FMO2_HUMAN
ID FMO2_HUMAN Reviewed; 535 AA.
AC Q99518; Q5EBX4; Q86U73; Q9BRX1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 5.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Flavin-containing monooxygenase 2 {ECO:0000305};
DE EC=1.14.13.- {ECO:0000269|PubMed:9804831};
DE AltName: Full=Dimethylaniline oxidase 2;
DE AltName: Full=FMO 1B1;
DE AltName: Full=Pulmonary flavin-containing monooxygenase 2;
DE Short=FMO 2;
GN Name=FMO2 {ECO:0000312|HGNC:HGNC:3770};
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] (ALLELE FMO2*2A), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POLYMORPHISM, AND
RP CHARACTERIZATION OF VARIANT 472-GLN--SER-535 DEL.
RC TISSUE=Lung;
RX PubMed=9804831; DOI=10.1074/jbc.273.46.30599;
RA Dolphin C.T., Beckett D.J., Janmohamed A., Cullingford T.E., Smith R.L.,
RA Shephard E.A., Phillips I.R.;
RT "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of
RT other primates, encodes a truncated, nonfunctional protein.";
RL J. Biol. Chem. 273:30599-30607(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE FMO2*2A), AND VARIANTS GLY-36;
RP TYR-69; SER-81; SER-182; LEU-195; GLN-238; GLY-314; THR-391 AND LYS-413.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE FMO2*2A).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE FMO2*1).
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] (ALLELE FMO2*2A).
RA Mural R.J., Istrail S., Sutton 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] (ALLELE FMO2*2A).
RC TISSUE=Skeletal muscle;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND POLYMORPHISM.
RX PubMed=11042094; DOI=10.1006/taap.2000.9050;
RA Whetstine J.R., Yueh M.F., McCarver D.G., Williams D.E., Park C.S.,
RA Kang J.H., Cha Y.N., Dolphin C.T., Shephard E.A., Phillips I.R.,
RA Hines R.N.;
RT "Ethnic differences in human flavin-containing monooxygenase 2 (FMO2)
RT polymorphisms: detection of expressed protein in African-Americans.";
RL Toxicol. Appl. Pharmacol. 168:216-224(2000).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15294458; DOI=10.1016/j.bcp.2004.05.051;
RA Henderson M.C., Krueger S.K., Siddens L.K., Stevens J.F., Williams D.E.;
RT "S-oxygenation of the thioether organophosphate insecticides phorate and
RT disulfoton by human lung flavin-containing monooxygenase 2.";
RL Biochem. Pharmacol. 68:959-967(2004).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15144220; DOI=10.1021/tx034253s;
RA Henderson M.C., Krueger S.K., Stevens J.F., Williams D.E.;
RT "Human flavin-containing monooxygenase form 2 S-oxygenation: sulfenic acid
RT formation from thioureas and oxidation of glutathione.";
RL Chem. Res. Toxicol. 17:633-640(2004).
RN [10]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18930751; DOI=10.1016/j.taap.2008.09.017;
RA Henderson M.C., Siddens L.K., Morre J.T., Krueger S.K., Williams D.E.;
RT "Metabolism of the anti-tuberculosis drug ethionamide by mouse and human
RT FMO1, FMO2 and FMO3 and mouse and human lung microsomes.";
RL Toxicol. Appl. Pharmacol. 233:420-427(2008).
RN [11]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18948378; DOI=10.1124/dmd.108.024158;
RA Francois A.A., Nishida C.R., de Montellano P.R., Phillips I.R.,
RA Shephard E.A.;
RT "Human flavin-containing monooxygenase 2.1 catalyzes oxygenation of the
RT antitubercular drugs thiacetazone and ethionamide.";
RL Drug Metab. Dispos. 37:178-186(2009).
RN [12]
RP SUMOYLATION AT LYS-492.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
RN [13]
RP VARIANTS GLY-36; ILE-59; SER-182; LEU-195; GLN-238; THR-391 AND LYS-413.
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).
RN [14]
RP POLYMORPHISM.
RX PubMed=18794725; DOI=10.1097/fpc.0b013e3283097311;
RA Veeramah K.R., Thomas M.G., Weale M.E., Zeitlyn D., Tarekegn A., Bekele E.,
RA Mendell N.R., Shephard E.A., Bradman N., Phillips I.R.;
RT "The potentially deleterious functional variant flavin-containing
RT monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa.";
RL Pharmacogenet. Genomics 18:877-886(2008).
