FMO1_HUMAN
ID FMO1_HUMAN Reviewed; 532 AA.
AC Q01740; A8K248; B7Z3P4; Q5QPT2; Q9UJC2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE EC=1.14.13.8;
DE AltName: Full=Dimethylaniline oxidase 1;
DE AltName: Full=Fetal hepatic flavin-containing monooxygenase 1;
DE Short=FMO 1;
GN Name=FMO1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1712018; DOI=10.1016/s0021-9258(18)98908-8;
RA Dolphin C.T., Shephard E.A., Povey S., Palmer C.N.A., Ziegler D.M.,
RA Ayesh R., Smith R.L., Phillips I.R.;
RT "Cloning, primary sequence, and chromosomal mapping of a human flavin-
RT containing monooxygenase (FMO1).";
RL J. Biol. Chem. 266:12379-12385(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-223; THR-227; VAL-303;
RP VAL-322; LEU-327; ARG-373 AND HIS-474.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [7]
RP VARIANTS GLN-97; THR-303 AND VAL-303.
RX PubMed=12527699; DOI=10.1124/dmd.31.2.187;
RA Furnes B., Feng J., Sommer S.S., Schlenk D.;
RT "Identification of novel variants of the flavin-containing monooxygenase
RT gene family in African Americans.";
RL Drug Metab. Dispos. 31:187-193(2003).
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 -!- INTERACTION:
CC Q01740; O43889-2: CREB3; NbExp=3; IntAct=EBI-12701460, EBI-625022;
CC Q01740; Q7Z429: GRINA; NbExp=3; IntAct=EBI-12701460, EBI-2832909;
CC Q01740; O95214: LEPROTL1; NbExp=3; IntAct=EBI-12701460, EBI-750776;
CC Q01740; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-12701460, EBI-373355;
CC Q01740; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12701460, EBI-7545592;
CC Q01740; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12701460, EBI-18159983;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01740-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01740-2; Sequence=VSP_054543;
CC -!- TISSUE SPECIFICITY: Expressed mainly in fetal and adult liver.
CC {ECO:0000269|PubMed:1712018}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fmo1/";
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DR EMBL; M64082; AAA52457.1; -; mRNA.
DR EMBL; AY879266; AAW56076.1; -; Genomic_DNA.
DR EMBL; AK290113; BAF82802.1; -; mRNA.
DR EMBL; AK296198; BAH12280.1; -; mRNA.
DR EMBL; AL021026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90892.1; -; Genomic_DNA.
DR EMBL; BC047129; AAH47129.1; -; mRNA.
DR CCDS; CCDS1294.1; -. [Q01740-1]
DR CCDS; CCDS60351.1; -. [Q01740-2]
DR PIR; A40876; A40876.
DR RefSeq; NP_001269621.1; NM_001282692.1.
DR RefSeq; NP_001269622.1; NM_001282693.1. [Q01740-1]
DR RefSeq; NP_001269623.1; NM_001282694.1. [Q01740-2]
DR RefSeq; NP_002012.1; NM_002021.2. [Q01740-1]
DR AlphaFoldDB; Q01740; -.
DR SMR; Q01740; -.
DR BioGRID; 108613; 9.
DR IntAct; Q01740; 7.
DR STRING; 9606.ENSP00000481732; -.
DR ChEMBL; CHEMBL3430872; -.
DR DrugBank; DB00185; Cevimeline.
DR DrugBank; DB00501; Cimetidine.
DR DrugBank; DB04871; Lorcaserin.
DR DrugBank; DB00768; Olopatadine.
DR DrugBank; DB12278; Propiverine.
DR DrugBank; DB15305; Risdiplam.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB13609; Umifenovir.
DR DrugBank; DB05294; Vandetanib.
DR DrugBank; DB00582; Voriconazole.
DR iPTMnet; Q01740; -.
DR PhosphoSitePlus; Q01740; -.
DR BioMuta; FMO1; -.
DR DMDM; 399505; -.
DR jPOST; Q01740; -.
DR MassIVE; Q01740; -.
DR PaxDb; Q01740; -.
DR PeptideAtlas; Q01740; -.
DR PRIDE; Q01740; -.
DR ProteomicsDB; 57985; -. [Q01740-1]
DR Antibodypedia; 20550; 90 antibodies from 23 providers.
DR DNASU; 2326; -.
