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Entry version 205 (23 Feb 2022)
Sequence version 5 (23 Jan 2007)
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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

FMO3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Essential hepatic enzyme that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds (PubMed:10759686, PubMed:30381441).

Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite (PubMed:9776311).

TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thrombus formation (PubMed:29981269).

By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=21 µM for trimethylamine (at pH 8.5)2 Publications
  2. KM=31 µM for trimethylamine (at pH 7.4 and 37 degrees Celsius)2 Publications
  3. KM=43 µM for benzydamine (at pH 7.4 and 37 degrees Celsius)2 Publications
  4. KM=55.7 µM for ethylenethiourea (at pH 8.5)2 Publications
  5. KM=71.8 µM for methimazole (at pH 8.5)2 Publications
  6. KM=150.1 µM for sulindac (at pH 8.5)2 Publications
  7. KM=248 µM for methyl p-tolyl sulfide (at pH 7.4 and 37 degrees Celsius)2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei32FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi9 – 13FADBy similarity5
Nucleotide bindingi40 – 41FADBy similarity2
Nucleotide bindingi60 – 61NADPBy similarity2
Nucleotide bindingi61 – 62FADBy similarity2
Nucleotide bindingi195 – 198NADPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.13.148, 2681
1.14.13.8, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P31513

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-217271, FMO oxidises nucleophiles
R-HSA-5579019, Defective FMO3 causes TMAU

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P31513

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P31513

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 3 (EC:1.14.13.81 Publication, EC:1.14.14.731 Publication)
Alternative name(s):
Dimethylaniline oxidase 3
FMO II
FMO form 2
Hepatic flavin-containing monooxygenase 3
Short name:
FMO 3
Trimethylamine monooxygenase (EC:1.14.13.148)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FMO3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3771, FMO3

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
136132, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P31513

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000007933

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei510 – 530HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Trimethylaminuria (TMAU)6 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionInborn error of metabolism associated with an offensive body odor and caused by deficiency of FMO-mediated N-oxidation of amino-trimethylamine (TMA) derived from foodstuffs. Affected individuals excrete relatively large amounts of TMA in their urine, sweat, and breath, and exhibit a fishy body odor characteristic of the malodorous free amine.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03730632E → K in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549320EnsemblClinVar.1
Natural variantiVAR_00814652A → T in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549321EnsemblClinVar.1
Natural variantiVAR_03730761N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. 2 PublicationsCorresponds to variant dbSNP:rs72549322EnsemblClinVar.1
Natural variantiVAR_00242366M → I in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549323EnsemblClinVar.1
Natural variantiVAR_002424153P → L in TMAU; 90% reduction in catalytic efficiency toward trimethylamine and benzydamine; 34% reduction in catalytic efficiency toward methyl p-tolyl sulfide; nearly no effect on affinity for these substrates. 3 PublicationsCorresponds to variant dbSNP:rs72549326EnsemblClinVar.1
Natural variantiVAR_008147387R → L in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549331EnsemblClinVar.1
Natural variantiVAR_037308434M → I in TMAU; profoundly alters enzyme function. 1 PublicationCorresponds to variant dbSNP:rs72549332EnsemblClinVar.1
Natural variantiVAR_008145492R → W in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549334EnsemblClinVar.1

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

More...
DisGeNETi
2328

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
FMO3

MalaCards human disease database

More...
MalaCardsi
FMO3
MIMi602079, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000007933

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
35056, NON RARE IN EUROPE: Trimethylaminuria
468726, Severe primary trimethylaminuria

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA166

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P31513, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3430864

Drug and drug target database

More...
DrugBanki
DB00918, Almotriptan
DB00501, Cimetidine
DB00363, Clozapine
DB00250, Dapsone
DB01254, Dasatinib
DB12500, Fedratinib
DB00763, Methimazole
DB11828, Neratinib
DB00334, Olanzapine
DB00768, Olopatadine
DB12278, Propiverine
DB15305, Risdiplam
DB00675, Tamoxifen
DB13609, Umifenovir
DB05294, Vandetanib
DB00582, Voriconazole