CC -!- FUNCTION: Catalyzes the oxidative metabolism of numerous xenobiotics,
CC including mainly therapeutic drugs and insecticides that contain a soft
CC nucleophile, most commonly nitrogen and sulfur and participates to
CC their bioactivation (PubMed:9804831, PubMed:15294458, PubMed:15144220,
CC PubMed:18948378, PubMed:18930751). Specifically catalyzes S-oxygenation
CC of sulfur derived compounds such as thioureas-derived compounds,
CC thioetherorganophosphates to their sulfenic acid (PubMed:9804831,
CC PubMed:15144220). In vitro, catalyzes S-oxygenation of the second-line
CC antitubercular drugs thiacetazone (TAZ) and ethionamide (ETA), forming
CC a sulfinic acid and a carbodiimide via a postulated sulfenic acid
CC intermediate (PubMed:18948378, PubMed:18930751). Also catalyzes S-
CC oxygenation of the thioether-containing organophosphate insecticides,
CC phorate and disulfoton (PubMed:15294458). {ECO:0000269|PubMed:15144220,
CC ECO:0000269|PubMed:15294458, ECO:0000269|PubMed:18930751,
CC ECO:0000269|PubMed:18948378, ECO:0000269|PubMed:9804831}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=411 uM for methimazole {ECO:0000269|PubMed:9804831};
CC KM=27 uM for thiourea {ECO:0000269|PubMed:15144220};
CC KM=14 uM for ethylenethiourea {ECO:0000269|PubMed:15144220};
CC KM=29 uM for N-phenylthiourea {ECO:0000269|PubMed:15144220};
CC KM=42 uM for ANTU {ECO:0000269|PubMed:15144220};
CC KM=5.8 uM for thioacetazone {ECO:0000269|PubMed:18948378};
CC KM=575.75 uM for methimazole {ECO:0000269|PubMed:18948378};
CC KM=261 uM for ethionamide {ECO:0000269|PubMed:18930751};
CC KM=57 uM for phorate {ECO:0000269|PubMed:15294458};
CC KM=32 uM for disulfoton {ECO:0000269|PubMed:15294458};
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in lung (at protein level). Expressed
CC predominantly in lung, and at a much lesser extent in kidney. Also
CC expressed in fetal lung, but not in liver, kidney and brain.
CC {ECO:0000269|PubMed:11042094, ECO:0000269|PubMed:9804831}.
CC -!- POLYMORPHISM: The sequence shown is that of the allele FMO2*1. FMO2*2A
CC is the major allele in the human population, however it encodes a
CC truncated and catalytically inactive protein (PubMed:9804831). FMO2*2A
CC occurs in essentially 100% of Caucasians and Asians (PubMed:9804831).
CC FMO2*1 is present at a frequency of approximately 4% to 13% in the
CC sample of population of African descent (PubMed:9804831,
CC PubMed:11042094, PubMed:18794725). {ECO:0000269|PubMed:11042094,
CC ECO:0000269|PubMed:18794725, ECO:0000269|PubMed:9804831}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fmo2/";
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DR EMBL; Y09267; CAA70462.1; -; mRNA.
DR EMBL; AY916056; AAW82431.1; -; Genomic_DNA.
DR EMBL; BT006979; AAP35625.1; -; mRNA.
DR EMBL; AL021026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90889.1; -; Genomic_DNA.
DR EMBL; BC005894; AAH05894.1; -; mRNA.
DR CCDS; CCDS1293.2; -.
DR RefSeq; NP_001451.2; NM_001460.4.
DR AlphaFoldDB; Q99518; -.
DR SMR; Q99518; -.
DR BioGRID; 108614; 9.
DR IntAct; Q99518; 4.
DR MINT; Q99518; -.
DR STRING; 9606.ENSP00000209929; -.
DR ChEMBL; CHEMBL3542432; -.
DR iPTMnet; Q99518; -.
DR PhosphoSitePlus; Q99518; -.
DR BioMuta; FMO2; -.
DR DMDM; 327478599; -.
DR MassIVE; Q99518; -.
DR PaxDb; Q99518; -.
DR PeptideAtlas; Q99518; -.