DR Ensembl; ENST00000354841.4; ENSP00000346901.4; ENSG00000010932.17. [Q01740-1]
DR Ensembl; ENST00000367750.7; ENSP00000356724.3; ENSG00000010932.17. [Q01740-1]
DR Ensembl; ENST00000402921.6; ENSP00000385543.2; ENSG00000010932.17. [Q01740-2]
DR Ensembl; ENST00000617670.6; ENSP00000481732.1; ENSG00000010932.17. [Q01740-1]
DR GeneID; 2326; -.
DR KEGG; hsa:2326; -.
DR MANE-Select; ENST00000617670.6; ENSP00000481732.1; NM_001282693.2; NP_001269622.1.
DR UCSC; uc001ghl.5; human. [Q01740-1]
DR CTD; 2326; -.
DR DisGeNET; 2326; -.
DR GeneCards; FMO1; -.
DR HGNC; HGNC:3769; FMO1.
DR HPA; ENSG00000010932; Tissue enriched (kidney).
DR MIM; 136130; gene.
DR neXtProt; NX_Q01740; -.
DR OpenTargets; ENSG00000010932; -.
DR PharmGKB; PA165; -.
DR VEuPathDB; HostDB:ENSG00000010932; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160945; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; Q01740; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q01740; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 2681.
DR PathwayCommons; Q01740; -.
DR Reactome; R-HSA-217271; FMO oxidises nucleophiles.
DR SABIO-RK; Q01740; -.
DR SignaLink; Q01740; -.
DR BioGRID-ORCS; 2326; 41 hits in 1071 CRISPR screens.
DR GeneWiki; Flavin_containing_monooxygenase_1; -.
DR GenomeRNAi; 2326; -.
DR Pharos; Q01740; Tbio.
DR PRO; PR:Q01740; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q01740; protein.
DR Bgee; ENSG00000010932; Expressed in nephron tubule and 134 other tissues.
DR ExpressionAtlas; Q01740; baseline and differential.
DR Genevisible; Q01740; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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; IDA:MGI.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IDA:BHF-UCL.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0070995; P:NADPH oxidation; IDA:BHF-UCL.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0006082; P:organic acid metabolic process; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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 Acetylation; Alternative splicing; Endoplasmic reticulum; FAD;
KW Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16549"
FT CHAIN 2..532
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 1"
FT /id="PRO_0000147639"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P16549"
FT VAR_SEQ 45..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054543"
FT VARIANT 97
FT /note="H -> Q (in dbSNP:rs56841822)"
FT /evidence="ECO:0000269|PubMed:12527699"
FT /id="VAR_015358"
FT VARIANT 223
FT /note="R -> Q (in dbSNP:rs16864310)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022204"
FT VARIANT 227
FT /note="S -> T"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022205"
FT VARIANT 303
FT /note="I -> T (in dbSNP:rs28360418)"
FT /evidence="ECO:0000269|PubMed:12527699"
FT /id="VAR_015359"
FT VARIANT 303
FT /note="I -> V (in dbSNP:rs16864314)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_015360"
FT VARIANT 322
FT /note="I -> V (in dbSNP:rs28360419)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022206"
FT VARIANT 327
FT /note="F -> L (in dbSNP:rs28360420)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022207"
FT VARIANT 373
FT /note="K -> R (in dbSNP:rs28360421)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022208"
FT VARIANT 474
FT /note="R -> H (in dbSNP:rs28360433)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022209"
SQ SEQUENCE 532 AA; 60311 MW; 627B855F38C2EB6D CRC64;
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS
NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANHFDL LKHIQFKTKV CSVTKCSDSA
VSGQWEVVTM HEEKQESAIF DAVMVCTGFL TNPYLPLDSF PGINAFKGQY FHSRQYKHPD
IFKDKRVLVI GMGNSGTDIA VEASHLAEKV FLSTTGGGWV ISRIFDSGYP WDMVFMTRFQ
NMLRNSLPTP IVTWLMERKI NNWLNHANYG LIPEDRTQLK EFVLNDELPG RIITGKVFIR
PSIKEVKENS VIFNNTSKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH
LQKPTLAIIG LIKPLGSMIP TGETQARWAV RVLKGVNKLP PPSVMIEEIN ARKENKPSWF
GLCYCKALQS DYITYIDELL TYINAKPNLF SMLLTDPHLA LTVFFGPCSP YQFRLTGPGK
WEGARNAIMT QWDRTFKVIK ARVVQESPSP FESFLKVFSF LALLVAIFLI FL
