FMO1_RAT
ID FMO1_RAT Reviewed; 532 AA.
AC P36365; Q6P7Q5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE EC=1.14.13.8 {ECO:0000269|PubMed:8504165};
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8504165; DOI=10.1016/0167-4781(93)90177-f;
RA Itoh K., Kimura T., Yokoi T., Itoh S., Kamataki T.;
RT "Rat liver flavin-containing monooxygenase (FMO): cDNA cloning and
RT expression in yeast.";
RL Biochim. Biophys. Acta 1173:165-171(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP PROTEIN SEQUENCE OF 34-42 AND 52-56.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9094723; DOI=10.1016/s0092-8674(00)80191-9;
RA Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.;
RT "Protein interactions regulating vesicle transport between the endoplasmic
RT reticulum and Golgi apparatus in mammalian cells.";
RL Cell 89:149-158(1997).
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 {ECO:0000269|PubMed:8504165}.
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 Evidence={ECO:0000269|PubMed:8504165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC Evidence={ECO:0000305|PubMed:8504165};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:8504165};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, lung and kidney and to a lesser
CC extent in the heart and brain. {ECO:0000269|PubMed:8504165}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; M84719; AAA41165.1; -; mRNA.
DR EMBL; BC061567; AAH61567.1; -; mRNA.
DR PIR; S33758; S33758.
DR RefSeq; NP_036924.1; NM_012792.1.
DR RefSeq; XP_006250207.1; XM_006250145.3.
DR RefSeq; XP_006250208.1; XM_006250146.3.
DR AlphaFoldDB; P36365; -.
DR SMR; P36365; -.
DR STRING; 10116.ENSRNOP00000044613; -.
DR iPTMnet; P36365; -.
DR PhosphoSitePlus; P36365; -.
DR PaxDb; P36365; -.
DR PRIDE; P36365; -.
DR Ensembl; ENSRNOT00000041908; ENSRNOP00000044613; ENSRNOG00000034191.
DR GeneID; 25256; -.
DR KEGG; rno:25256; -.
DR UCSC; RGD:2622; rat.
DR CTD; 2326; -.
DR RGD; 2622; Fmo1.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160945; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; P36365; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; P36365; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 5301.
DR Reactome; R-RNO-217271; FMO oxidises nucleophiles.
DR SABIO-RK; P36365; -.
DR PRO; PR:P36365; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000034191; Expressed in adult mammalian kidney and 16 other tissues.
DR Genevisible; P36365; RN.
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; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IDA:RGD.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0070995; P:NADPH oxidation; ISO:RGD.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISO:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
DR GO; GO:0009404; P:toxin metabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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_0000147643"
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"
FT CONFLICT 141
FT /note="D -> A (in Ref. 1; AAA41165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 59825 MW; 188EABAF96653977 CRC64;
MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSCDLGGL WRFTEHVEEG RASLYNSVVS
NSSKEMSCYS DFPFPEDYPN FVPNSLFLEY LQLYATQFNL LRCIYFNTKV CSITKRPDFA
VSGQWEVVTV CQGKQSSDTF DAVMVCTGFL TNPHLPLDSF PGIQTFKGQY FHSRQYKHPD
VFKDKRVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMIFMTRFQ
NMLRNLLPTP VVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVLIK
PSIKEVKENS VVFNNTPKEE PIDVIVFATG YSFAFPFLDE SIVKVEDGQA SLYKYIFPAH
LPKPTLAVIG LIKPLGSMIP TGETQARWVV QVLKGATTLP PPSVMMKEVN ERKKNKHSGF
GLCYCKALQS DYITYIDDLL TSINAKPDLR AMLLTDPRLA LSIFFGPCTP YHFRLTGPGK
WEGARKAILT QWDRTVNVTK TRTVQETPST FETLLKLFSF LALLVAVFFI FL