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FMO3

Domain mapping of disease mutations (DMDM)

More...
DMDMi
6166183

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001476542 – 532Dimethylaniline monooxygenase [N-oxide-forming] 3Add BLAST531

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei401PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P31513

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P31513

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P31513

PeptideAtlas

More...
PeptideAtlasi
P31513

PRoteomics IDEntifications database

More...
PRIDEi
P31513

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
54793

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P31513

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P31513

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Liver.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000007933, Expressed in liver and 142 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P31513, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P31513, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000007933, Tissue enriched (liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
108615, 5 interactors

Protein interaction database and analysis system

More...
IntActi
P31513, 4 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000356729

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P31513, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P31513

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1399, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000161339

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_006909_8_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P31513

Identification of Orthologs from Complete Genome Data

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OMAi
AISDWWY

Database of Orthologous Groups

More...
OrthoDBi
405736at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P31513

TreeFam database of animal gene trees

More...
TreeFami
TF105285

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.50.50.60, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR000960, Flavin_mOase
IPR020946, Flavin_mOase-like
IPR002255, Flavin_mOase_3

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00743, FMO-like, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000332, FMO, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00370, FMOXYGENASE
PR01123, FMOXYGENASE3

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51905, SSF51905, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P31513-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG
60 70 80 90 100
RASIYKSVFS NSSKEMMCFP DFPFPDDFPN FMHNSKIQEY IIAFAKEKNL
110 120 130 140 150
LKYIQFKTFV SSVNKHPDFA TTGQWDVTTE RDGKKESAVF DAVMVCSGHH
160 170 180 190 200
VYPNLPKESF PGLNHFKGKC FHSRDYKEPG VFNGKRVLVV GLGNSGCDIA
210 220 230 240 250
TELSRTAEQV MISSRSGSWV MSRVWDNGYP WDMLLVTRFG TFLKNNLPTA
260 270 280 290 300
ISDWLYVKQM NARFKHENYG LMPLNGVLRK EPVFNDELPA SILCGIVSVK
310 320 330 340 350
PNVKEFTETS AIFEDGTIFE GIDCVIFATG YSFAYPFLDE SIIKSRNNEI
360 370 380 390 400
ILFKGVFPPL LEKSTIAVIG FVQSLGAAIP TVDLQSRWAA QVIKGTCTLP
410 420 430 440 450
SMEDMMNDIN EKMEKKRKWF GKSETIQTDY IVYMDELSSF IGAKPNIPWL
460 470 480 490 500
FLTDPKLAME VYFGPCSPYQ FRLVGPGQWP GARNAILTQW DRSLKPMQTR
510 520 530
VVGRLQKPCF FFHWLKLFAI PILLIAVFLV LT
Length:532
Mass (Da):60,033
Last modified:January 23, 2007 - v5
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i729E41D53EFC4110
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
V9GZ60V9GZ60_HUMAN
Flavin-containing monooxygenase
FMO3
218Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GYP3V9GYP3_HUMAN
Flavin-containing monooxygenase
FMO3
48Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti298S → T in AAA86284 (PubMed:1542660).Curated1
Sequence conflicti369I → L in AAA86284 (PubMed:1542660).Curated1
Sequence conflicti400 – 405PSMEDM → GPFYGKTL in AAA86284 (PubMed:1542660).Curated6
Sequence conflicti410N → I in AAA86284 (PubMed:1542660).Curated1
Sequence conflicti418 – 419KW → ANG in AAA86284 (PubMed:1542660).Curated2
Sequence conflicti444 – 445KP → T in AAA86284 (PubMed:1542660).Curated2
Sequence conflicti449W → M in AAA86284 (PubMed:1542660).Curated1
Sequence conflicti454D → G in AAA86284 (PubMed:1542660).Curated1
Sequence conflicti461 – 462VY → L in AAA86284 (PubMed:1542660).Curated2
Sequence conflicti478Q → S in AAA86284 (PubMed:1542660).Curated1
