Dimethylaniline monooxygenase [N-oxide-forming] 2

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 2
    EC=1.14.13.8
Alternative name(s):
    Pulmonary flavin-containing monooxygenase 2
      Short name=FMO 2
    FMO 1B1
    Dimethylaniline oxidase 2

Gene names

Name:

FMO2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive.
Catalytic activity	N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
Cofactor	FAD. Magnesium.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Expressed predominantly in lung, and at a much lesser extent in kidney.
Post-translational modification	The truncated form is probably unable to fold correctly and is rapidly degraded.
Polymorphism	There are two alleles; one major, FMO2X472, (truncated form) and one minor, FMO2Q472, (shown here) (full-length form similar to the protein found in other mammals). A nonsense mutation transforms the Gln-472 in a premature stop codon. The truncated protein is catalytically inactive. The minor allele is present at a frequency of approximately 4% in the sample of population of African descent.
Sequence similarities	Belongs to the FMO family.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	FAD Flavoprotein Magnesium NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome
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: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed By similarity

Chain

2 – 535

534

Dimethylaniline monooxygenase [N-oxide-forming] 2

PRO_0000147646

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

36

1

D → G: dbSNP rs2020870. Ref.2 Ref.5

VAR_014840

Natural variant

59

1

V → I Ref.5

VAR_015361

Natural variant

69

1

F → Y: dbSNP rs28745274.

VAR_022185

Natural variant

81

1

F → S: dbSNP rs2020860. Ref.2

VAR_014841

Natural variant

182

1

F → S: dbSNP rs2307492. Ref.2 Ref.5

VAR_014842

Natural variant

195

1

S → L: dbSNP rs2020862. Ref.2 Ref.5

VAR_014843

Natural variant

238

1

R → Q: dbSNP rs28369895.

VAR_015362

Natural variant

314

1

E → G: dbSNP rs2020863.

VAR_022186

Natural variant

391

1

R → T: dbSNP rs28369899.

VAR_015363

Natural variant

413

1

N → K: dbSNP rs2020865. Ref.2 Ref.5

VAR_014844

Experimental info

Sequence conflict

71

1

D → DD in AAW82431. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q99518-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 39A5587AC7BF50B8
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FASTA

535

60,907

        10         20         30         40         50         60 
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVVT 

        70         80         90        100        110        120 
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS 

       130        140        150        160        170        180 
SSGQWKVVTQ SNGKEQSAVF DAVMVCSGHH ILPHIPLKSF PGMERFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV MSRISEDGYP WDSVFHTRFR 

       250        260        270        280        290        300 
SMLRNVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK 

       310        320        330        340        350        360 
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH 

       370        380        390        400        410        420 
LDKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIDLF 

       430        440        450        460        470        480 
GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARNAIFT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein." Dolphin C.T., Beckett D.J., Janmohamed A., Cullingford T.E., Smith R.L., Shephard E.A., Phillips I.R. J. Biol. Chem. 273:30599-30607(1998) [PubMed: 9804831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-36; TYR-69; SER-81; SER-182; LEU-195; GLN-238; GLY-314; THR-391 AND LYS-413.
[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. 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: Skeletal muscle.
[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 GLY-36; ILE-59; SER-182; LEU-195; GLN-238; THR-391 AND LYS-413.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases
	Y09267 mRNA. Translation: CAA70462.1. Different termination. AY916056 Genomic DNA. Translation: AAW82431.1. Different termination. AL021026 Genomic DNA. Translation: CAA15910.1. Different termination. BC005894 mRNA. Translation: AAH05894.1. Different termination.
IPI	IPI00016005.
RefSeq	NP_001451.1.
UniGene	Hs.144912
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q99518.
Genome annotation databases
Ensembl	ENSG00000094963. Homo sapiens. [Contig view]
GeneID	2327.
KEGG	hsa:2327.
Organism-specific databases
GeneCards	GC01P169420.
HGNC	HGNC:3770. FMO2.
MIM	603955. gene.
PharmGKB	PA28187.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q99518.
HOVERGEN	Q99518.
Enzyme and pathway databases
BRENDA	1.14.13.8. 247.
Reactome	REACT_13433. Biological oxidations.
Gene expression databases
ArrayExpress	Q99518.
Bgee	Q99518.
CleanEx	HS_FMO2.
GermOnline	ENSG00000094963. Homo sapiens.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR000960. Flavin_mOase. IPR002254. Flavin_mOase_2. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01122. FMOXYGENASE2.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	9443.
SOURCE	Search...

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Entry information

Entry name

FMO2_HUMAN

Accession

Primary (citable) accession number: Q99518
Secondary accession number(s): Q5EBX4, Q9BRX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents