FMO4_MOUSE
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 03-AUG-2022, entry version 135.
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; Q8VHG0; -.
DR PeptideAtlas; Q8VHG0; -.
DR PRIDE; Q8VHG0; -.
DR ProteomicsDB; 273011; -.
DR Antibodypedia; 34378; 108 antibodies from 22 providers.
DR DNASU; 226564; -.
DR Ensembl; ENSMUST00000028014; ENSMUSP00000028014; ENSMUSG00000026692.
DR Ensembl; ENSMUST00000111525; ENSMUSP00000107150; ENSMUSG00000026692.
DR GeneID; 226564; -.
DR KEGG; mmu:226564; -.
DR UCSC; uc007dgv.1; mouse.
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; SHYLKVW; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q8VHG0; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 3474.
DR BioGRID-ORCS; 226564; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q8VHG0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VHG0; protein.
DR Bgee; ENSMUSG00000026692; Expressed in right kidney and 33 other tissues.
DR ExpressionAtlas; Q8VHG0; baseline and differential.
DR Genevisible; Q8VHG0; MM.
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:0004497; F:monooxygenase activity; IBA:GO_Central.
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: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; -; 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 Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01124; FMOXYGENASE4.
DR SUPFAM; SSF51905; SSF51905; 2.
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
