Reviewed, UniProtKB/Swiss-Prot Q01740 (FMO1_HUMAN)

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 1
    EC=1.14.13.8
Alternative name(s):
    Fetal hepatic flavin-containing monooxygenase 1
      Short name=FMO 1
    Dimethylaniline oxidase 1

Gene names

Name:

FMO1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.
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.
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
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro microsome Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity 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		VAR_015358
	Natural variant	223	1	R → Q		VAR_022204
	Natural variant	227	1	S → T		VAR_022205
	Natural variant	303	1	I → T: dbSNP rs28360418.		VAR_015359
	Natural variant	303	1	I → V: dbSNP rs16864314.		VAR_015360
	Natural variant	322	1	I → V		VAR_022206
	Natural variant	327	1	F → L		VAR_022207
	Natural variant	373	1	K → R		VAR_022208
	Natural variant	474	1	R → H		VAR_022209

Sequences

	Sequence		Length	Mass (Da)
	Q01740-1 [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: 1712018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." 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. 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]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[5]	"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: 12527699] [Abstract] Cited for: VARIANTS GLN-97; THR-303 AND VAL-303.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64082 mRNA. Translation: AAA52457.1. AY879266 Genomic DNA. Translation: AAW56076.1. AL445673, AL031274 Genomic DNA. Translation: CAI21383.1. AL031274, AL445673 Genomic DNA. Translation: CAI22846.1. BC047129 mRNA. Translation: AAH47129.1.
PIR	A40876.
RefSeq	NP_002012.1.
UniGene	Hs.1424
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q01740.
Polymorphism databases
NIEHS-SNPs	Search...
Genome annotation databases
Ensembl	ENSG00000010932. Homo sapiens. [Contig view]
GeneID	2326.
KEGG	hsa:2326.
Organism-specific databases
H-InvDB	HIX0028548.
HGNC	HGNC:3769. FMO1.
MIM	136130. gene.
PharmGKB	PA165.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q01740.
HOVERGEN	Q01740.
Gene expression databases
ArrayExpress	Q01740.
CleanEx	HS_FMO1.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000960. Flavin_mOase. IPR002253. Flavin_mOase_1. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00368. FADPNR. PR00370. FMOXYGENASE. PR01121. FMOXYGENASE1.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	9439.
SOURCE	Search...

Entry information

Entry name

FMO1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)