FMO1_MOUSE
ID FMO1_MOUSE Reviewed; 532 AA.
AC P50285;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE EC=1.14.13.8;
DE AltName: Full=Dimethylaniline oxidase 1;
DE AltName: Full=Hepatic flavin-containing monooxygenase 1;
DE Short=FMO 1;
GN Name=Fmo1; Synonyms=Fmo-1;
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].
RA Itoh K., Nakamura K., Kimura T., Itoh S., Kamataki T.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=9580872;
RX DOI=10.1002/(sici)1099-0461(1998)12:4<205::aid-jbt2>3.0.co;2-p;
RA Cherrington N.J., Falls J.G., Rose R.L., Clements K.M., Philpot R.M.,
RA Levi P.E., Hodgson E.;
RT "Molecular cloning, sequence, and expression of mouse flavin-containing
RT monooxygenases 1 and 5 (FMO1 and FMO5).";
RL J. Biochem. Mol. Toxicol. 12:205-212(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 297-307, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Lung;
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. Form I catalyzes
CC the N-oxygenation of secondary and tertiary amines.
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:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; D16215; BAA03745.1; -; mRNA.
DR EMBL; U87456; AAB47569.1; -; mRNA.
DR EMBL; BC011229; AAH11229.1; -; mRNA.
DR CCDS; CCDS15424.1; -.
DR PIR; B61243; B61243.
DR RefSeq; NP_001317220.1; NM_001330291.1.
DR RefSeq; NP_034361.1; NM_010231.3.
DR RefSeq; XP_006496726.1; XM_006496663.3.
DR AlphaFoldDB; P50285; -.
DR SMR; P50285; -.
DR STRING; 10090.ENSMUSP00000037259; -.
DR iPTMnet; P50285; -.
DR PhosphoSitePlus; P50285; -.
DR SwissPalm; P50285; -.
DR jPOST; P50285; -.
DR MaxQB; P50285; -.
DR PaxDb; P50285; -.
DR PeptideAtlas; P50285; -.
DR PRIDE; P50285; -.
DR ProteomicsDB; 267488; -.
DR Antibodypedia; 20550; 90 antibodies from 23 providers.
DR DNASU; 14261; -.
DR Ensembl; ENSMUST00000046049; ENSMUSP00000037259; ENSMUSG00000040181.
DR GeneID; 14261; -.
DR KEGG; mmu:14261; -.
DR UCSC; uc007dgx.1; mouse.
DR CTD; 2326; -.
DR MGI; MGI:1310002; Fmo1.
DR VEuPathDB; HostDB:ENSMUSG00000040181; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160945; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; P50285; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; P50285; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 3474.
DR Reactome; R-MMU-217271; FMO oxidises nucleophiles.
DR BioGRID-ORCS; 14261; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Fmo1; mouse.
DR PRO; PR:P50285; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P50285; protein.
DR Bgee; ENSMUSG00000040181; Expressed in right kidney and 198 other tissues.
DR ExpressionAtlas; P50285; baseline and differential.
DR Genevisible; P50285; 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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IMP:MGI.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; ISO:MGI.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; IGI:MGI.
DR GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IGI:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0009404; P:toxin metabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic 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; IPR002253; Flavin_mOase_1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01121; FMOXYGENASE1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein;
KW Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 1"
FT /id="PRO_0000147640"
FT TRANSMEM 511..531
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 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
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"
FT SITE 208
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 532 AA; 59915 MW; C3CEDC7FC82DAC59 CRC64;
MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSSDLGGL WRFTEHVEEG RASLYKSVVS
NSSREMSCYP DFPFPEDYPN FVPNSLFLEY LKLYSTQFNL QRCIYFNTKV CSITKRPDFA
VSGQWEVVTV TNGKQNSAIF DAVMVCTGFL TNPHLPLDSF PGILTFKGEY FHSRQYKHPD
IFKDKRVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMIFMTRFQ
NMLRNLLPTP IVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVFIK
PSIKEVKENS VVFNNTPKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH
LPKPTLAVIG LIKPLGSMVP TGETQARWVV QVLKGATTLP PPSVMMEEVN ERKKNKHSGF
GLCYCKALQT DYITYIDDLL TSINAKPDLR AMLLTDPRLA LSIFFGPCTP YHFRLTGPGK
WEGARKAILT QWDRTVKVTK TRTIQESPSS FETLLKLFSF LALLIAVFLI FL
