Q01740 (FMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 1
EC=1.14.13.8

Alternative name(s):
Dimethylaniline oxidase 1
Fetal hepatic flavin-containing monooxygenase 1
Short name=FMO 1

Gene names

Name:

FMO1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (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 kidney and, to a lesser extent, the intestine.
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from direct assay PubMed 15144220. Source: BHF-UCL organic acid metabolic process Inferred from direct assay PubMed 15144220. Source: BHF-UCL response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to osmotic stress Inferred from electronic annotation. Source: Compara toxin metabolic process Inferred from direct assay PubMed 15144220. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	N,N-dimethylaniline monooxygenase activity Inferred from direct assay PubMed 15144220. Source: BHF-UCL NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 532	531	Dimethylaniline monooxygenase [N-oxide-forming] 1		PRO_0000147639
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Natural variations
	Natural variant	97	1	H → Q. Ref.7 Corresponds to variant rs56841822 [ dbSNP | Ensembl ].		VAR_015358
	Natural variant	223	1	R → Q. Ref.2 Corresponds to variant rs16864310 [ dbSNP | Ensembl ].		VAR_022204
	Natural variant	227	1	S → T. Ref.2		VAR_022205
	Natural variant	303	1	I → T. Ref.7 Corresponds to variant rs28360418 [ dbSNP | Ensembl ].		VAR_015359
	Natural variant	303	1	I → V. Ref.2 Ref.7 Corresponds to variant rs16864314 [ dbSNP | Ensembl ].		VAR_015360
	Natural variant	322	1	I → V. Ref.2 Corresponds to variant rs28360419 [ dbSNP | Ensembl ].		VAR_022206
	Natural variant	327	1	F → L. Ref.2 Corresponds to variant rs28360420 [ dbSNP | Ensembl ].		VAR_022207
	Natural variant	373	1	K → R. Ref.2 Corresponds to variant rs28360421 [ dbSNP | Ensembl ].		VAR_022208
	Natural variant	474	1	R → H. Ref.2 Corresponds to variant rs28360433 [ dbSNP | Ensembl ].		VAR_022209

Sequences

	Sequence		Length	Mass (Da)
	Q01740 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 627B855F38C2EB6D	FASTA	532	60,311
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1)." Dolphin C.T., Shephard E.A., Povey S., Palmer C.N.A., Ziegler D.M., Ayesh R., Smith R.L., Phillips I.R. J. Biol. Chem. 266:12379-12385(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-223; THR-227; VAL-303; VAL-322; LEU-327; ARG-373 AND HIS-474.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thalamus.
[4]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[7]	"Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans." Furnes B., Feng J., Sommer S.S., Schlenk D. Drug Metab. Dispos. 31:187-193(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLN-97; THR-303 AND VAL-303.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64082 mRNA. Translation: AAA52457.1. AY879266 Genomic DNA. Translation: AAW56076.1. AK290113 mRNA. Translation: BAF82802.1. AL445673, AL031274 Genomic DNA. Translation: CAI21383.1. AL031274, AL445673 Genomic DNA. Translation: CAI22846.1. CH471067 Genomic DNA. Translation: EAW90892.1. BC047129 mRNA. Translation: AAH47129.1.
IPI	IPI00182179.
PIR	A40876.
RefSeq	NP_002012.1. NM_002021.1.
UniGene	Hs.1424.
3D structure databases
ProteinModelPortal	Q01740.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000346901.
PTM databases
PhosphoSite	Q01740.
Polymorphism databases
DMDM	399505.
Proteomic databases
PaxDb	Q01740.
PRIDE	Q01740.
Protocols and materials databases
DNASU	2326.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354841; ENSP00000346901; ENSG00000010932. ENST00000367750; ENSP00000356724; ENSG00000010932.
GeneID	2326.
KEGG	hsa:2326.
UCSC	uc001ghl.3. human.
Organism-specific databases
CTD	2326.
GeneCards	GC01P171217.
H-InvDB	HIX0028548.
HGNC	HGNC:3769. FMO1.
HPA	HPA023680.
MIM	136130. gene.
neXtProt	NX_Q01740.
PharmGKB	PA165.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2072.
HOGENOM	HOG000076537.
HOVERGEN	HBG002037.
InParanoid	Q01740.
KO	K00485.
OMA	PSVMIEE.
OrthoDB	EOG42RD71.
PhylomeDB	Q01740.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q01740.
Bgee	Q01740.
CleanEx	HS_FMO1.
Genevestigator	Q01740.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR012143. DiMe-aniline_mOase. IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. IPR002253. Flavin_mOase_1. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01121. FMOXYGENASE1.
ProtoNet	Search...
Other
GenomeRNAi	2326.
NextBio	9439.
SOURCE	Search...

Entry information

Entry name

FMO1_HUMAN

Accession

Primary (citable) accession number: Q01740
Secondary accession number(s): A8K248, Q5QPT2, Q9UJC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.