ID   FMO5_RABIT              Reviewed;         533 AA.
AC   Q04799;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-DEC-2008, entry version 66.
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=FMO form 3;
DE   AltName: Full=FMO 1C1;
DE   AltName: Full=Dimethylaniline oxidase 5;
GN   Name=FMO5;
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   TISSUE=Liver;
RX   MEDLINE=93252844; PubMed=8486656;
RA   Atta-Asafo-Adjei E., Lawton M.P., Philpot R.M.;
RT   "Cloning, sequencing, distribution, and expression in Escherichia coli
RT   of flavin-containing monooxygenase 1C1. Evidence for a third gene
RT   subfamily in rabbits.";
RL   J. Biol. Chem. 268:9681-9689(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 3-514.
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   MEDLINE=94190897; PubMed=8142375; DOI=10.1021/bi00178a035;
RA   Ozols J.;
RT   "Isolation and structure of a third form of liver microsomal flavin
RT   monooxygenase.";
RL   Biochemistry 33:3751-3757(1994).
CC   -!- FUNCTION: In contrast with other forms of FMO it does not seem to
CC       be a drug-metabolizing enzyme.
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.
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; L08449; AAA31235.1; -; mRNA.
DR   PIR; A45912; A45912.
DR   PIR; A46677; A46677.
DR   RefSeq; NP_001075714.1; -.
DR   UniGene; Ocu.1864; -.
DR   GeneID; 100009064; -.
DR   HOVERGEN; Q04799; -.
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:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004499; F:flavin-containing monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; IPR002257; Flavin_mOase_5.
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; PR01125; FMOXYGENASE5.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Endoplasmic reticulum; FAD;
KW   Flavoprotein; Membrane; Methylation; Microsome; Monooxygenase; NADP;
KW   Oxidoreductase; Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    533       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 5.
FT                                /FTId=PRO_0000147667.
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 (By
FT                                similarity).
FT   VARIANT     132    132       C -> V.
FT   VARIANT     241    241       S -> Q.
FT   VARIANT     390    390       T -> V.
FT   VARIANT     419    419       R -> F.
FT   VARIANT     451    451       S -> P.
FT   VARIANT     509    509       S -> L.
FT   CONFLICT      5      5       R -> K (in Ref. 2; AA sequence).
FT   CONFLICT    160    160       S -> K (in Ref. 2; AA sequence).
FT   CONFLICT    306    306       E -> ELKE (in Ref. 2; AA sequence).
FT   CONFLICT    512    512       Missing (in Ref. 2; AA sequence).
SQ   SEQUENCE   533 AA;  59845 MW;  188617ACA56E9286 CRC64;
     MAGKRVAVIG AGASGLACIK CCLEEGLEPV CFERTDDIGG LWRFQESPDE GRASIYKSVI
     INTSKEMMCF SDYPIPDHFP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKRPDF
     STSGQWEVLT ECEGKKESAV FDGVLVCTGH HTSAHLPLES FPGIEKFKGQ YLHSRDYKNP
     EKFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW IMNRVGDHGY PIDILLSSRF
     SQFLKKITGE TIANSFLERK MNQRFDHAMF GLKPKHRALS QHPTVNDDLP NRIISGSVKI
     KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFSFPFLE DSVKVVKNKV SLYKKVFPPN
     LEKPTLAIIG LIQPLGAIMP ISELQARWAT LVFKGLKTLP SQSEMMTEIS QVQEKMAKRY
     VESQRHTIQG DYIETMEEIA DLVGVRPNLL SLAFTDPRLA LQLLLGPCTP VHYRLQGRGK
     WDGARKTILT VEDRIRKPLM TRVTESSNSV TSMMTMGKFM LAIAFLAIAV VYF
//