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UniProtKB/Swiss-Prot entry Q01740


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

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Entry information
Entry name FMO1_HUMAN
Primary accession number Q01740
Secondary accession numbers Q5QPT2 Q9UJC2
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 73)
Name and origin of the protein
Protein name Dimethylaniline monooxygenase [N-oxide-forming] 1
Synonyms EC 1.14.13.8
Fetal hepatic flavin-containing monooxygenase 1
FMO 1
Dimethylaniline oxidase 1
Gene name
Name: FMO1
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 [MRNA].
TISSUE=Liver;
PubMed=1712018 [NCBI, ExPASy, EBI, Israel, Japan]
Dolphin C.T., Shephard E.A., Povey S., Palmer C.N.A., Ziegler D.M., Ayesh R., Smith R.L., Phillips I.R.;
"Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1).";
J. Biol. Chem. 266:12379-12385(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-223; THR-227; VAL-303; VAL-322; LEU-327; ARG-373 AND HIS-474.
Livingston R.J., Rieder M.J., Chung M.-W., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
VARIANTS GLN-97; THR-303 AND VAL-303.
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: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.
  • CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
  • COFACTOR: FAD.
  • SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane.
  • TISSUE SPECIFICITY: Expressed mainly in fetal liver, adult kindney and to a lesser extent, the intestine.
  • 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
M64082; AAA52457.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY879266; AAW56076.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445673; CAI21383.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031274; CAI21383.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031274; CAI22846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445673; CAI22846.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047129; AAH47129.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40876; A40876.
RefSeq NP_002012.1; -.
UniGene Hs.1424
3D structure databases
ModBase Q01740.
PTM databases
PhosphoSite Q01740; -.
Polymorphism databases
NIEHS-SNPs FMO1.
Organism-specific databases
H-InvDB HIX0028548; -.
HGNC HGNC:3769; FMO1.
GenAtlas FMO1.
MIM 136130; gene. [NCBI / EBI]
PharmGKB PA165; -.
GeneCards Q01740.
Gene expression databases
ArrayExpress Q01740; -.
CleanEx HS_FMO1; -.
Ontologies
GO
GO:0004497; Molecular function: monooxygenase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002253; Flavin_mOase_1.
Graphical view of domain structure.
Pfam PF00743; FMO-like; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000332; FMO; 1.
PRINTS PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01121; FMOXYGENASE1.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q01740.
Genome annotation databases
Ensembl ENSG00000010932; Homo sapiens. [Contig view]
GeneID 2326; -.
KEGG hsa:2326; -.
Phylogenomic databases
HOGENOM Q01740; -.
HOVERGEN Q01740; -.
Other
SOURCE FMO1; Homo sapiens.
ProtoNet Q01740.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   532  531     Dimethylaniline monooxygenase [N-oxide-forming] 1. PRO_0000147639
NP_BIND   9    14  6     FAD (Potential). 
NP_BIND   191   196  6     NADP (Potential). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
VARIANT   97    97  1     H -> Q. VAR_015358 
VARIANT   223   223  1     R -> Q. VAR_022204 
VARIANT   227   227  1     S -> T. VAR_022205 
VARIANT   303   303  1     I -> T (in dbSNP:rs28360418 [NCBI]). VAR_015359 
VARIANT   303   303  1     I -> V (in dbSNP:rs16864314 [NCBI]). VAR_015360 
VARIANT   322   322  1     I -> V. VAR_022206 
VARIANT   327   327  1     F -> L. VAR_022207 
VARIANT   373   373  1     K -> R. VAR_022208 
VARIANT   474   474  1     R -> H. VAR_022209 
Sequence information
Length: 532 AA [This is the length of the unprocessed precursor] Molecular weight: 60311 Da [This is the MW of the unprocessed precursor] CRC64: 627B855F38C2EB6D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS 

        70         80         90        100        110        120 
NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANHFDL LKHIQFKTKV CSVTKCSDSA 

       130        140        150        160        170        180 
VSGQWEVVTM HEEKQESAIF DAVMVCTGFL TNPYLPLDSF PGINAFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
IFKDKRVLVI GMGNSGTDIA VEASHLAEKV FLSTTGGGWV ISRIFDSGYP WDMVFMTRFQ 

       250        260        270        280        290        300 
NMLRNSLPTP IVTWLMERKI NNWLNHANYG LIPEDRTQLK EFVLNDELPG RIITGKVFIR 

       310        320        330        340        350        360 
PSIKEVKENS VIFNNTSKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH 

       370        380        390        400        410        420 
LQKPTLAIIG LIKPLGSMIP TGETQARWAV RVLKGVNKLP PPSVMIEEIN ARKENKPSWF 

       430        440        450        460        470        480 
GLCYCKALQS DYITYIDELL TYINAKPNLF SMLLTDPHLA LTVFFGPCSP YQFRLTGPGK 

       490        500        510        520        530 
WEGARNAIMT QWDRTFKVIK ARVVQESPSP FESFLKVFSF LALLVAIFLI FL 

Q01740 in FASTA format

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