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   03-AUG-2022, entry version 120.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 4;
DE            EC=1.14.13.8;
DE   AltName: Full=Dimethylaniline oxidase 4;
DE   AltName: Full=FMO 1E1;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 4;
DE            Short=FMO 4;
GN   Name=FMO4;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=8188717; DOI=10.1016/s0021-9258(17)36791-1;
RA   Burnett V.L., Lawton M.P., Philpot R.M.;
RT   "Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4
RT   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 a
CC       variety of xenobiotics such as drugs and pesticides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-
CC         dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.13.8;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:Q8K4B7}; Single-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8K4B7}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Kidney and liver.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L10392; AAA21177.1; -; mRNA.
DR   PIR; A54096; A54096.
DR   RefSeq; NP_001076253.1; NM_001082784.1.
DR   AlphaFoldDB; P36367; -.
DR   SMR; P36367; -.
DR   STRING; 9986.ENSOCUP00000002427; -.
DR   PRIDE; P36367; -.
DR   GeneID; 100009582; -.
DR   KEGG; ocu:100009582; -.
DR   CTD; 2329; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; P36367; -.
DR   OrthoDB; 405736at2759; -.
DR   BRENDA; 1.14.13.148; 1749.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0070995; P:NADPH oxidation; IDA:BHF-UCL.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
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   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..555
FT                   /note="Dimethylaniline monooxygenase [N-oxide-forming] 4"
FT                   /id="PRO_0000147662"
FT   TRANSMEM        515..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         32
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         40..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         60..61
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         195..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
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