Sequence conflicti486I → M in CAA87632 (PubMed:8654418).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04270524E → D Modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac. 1 Publication1
Natural variantiVAR_03730632E → K in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549320EnsemblClinVar.1
Natural variantiVAR_00814652A → T in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549321EnsemblClinVar.1
Natural variantiVAR_04270661N → K Loss of activity. 1 Publication1
Natural variantiVAR_03730761N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. 2 PublicationsCorresponds to variant dbSNP:rs72549322EnsemblClinVar.1
Natural variantiVAR_00242366M → I in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549323EnsemblClinVar.1
Natural variantiVAR_015364132D → H2 PublicationsCorresponds to variant dbSNP:rs12072582EnsemblClinVar.1
Natural variantiVAR_002424153P → L in TMAU; 90% reduction in catalytic efficiency toward trimethylamine and benzydamine; 34% reduction in catalytic efficiency toward methyl p-tolyl sulfide; nearly no effect on affinity for these substrates. 3 PublicationsCorresponds to variant dbSNP:rs72549326EnsemblClinVar.1
Natural variantiVAR_002425158E → K 35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively. 6 PublicationsCorresponds to variant dbSNP:rs2266782EnsemblClinVar.1
Natural variantiVAR_018345198D → E1 PublicationCorresponds to variant dbSNP:rs529940450Ensembl.1
Natural variantiVAR_018346205R → C2 PublicationsCorresponds to variant dbSNP:rs28363549EnsemblClinVar.1
Natural variantiVAR_002426257V → M 65% increase in catalytic efficiency toward trimethylamine and 60% reduction toward benzydamine and methyl p-tolyl sulfide. 6 PublicationsCorresponds to variant dbSNP:rs1736557EnsemblClinVar.1
Natural variantiVAR_014845277V → A1 PublicationCorresponds to variant dbSNP:rs2066530EnsemblClinVar.1
Natural variantiVAR_002427308E → G 16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide. 5 PublicationsCorresponds to variant dbSNP:rs2266780EnsemblClinVar.1
Natural variantiVAR_015365360L → P2 PublicationsCorresponds to variant dbSNP:rs28363581EnsemblClinVar.1
Natural variantiVAR_014846362E → Q2 PublicationsCorresponds to variant dbSNP:rs2066532EnsemblClinVar.1
Natural variantiVAR_008147387R → L in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549331EnsemblClinVar.1
Natural variantiVAR_042707416K → N 2-fold decrease in affinity for trimethylamine; 3-fold decrease in catalytic efficiency toward methimazole; 3-fold increase in catalytic efficiency toward sulindac; 30% increase in catalytic efficiency toward ethylenethiourea. 1 PublicationCorresponds to variant dbSNP:rs774785217Ensembl.1
Natural variantiVAR_037308434M → I in TMAU; profoundly alters enzyme function. 1 PublicationCorresponds to variant dbSNP:rs72549332EnsemblClinVar.1
Natural variantiVAR_008145492R → W in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549334EnsemblClinVar.1
Natural variantiVAR_015366503G → R1 PublicationCorresponds to variant dbSNP:rs72549335EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M83772 mRNA Translation: AAA86284.1
Z47552 mRNA Translation: CAA87632.1
U39967 U39966 Genomic DNA Translation: AAC51932.1
AY895830 Genomic DNA Translation: AAW65372.1
AK313197 mRNA Translation: BAG36013.1
AL021026 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW90887.1
BC032016 mRNA Translation: AAH32016.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1292.1

Protein sequence database of the Protein Information Resource

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PIRi
A38228
S62367, S51130

NCBI Reference Sequences

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RefSeqi
NP_001002294.1, NM_001002294.2
NP_001306102.1, NM_001319173.1
NP_001306103.1, NM_001319174.1
NP_008825.4, NM_006894.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000367755; ENSP00000356729; ENSG00000007933

Database of genes from NCBI RefSeq genomes

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GeneIDi
2328

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2328

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

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MANE-Selecti
ENST00000367755.9; ENSP00000356729.4; NM_001002294.3; NP_001002294.1

UCSC genome browser

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UCSCi
uc001ghi.3, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Protein Spotlight

