ID   FMO3_RAT                Reviewed;         531 AA.
AC   Q9EQ76; Q5PQV6;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   04-NOV-2008, entry version 46.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3;
DE            EC=1.14.13.8;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 3;
DE            Short=FMO 3;
DE   AltName: Full=Dimethylaniline oxidase 3;
GN   Name=Fmo3;
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], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=21308417; PubMed=11414682; DOI=10.1006/abbi.2001.2317;
RA   Lattard V., Buronfosse T., Lachuer J., Longin-Sauvageon C., Moulin C.,
RA   Benoit E.;
RT   "Cloning, sequencing, tissue distribution, and heterologous expression
RT   of rat flavin-containing monooxygenase 3.";
RL   Arch. Biochem. Biophys. 391:30-40(2001).
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: Involved in the oxidative metabolism of a variety of
CC       xenobiotics such as drugs and pesticides. It N-oxygenates primary
CC       aliphatic alkylamines as well as secondary and tertiary amines.
CC       Acts on TMA to produce TMA-N-oxide. Has activities of methimazole
CC       S-oxidation and NADPH oxidation associated with the N- or S-
CC       oxidation of trimethylamine and thioacetamide.
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   -!- TISSUE SPECIFICITY: Expressed in kidney and liver. Weakly
CC       expressed in lung. Does not seem to be expressed in brain, adipose
CC       tissue, or muscle.
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; AF286595; AAG44891.1; -; mRNA.
DR   EMBL; BC087008; AAH87008.1; -; mRNA.
DR   RefSeq; NP_445885.2; -.
DR   UniGene; Rn.163228; -.
DR   Ensembl; ENSRNOG00000003620; Rattus norvegicus.
DR   GeneID; 84493; -.
DR   KEGG; rno:84493; -.
DR   RGD; 619761; Fmo3.
DR   HOVERGEN; Q9EQ76; -.
DR   NextBio; 617057; -.
DR   ArrayExpress; Q9EQ76; -.
DR   GermOnline; ENSRNOG00000003620; Rattus norvegicus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002255; Flavin_mOase_3.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01123; FMOXYGENASE3.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    531       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 3.
FT                                /FTId=PRO_0000147659.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   CONFLICT    501    501       V -> D (in Ref. 2; AAH87008).
SQ   SEQUENCE   531 AA;  59960 MW;  35A89988323B311F CRC64;
     MKRKVAVIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHTEEG RASIYQSVFT
     NSSKEMMCFP DFPYPDDFPN FMHNSKLQEY ITSFATEKNL LKYIQFETLV TRINKCPDFS
     TTGKWEVTTE KNSKKETAVF DAVMICSGHH VYPHLPKDSF PGLNRFKGKC FHSRDYKEPG
     TWKGKRVLVI GLGNSGCDIA AELSHVAQQV IISSRSGSWV MSRVWNDGYP WDMVVITRFQ
     TFLKNNLPTA ISDWWYMKQM NARFKHENYG LMPLNGTLRK EPVFNDELPA RILCGTVSIK
     PNVKEFTETS AVFEDGTVFE GIDCVIFATG YGYAYPFLDD SIIKSRNNEV TLYKGIFPPQ
     LEKPTMAVIG LVQSLGAAIP TTDLQARWAA QVIRGTCILP SVNDMMDDID EKMGKKLKWF
     GNSTTIQTDY IVYMDELASF IGAKPNILWL FLKDPRLAIE VFFGPCSPYQ FRLVGPGKWS
     GARNAILTQW DRSLKPMKTR VVGGIQKPCL YSHFLRLLAV PVLIALFLVL I
//