ID   FMO4_MOUSE              Reviewed;         560 AA.
AC   Q8VHG0;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 4;
DE            EC=1.14.13.8;
DE   AltName: Full=Dimethylaniline oxidase 4;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 4;
DE            Short=FMO 4;
GN   Name=Fmo4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv; TISSUE=Kidney;
RA   Hernandez D., Janmohamed A., Chandan P., Phillips I.R., Shephard E.A.;
RT   "The mouse flavin-containing monooxygenase gene cluster.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: This protein is involved in the oxidative metabolism of a
CC       variety of xenobiotics such as drugs and pesticides. {ECO:0000250}.
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; Evidence={ECO:0000250};
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   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; AF461145; AAL66366.1; -; mRNA.
DR   CCDS; CCDS15423.1; -.
DR   RefSeq; NP_659127.1; NM_144878.1.
DR   RefSeq; XP_006496839.1; XM_006496776.3.
DR   RefSeq; XP_006496840.1; XM_006496777.2.
DR   AlphaFoldDB; Q8VHG0; -.
DR   SMR; Q8VHG0; -.
DR   BioGRID; 230532; 4.
DR   STRING; 10090.ENSMUSP00000107150; -.
DR   iPTMnet; Q8VHG0; -.
DR   PhosphoSitePlus; Q8VHG0; -.
DR   jPOST; Q8VHG0; -.
DR   MaxQB; Q8VHG0; -.
DR   PaxDb; 10090-ENSMUSP00000107150; -.
DR   PeptideAtlas; Q8VHG0; -.
DR   ProteomicsDB; 273011; -.
DR   Antibodypedia; 34378; 121 antibodies from 22 providers.
DR   DNASU; 226564; -.
DR   Ensembl; ENSMUST00000028014.10; ENSMUSP00000028014.4; ENSMUSG00000026692.13.
DR   Ensembl; ENSMUST00000111525.8; ENSMUSP00000107150.2; ENSMUSG00000026692.13.
DR   GeneID; 226564; -.
DR   KEGG; mmu:226564; -.
DR   UCSC; uc007dgv.1; mouse.
DR   AGR; MGI:2429497; -.
DR   CTD; 2329; -.
DR   MGI; MGI:2429497; Fmo4.
DR   VEuPathDB; HostDB:ENSMUSG00000026692; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   GeneTree; ENSGT00940000160256; -.
DR   HOGENOM; CLU_006909_8_2_1; -.
DR   InParanoid; Q8VHG0; -.
DR   OMA; HYLKVWG; -.
DR   OrthoDB; 2079054at2759; -.
DR   PhylomeDB; Q8VHG0; -.
DR   TreeFam; TF105285; -.
DR   BRENDA; 1.14.13.8; 3474.
DR   BioGRID-ORCS; 226564; 4 hits in 79 CRISPR screens.
DR   PRO; PR:Q8VHG0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8VHG0; Protein.
DR   Bgee; ENSMUSG00000026692; Expressed in right kidney and 35 other cell types or tissues.
DR   ExpressionAtlas; Q8VHG0; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0097009; P:energy homeostasis; IGI:MGI.
DR   GO; GO:0046322; P:negative regulation of fatty acid oxidation; IGI:MGI.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IMP:MGI.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF74; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING] 4; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01124; FMOXYGENASE4.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   Genevisible; Q8VHG0; MM.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..560
FT                   /note="Dimethylaniline monooxygenase [N-oxide-forming] 4"
FT                   /id="PRO_0000147661"
FT   TRANSMEM        510..530
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   560 AA;  63792 MW;  75C3AEE53693B7AD CRC64;
     MAKKVAVIGA GVSGLSSIKC CLDENLEPTC FERTSDFGGL WKFADTSEDG MTRVYRSLVT
     NVCKEMSCYS DFPFREDYPN FMSHEKFWDY LREFAEHFGL LRYIRFKTTV LSVTKRPDFS
     ETGQWDVVTE TEGKRDRAVF DAVMVCTGQF LSPHLPLESF PGIHKFKGQI LHSQEYRIPD
     AFRGKRILVV GLGNTGGDIA VELSEIAAQV FLSTRTGTWV LSRSSPGGYP FNMIQTRWLN
     FLVRVLPSRF INWTHERKMN KILNHENYGL SIAKGKKPKF IVNDELPTCI LCGKVTMKTS
     VKDFTESSVI FEDGTTEANI DVVIFTTGYE FSFPFFEEPL KSLCTKKIIL YKRVFPPNLE
     RATLAIIGLI SLNGSILVGT EFQARWATRV FKGLCSIPPS QKLMAEATKT EQLIKRGVIK
     DTSQDKLDFI TYMDELTQCI GAKPSIPLLF IKDPRLAWEV FFGPCTPYQY RLVGPGRWDG
     ARNAILTQWD RTLKPLKTRI VPKSPEPTSL SHYLIAWGAP VLLVSLLLIY KSSHFLELVQ
     GKLPRRFPPY RLLWYMPQNS
//