ID   FMO5_RAT                Reviewed;         533 AA.
AC   Q8K4C0; Q6IRL0;
DT   29-MAR-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] 5;
DE            EC=1.14.13.8;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 5;
DE            Short=FMO 5;
DE   AltName: Full=Dimethylaniline oxidase 5;
GN   Name=Fmo5;
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., Benoit E.;
RT   "Cloning, sequencing of flavin-containing monooxygenase 5 (FMO5) in
RT   the rat.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
RN   [3]
RP   METHYLATION AT ARG-5, AND MASS SPECTROMETRY.
RX   PubMed=15047867; DOI=10.1091/mbc.E04-02-0101;
RA   Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA   Yates J.R. III, Howell K.E.;
RT   "Organellar proteomics reveals Golgi arginine dimethylation.";
RL   Mol. Biol. Cell 15:2907-2919(2004).
CC   -!- FUNCTION: In contrast with other forms of FMO it does not seem to
CC       be a drug-metabolizing enzyme (By similarity).
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   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; AF458413; AAM46761.1; -; mRNA.
DR   EMBL; BC070883; AAH70883.1; -; mRNA.
DR   IPI; IPI00203106; -.
DR   RefSeq; NP_653340.1; -.
DR   UniGene; Rn.7038; -.
DR   PhosphoSite; Q8K4C0; -.
DR   PRIDE; Q8K4C0; -.
DR   Ensembl; ENSRNOG00000018076; Rattus norvegicus.
DR   GeneID; 246248; -.
DR   KEGG; rno:246248; -.
DR   RGD; 628602; Fmo5.
DR   HOVERGEN; Q8K4C0; -.
DR   BRENDA; 1.14.13.8; 248.
DR   NextBio; 623578; -.
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; IDA:RGD.
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; IPR002257; Flavin_mOase_5.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01125; FMOXYGENASE5.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    533       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 5.
FT                                /FTId=PRO_0000147668.
FT   NP_BIND      10     15       FAD (Potential).
FT   NP_BIND     192    197       NADP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       5      5       Omega-N-methylated arginine.
FT   CONFLICT     34     34       R -> M (in Ref. 2; AAH70883).
FT   CONFLICT     50     50       K -> E (in Ref. 2; AAH70883).
FT   CONFLICT    136    136       Q -> E (in Ref. 2; AAH70883).
FT   CONFLICT    228    228       R -> H (in Ref. 2; AAH70883).
SQ   SEQUENCE   533 AA;  60056 MW;  A16A10779E91A8F8 CRC64;
     MAKKRIAVIG SGASGLTCIK CCLEEGLEPV CFERSDDIGG LWRYQENPEK GRASIYKSVI
     INTSKEMMCF SDYPIPDHYP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKQPDF
     STSGQWQVVT EHEGKQQVDV FDGVLVCTGH HTDPHLPLDS FPGIEKFKGK YFHSREYKNP
     VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKRGY PIDILLSSRI
     TNYLSKICGS ALKNRYMEKQ LNQRFDHEMF GLKPKHSALG QHPTINDDLP NRIISGLVKV
     KGNVKEFTET AAIFEDGSRE DDIDVVIFAT GYSFAFPFLE DSVKVVQNKV SLYKKVFPPN
     LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KTREEMAKRY
     VDSQRHTIQG DYIDTMEEIA DLVGVRPNLL SLAFTDPKLA FQLLVGPCTP VQYRLQGPGK
     WAGARKTILT TEDRIRKPLM TRVVERDSSG TSLVTVRVLM LAVTFLAVIL AYF
//