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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 2

Gene

Fmo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Shows catalytic activity towards methimazole, thiourea, trimethylamine, and the insecticide phorate.

Catalytic activityi

N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.

Cofactori

Protein has several cofactor binding sites:

pH dependencei

Optimum pH is 10.5.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146FADSequence Analysis
Nucleotide bindingi191 – 1966NADPSequence Analysis

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. monooxygenase activity Source: MGI
  3. N,N-dimethylaniline monooxygenase activity Source: MGI
  4. NADP binding Source: InterPro

GO - Biological processi

  1. drug metabolic process Source: MGI
  2. NADPH oxidation Source: UniProtKB
  3. NADP metabolic process Source: MGI
  4. organic acid metabolic process Source: MGI
  5. oxygen metabolic process Source: MGI
  6. toxin metabolic process Source: MGI
  7. xenobiotic metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, NADP

Enzyme and pathway databases

ReactomeiREACT_244058. FMO oxidises nucleophiles.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 2
Pulmonary flavin-containing monooxygenase 2
Short name:
FMO 2
Gene namesi
Name:Fmo2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1916776. Fmo2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 535534Dimethylaniline monooxygenase [N-oxide-forming] 2PRO_0000147648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ8K2I3.
PaxDbiQ8K2I3.
PRIDEiQ8K2I3.

PTM databases

PhosphoSiteiQ8K2I3.

Expressioni

Gene expression databases

BgeeiQ8K2I3.
CleanExiMM_FMO2.
ExpressionAtlasiQ8K2I3. baseline and differential.
GenevestigatoriQ8K2I3.

Interactioni

Protein-protein interaction databases

IntActiQ8K2I3. 1 interaction.
MINTiMINT-4117353.
STRINGi10090.ENSMUSP00000107135.

Structurei

3D structure databases

ProteinModelPortaliQ8K2I3.
SMRiQ8K2I3. Positions 5-215, 307-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiCOG2072.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ8K2I3.
KOiK00485.
OMAiVEEHTRG.
OrthoDBiEOG7GXPB6.
PhylomeDBiQ8K2I3.
TreeFamiTF105285.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002254. Flavin_mOase_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K2I3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKVVVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG
60 70 80 90 100
RASIYRSVIT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL
110 120 130 140 150
LKYIQFQTTV ISVKKRPDFA SSGQWEVYTQ SNGKEQRTVF DAVMVCSGHH
160 170 180 190 200
IQPHLPLKSF PGIERFRGQY FHSREYKHPV GFEGKRILVV GIGNSAADIA
210 220 230 240 250
SELSKTAAQV FVSTRHGSWV MSRISEDGYP WDMVFHTRFS SMLRNVLPRT
260 270 280 290 300
VVKWMMEQQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK
310 320 330 340 350
TRVKELTETA VVFEDGTVEE DVDIIVFATG YTFSFSFLED SLVKVEDNRV
360 370 380 390 400
SLYKAMFPPH LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGLCSLP
410 420 430 440 450
SETTMMADIV ERNEKRVNLF GKSQSQILQT NYVDYLDELA LEIGAKPDFV
460 470 480 490 500
SLFFKDPKLA VKLYFGPCNS YQYRLVGPGQ WEGARNAILT QKQRILKPLK
510 520 530
TRTLQSSDSA PVSFLLKILG LLAVVLAFFF QLQGF
Length:535
Mass (Da):60,974
Last modified:January 23, 2007 - v3
Checksum:i705FAD9D8EADB1B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691Q → R in AAD56413. (PubMed:11835629)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184981 mRNA. Translation: AAD56413.1.
BC031415 mRNA. Translation: AAH31415.1.
CCDSiCCDS15425.1.
RefSeqiNP_061369.2. NM_018881.3.
XP_006497012.1. XM_006496949.1.
UniGeneiMm.10929.

Genome annotation databases

EnsembliENSMUST00000045902; ENSMUSP00000044405; ENSMUSG00000040170.
ENSMUST00000111510; ENSMUSP00000107135; ENSMUSG00000040170.
GeneIDi55990.
KEGGimmu:55990.
UCSCiuc007dgz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184981 mRNA. Translation: AAD56413.1.
BC031415 mRNA. Translation: AAH31415.1.
CCDSiCCDS15425.1.
RefSeqiNP_061369.2. NM_018881.3.
XP_006497012.1. XM_006496949.1.
UniGeneiMm.10929.

3D structure databases

ProteinModelPortaliQ8K2I3.
SMRiQ8K2I3. Positions 5-215, 307-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K2I3. 1 interaction.
MINTiMINT-4117353.
STRINGi10090.ENSMUSP00000107135.

PTM databases

PhosphoSiteiQ8K2I3.

Proteomic databases

MaxQBiQ8K2I3.
PaxDbiQ8K2I3.
PRIDEiQ8K2I3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045902; ENSMUSP00000044405; ENSMUSG00000040170.
ENSMUST00000111510; ENSMUSP00000107135; ENSMUSG00000040170.
GeneIDi55990.
KEGGimmu:55990.
UCSCiuc007dgz.1. mouse.

Organism-specific databases

CTDi2327.
MGIiMGI:1916776. Fmo2.

Phylogenomic databases

eggNOGiCOG2072.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ8K2I3.
KOiK00485.
OMAiVEEHTRG.
OrthoDBiEOG7GXPB6.
PhylomeDBiQ8K2I3.
TreeFamiTF105285.

Enzyme and pathway databases

ReactomeiREACT_244058. FMO oxidises nucleophiles.

Miscellaneous databases

ChiTaRSiFmo2. mouse.
NextBioi311714.
PROiQ8K2I3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2I3.
CleanExiMM_FMO2.
ExpressionAtlasiQ8K2I3. baseline and differential.
GenevestigatoriQ8K2I3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002254. Flavin_mOase_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse."
    Karoly E.D., Rose R.L.
    J. Biochem. Mol. Toxicol. 15:300-308(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: C57BL/6.
    Tissue: Kidney.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiFMO2_MOUSE
AccessioniPrimary (citable) accession number: Q8K2I3
Secondary accession number(s): Q9QZF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.