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UniProtKB/Swiss-Prot entry O60774


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FMO6_HUMAN
Primary accession number O60774
Secondary accession numbers None
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Putative dimethylaniline monooxygenase [N-oxide-forming] 6
Synonyms EC 1.14.13.8
Flavin-containing monooxygenase 6
FMO 6
Dimethylaniline oxidase 6
Gene name
Name: FMO6
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[2]
ANALYSIS OF SPLICE VARIANTS.
DOI=10.1124/mol.62.2.320; PubMed=12130684 [NCBI, ExPASy, EBI, Israel, Japan]
Hines R.N., Hopp K.A., Franco J., Saeian K., Begun F.P.;
"Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase.";
Mol. Pharmacol. 62:320-325(2002).
[3]
VARIANTS ILE-127 AND ILE-257, AND POLYMORPHISM IN POSITION 105.
DOI=10.1124/dmd.31.2.187; PubMed=12527699 [NCBI, ExPASy, EBI, Israel, Japan]
Furnes B., Feng J., Sommer S.S., Schlenk D.;
"Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans.";
Drug Metab. Dispos. 31:187-193(2003).
Comments
  • FUNCTION: It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full length transcripts.
  • CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
  • COFACTOR: FAD (By similarity).
  • SUBCELLULAR LOCATION: Microsome membrane (By similarity). Endoplasmic reticulum membrane (By similarity).
  • POLYMORPHISM: There are two alleles; one major, FMO6X105 (truncated form) and one minor, FMO6Q105, (shown here) (full-length form similar to the protein found in other mammals). A nonsense mutation transforms the Gln-105 into a premature stop codon. The truncated protein is catalytically inactive.
  • SIMILARITY: Belongs to the FMO family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL021026; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
UniGene Hs.448988
3D structure databases
ModBase O60774.
PTM databases
PhosphoSite O60774; -.
Organism-specific databases
HGNC HGNC:24024; FMO6.
GenAtlas FMO6.
PharmGKB PA142671753; -.
GeneCards O60774.
Gene expression databases
ArrayExpress O60774; -.
GermOnline ENSG00000117507; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031227; Cellular component: intrinsic to endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0005792; Cellular component: microsome (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004499; Molecular function: flavin-containing monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002255; Flavin_mOase_3.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.
Pfam PF00743; FMO-like; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000332; FMO; 1.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01123; FMOXYGENASE3.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
ProtoNet O60774.
Genome annotation databases
Ensembl ENSG00000117507; Homo sapiens. [Contig view]
Phylogenomic databases
HOGENOM O60774; -.
HOVERGEN O60774; -.
Other
LinkHub O60774; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   539  539     Putative dimethylaniline monooxygenase [N-oxide-forming] 6. PRO_0000147669
TRANSMEM   518   538  21     Potential. 
NP_BIND   9    14  6     FAD (Potential). 
NP_BIND   191   196  6     NADP (By similarity). 
VARIANT   127   127  1     V -> I. VAR_015371 
VARIANT   257   257  1     V -> I. VAR_015372 
Sequence information
Length: 539 AA [This is the length of the unprocessed precursor] Molecular weight: 61291 Da [This is the MW of the unprocessed precursor] CRC64: 8E0D15CA4F79FF0C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKRVGIIGA GVSGLAAIWC CLEEGLEPTC FERSDDVGGL WKFSDHTEEG RASIYQSVFT 

        70         80         90        100        110        120 
NSSKEMMCFP DFPYPDDYPN YIHHSKLQEY IKTYAQKKDL LRYIQFETLV SGIKKCPSFL 

       130        140        150        160        170        180 
VTGQWVVVTE KDGKQESTIF DAVMICSGHH VYPNLPTDSF PGLDQFRGNY LHSRDYKNPE 

       190        200        210        220        230        240 
AFKGKRVLVI GLGNSGSDIA VELSRLATQV IISTRSASWV MSRVWDDGYP WDMMYVTRFA 

       250        260        270        280        290        300 
SFLRNVLPSF ISDWLYVQKM NTWFKHENYG LMPLNGSLRK EPVFNDELPS RILCGTLSIK 

       310        320        330        340        350        360 
PSVKEFTETS AVFEDGTMFE AIDSVIFATG YDYSYPFLDE TIMKSRNNEV TLFKGIFPPL 

       370        380        390        400        410        420 
MEKPTLAVIG LVQSLGAAIP TADLQAWWAA KVFANSCTLP TTNEMMDDTD EKMGKKLKCM 

       430        440        450        460        470        480 
FSSFFMFGQS QTLQTDYITY VDELGSFIGA KPNIPWLFLT DPRLALEVYF GPCSPYQFRL 

       490        500        510        520        530 
MGPGKWDGAR NAILTQWNRT VKPTRTRVVS EVQRPHPFYN LLKMLSFPLL LLAVTLTFY 

O60774 in FASTA format

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