A case for discomfort - Issue 149 of June 2013

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83772 mRNA Translation: AAA86284.1
Z47552 mRNA Translation: CAA87632.1
U39967 U39966 Genomic DNA Translation: AAC51932.1
AY895830 Genomic DNA Translation: AAW65372.1
AK313197 mRNA Translation: BAG36013.1
AL021026 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW90887.1
BC032016 mRNA Translation: AAH32016.1
CCDSiCCDS1292.1
PIRiA38228
S62367, S51130
RefSeqiNP_001002294.1, NM_001002294.2
NP_001306102.1, NM_001319173.1
NP_001306103.1, NM_001319174.1
NP_008825.4, NM_006894.5

3D structure databases

SMRiP31513
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi108615, 5 interactors
IntActiP31513, 4 interactors
STRINGi9606.ENSP00000356729

Chemistry databases

ChEMBLiCHEMBL3430864
DrugBankiDB00918, Almotriptan
DB00501, Cimetidine
DB00363, Clozapine
DB00250, Dapsone
DB01254, Dasatinib
DB12500, Fedratinib
DB00763, Methimazole
DB11828, Neratinib
DB00334, Olanzapine
DB00768, Olopatadine
DB12278, Propiverine
DB15305, Risdiplam
DB00675, Tamoxifen
DB13609, Umifenovir
DB05294, Vandetanib
DB00582, Voriconazole

PTM databases

iPTMnetiP31513
PhosphoSitePlusiP31513

Genetic variation databases

BioMutaiFMO3
DMDMi6166183

Proteomic databases

jPOSTiP31513
MassIVEiP31513
PaxDbiP31513
PeptideAtlasiP31513
PRIDEiP31513
ProteomicsDBi54793

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
2219, 357 antibodies from 32 providers

The DNASU plasmid repository

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DNASUi
2328

Genome annotation databases

EnsembliENST00000367755; ENSP00000356729; ENSG00000007933
GeneIDi2328
KEGGihsa:2328
MANE-SelectiENST00000367755.9; ENSP00000356729.4; NM_001002294.3; NP_001002294.1
UCSCiuc001ghi.3, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2328
DisGeNETi2328

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FMO3
GeneReviewsiFMO3
HGNCiHGNC:3771, FMO3
HPAiENSG00000007933, Tissue enriched (liver)
MalaCardsiFMO3
MIMi136132, gene
602079, phenotype
neXtProtiNX_P31513
OpenTargetsiENSG00000007933
Orphaneti35056, NON RARE IN EUROPE: Trimethylaminuria
468726, Severe primary trimethylaminuria
PharmGKBiPA166
VEuPathDBiHostDB:ENSG00000007933

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1399, Eukaryota
GeneTreeiENSGT00940000161339
HOGENOMiCLU_006909_8_2_1
InParanoidiP31513
OMAiAISDWWY
OrthoDBi405736at2759
PhylomeDBiP31513
TreeFamiTF105285

Enzyme and pathway databases

BRENDAi1.14.13.148, 2681
1.14.13.8, 2681
PathwayCommonsiP31513
ReactomeiR-HSA-217271, FMO oxidises nucleophiles
R-HSA-5579019, Defective FMO3 causes TMAU
SABIO-RKiP31513
SignaLinkiP31513

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
2328, 4 hits in 1037 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
FMO3, human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Flavin_containing_monooxygenase_3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2328
PharosiP31513, Tbio

Protein Ontology

More...
PROi
PR:P31513
RNActiP31513, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000007933, Expressed in liver and 142 other tissues
ExpressionAtlasiP31513, baseline and differential
GenevisibleiP31513, HS

Family and domain databases

Gene3Di3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR000960, Flavin_mOase
IPR020946, Flavin_mOase-like
IPR002255, Flavin_mOase_3
PfamiView protein in Pfam
PF00743, FMO-like, 1 hit
PIRSFiPIRSF000332, FMO, 1 hit
PRINTSiPR00370, FMOXYGENASE
PR01123, FMOXYGENASE3
SUPFAMiSSF51905, SSF51905, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFMO3_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P31513
Secondary accession number(s): B2R816, Q14854, Q8N5N5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 205 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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