DR PRIDE; Q99518; -.
DR ProteomicsDB; 78307; -.
DR Antibodypedia; 34377; 149 antibodies from 25 providers.
DR DNASU; 2327; -.
DR Ensembl; ENST00000209929.10; ENSP00000209929.8; ENSG00000094963.14.
DR GeneID; 2327; -.
DR KEGG; hsa:2327; -.
DR MANE-Select; ENST00000209929.10; ENSP00000209929.8; NM_001460.5; NP_001451.2.
DR UCSC; uc057ngi.1; human.
DR CTD; 2327; -.
DR DisGeNET; 2327; -.
DR GeneCards; FMO2; -.
DR HGNC; HGNC:3770; FMO2.
DR HPA; ENSG00000094963; Tissue enhanced (adipose tissue, esophagus, lung).
DR MIM; 603955; gene.
DR neXtProt; NX_Q99518; -.
DR OpenTargets; ENSG00000094963; -.
DR PharmGKB; PA164741534; -.
DR VEuPathDB; HostDB:ENSG00000094963; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000161099; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; Q99518; -.
DR OMA; DCYERET; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q99518; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 2681.
DR PathwayCommons; Q99518; -.
DR Reactome; R-HSA-217271; FMO oxidises nucleophiles.
DR SignaLink; Q99518; -.
DR BioGRID-ORCS; 2327; 3 hits in 1063 CRISPR screens.
DR ChiTaRS; FMO2; human.
DR GeneWiki; FMO2; -.
DR GenomeRNAi; 2327; -.
DR Pharos; Q99518; Tbio.
DR PRO; PR:Q99518; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99518; protein.
DR Bgee; ENSG00000094963; Expressed in pericardium and 170 other tissues.
DR ExpressionAtlas; Q99518; baseline and differential.
DR Genevisible; Q99518; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
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; IDA:BHF-UCL.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0006739; P:NADP metabolic process; IDA:BHF-UCL.
DR GO; GO:0070995; P:NADPH oxidation; IDA:UniProtKB.
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:0072592; P:oxygen metabolic process; IEA:Ensembl.
DR GO; GO:0009404; P:toxin metabolic process; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:BHF-UCL.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002254; Flavin_mOase_2.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01122; FMOXYGENASE2.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Isopeptide bond;
KW Magnesium; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P17635"
FT CHAIN 2..535
FT /note="Flavin-containing monooxygenase 2"
FT /id="PRO_0000147646"
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 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:P17635"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:20388717"
FT VARIANT 36
FT /note="D -> G (in dbSNP:rs2020870)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_014840"
FT VARIANT 59
FT /note="V -> I (in dbSNP:rs55708639)"
FT /evidence="ECO:0000269|PubMed:12527699"
FT /id="VAR_015361"
FT VARIANT 69
FT /note="F -> Y (in dbSNP:rs28745274)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022185"
FT VARIANT 81
FT /note="F -> S (in dbSNP:rs2020860)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_014841"
FT VARIANT 182
FT /note="F -> S (in dbSNP:rs2307492)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_014842"
FT VARIANT 195
FT /note="S -> L (in dbSNP:rs2020862)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_014843"
FT VARIANT 238
FT /note="R -> Q (in dbSNP:rs28369895)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_015362"
FT VARIANT 314
FT /note="E -> G (in dbSNP:rs2020863)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022186"
FT VARIANT 391
FT /note="R -> T (in dbSNP:rs28369899)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_015363"
FT VARIANT 413
FT /note="N -> K (in dbSNP:rs2020865)"
FT /evidence="ECO:0000269|PubMed:12527699, ECO:0000269|Ref.2"
FT /id="VAR_014844"
FT VARIANT 472..535
FT /note="Missing (in allele FMO2*2A; loss of monooxygenase
FT activity)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9804831, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5"
FT /id="VAR_081836"
FT CONFLICT 71
FT /note="D -> DD (in Ref. 2; AAW82431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 60907 MW; 39A5587AC7BF50B8 CRC64;
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVVT
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
SSGQWKVVTQ SNGKEQSAVF DAVMVCSGHH ILPHIPLKSF PGMERFKGQY FHSRQYKHPD
GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV MSRISEDGYP WDSVFHTRFR
SMLRNVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
LDKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIDLF
GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ
WEGARNAIFT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS
