
CC       Endoplasmic reticulum membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the FMO family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF458416; AAM46764.1; -; mRNA.
DR   EMBL; BC081721; AAH81721.1; -; mRNA.
DR   IPI; IPI00325823; -.
DR   RefSeq; NP_653147.1; -.
DR   UniGene; Rn.216582; -.
DR   Ensembl; ENSRNOG00000003400; Rattus norvegicus.
DR   GeneID; 246247; -.
DR   KEGG; rno:246247; -.
DR   RGD; 628601; Fmo4.
DR   HOVERGEN; Q8K4B7; -.
DR   OMA; Q8K4B7; PLKSLCT.
DR   BRENDA; 1.14.13.8; 248.
DR   NextBio; 623572; -.
DR   ArrayExpress; Q8K4B7; -.
DR   GermOnline; ENSRNOG00000003400; 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: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_0000147663.
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).
FT   CONFLICT    244    244       Q -> R (in Ref. 1; AAM46764).
SQ   SEQUENCE   560 AA;  63660 MW;  9A7A77C41A328EFB CRC64;
     MAKKVAVIGA GVSGLSSIKC CLDENLEPTC FERSSDFGGL WKFAEASEDG MTRVYRSLVT
     NVCKEMSCYS DFPFHEDYPN FMSHEKFWDY LREFAEHFGL LKYIRFKTTV RSVTKRPDFS
     ETGQWEVVTE TEGKQDRAVF DAVMVCTGQF LSPRLPLESF PGIHKFKGQI LHSQEYRIPD
     AFRGKRILVV GLGNTGGDVA VELSGIAAQV FLSTRTGAWV RSRSSVGGYP LNMMQTRWRN
     FLAQVLPSRF VSWNQERQMN KIFNHENYGL SIAKGKKPKF IVNDELPTCI LCGKITMKTS
     VKDFTESSIV FEDGTIEANI DVVIFTTGYE FSFPFFEEPL KSLCTKKVIL YKRVFPPNLE
     RSTLAIIGLI SLTGSILVGT EFQARWATRV FKGLCNIPPS QKLMAEAIKK EELIKRGVIK
     DTSQDKLDFI SYMDELTQCI GAKPNIPLLF LKDPRLAWEV FFGPCTPYQY RLMGPGRWDG
     ARNAILTQWD RTVKPLKTRT VPKSQEPASL SRYLKTWGAP VLIVSLLLIY KSSLFLELVQ
     SKLQGRFSPS RILWYIPQNS
//