Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P97501

- FMO3_MOUSE

UniProt

P97501 - FMO3_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

Fmo3

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

Functioni

Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Acts on TMA to produce TMA-N-oxide.1 Publication

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

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

GO - Molecular functioni

  1. amino acid binding Source: Ensembl
  2. flavin adenine dinucleotide binding Source: InterPro
  3. N,N-dimethylaniline monooxygenase activity Source: UniProtKB-EC
  4. NADP binding Source: Ensembl
  5. trimethylamine monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. drug metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiREACT_244058. FMO oxidises nucleophiles.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 3 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 3
Hepatic flavin-containing monooxygenase 3
Short name:
FMO 3
Trimethylamine monooxygenase (EC:1.14.13.148)
Gene namesi
Name:Fmo3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1100496. Fmo3.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
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 – 534533Dimethylaniline monooxygenase [N-oxide-forming] 3PRO_0000147656Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei401 – 4011Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP97501.
PaxDbiP97501.
PRIDEiP97501.

PTM databases

PhosphoSiteiP97501.

Expressioni

Tissue specificityi

Liver.

Inductioni

Expression is specifically repressed in male mice after puberty, preventing trimethylamine degradation. Trimethylamine is present at high concentration in the urine of male mice after puberty and acts as an attractant.1 Publication

Gene expression databases

BgeeiP97501.
CleanExiMM_FMO3.
ExpressionAtlasiP97501. baseline and differential.
GenevestigatoriP97501.

Interactioni

Protein-protein interaction databases

IntActiP97501. 3 interactions.
MINTiMINT-4095189.
STRINGi10090.ENSMUSP00000028010.

Structurei

3D structure databases

ProteinModelPortaliP97501.
SMRiP97501. Positions 3-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiCOG2072.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP97501.
KOiK00485.
OMAiFMHNSKL.
OrthoDBiEOG7GXPB6.
PhylomeDBiP97501.
TreeFamiTF105285.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.

Sequencei

Sequence statusi: Complete.

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

P97501-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKKVAIIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHIEEG
60 70 80 90 100
RASIYQSVFT NSSKEMMCFP DFPYPDDFPN FMHHSKLQEY ITSFAKEKNL
110 120 130 140 150
LKYIQFETPV TSINKCPNFS TTGKWEVTTE KHGKKETAVF DATMICSGHH
160 170 180 190 200
IFPHVPKDSF PGLNRFKGKC FHSRDYKEPG IWKGKRVLVI GLGNSGCDIA
210 220 230 240 250
AELSHVAQKV TISSRSGSWV MSRVWDDGYP WDMVVLTRFQ TFLKNNLPTA
260 270 280 290 300
ISDWWYTRQM NARFKHENYG LVPLNRTLRK EPVFNDELPA RILCGMVTIK
310 320 330 340 350
PNVKEFTETS AVFEDGTMFE AIDCVIFATG YGYAYPFLDD SIIKSRNNEV
360 370 380 390 400
TLYKGVFPPQ LEKPTMAVIG LVQSLGATIP ITDLQARWAA QVIKGTCTLP
410 420 430 440 450
SVNDMMDDID EKMGEKFKWY GNSTTIQTDY IVYMDELASF IGAKPNLLWL
460 470 480 490 500
FLKDPRLAVE VFFGPCSPYQ FRLVGPGKWS GARNAILTQW DRSLKPMKTR
510 520 530
VVSKVQKSCS HFYSRLLRLL AVPVLLIALF LVLI
Length:534
Mass (Da):60,516
Last modified:May 1, 1997 - v1
Checksum:iF72F7993C01AF9C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87147 mRNA. Translation: AAB47541.1.
CCDSiCCDS15426.1.
RefSeqiNP_032056.1. NM_008030.1.
UniGeneiMm.2900.

Genome annotation databases

EnsembliENSMUST00000028010; ENSMUSP00000028010; ENSMUSG00000026691.
GeneIDi14262.
KEGGimmu:14262.
UCSCiuc007dhe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87147 mRNA. Translation: AAB47541.1 .
CCDSi CCDS15426.1.
RefSeqi NP_032056.1. NM_008030.1.
UniGenei Mm.2900.

3D structure databases

ProteinModelPortali P97501.
SMRi P97501. Positions 3-208.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97501. 3 interactions.
MINTi MINT-4095189.
STRINGi 10090.ENSMUSP00000028010.

PTM databases

PhosphoSitei P97501.

Proteomic databases

MaxQBi P97501.
PaxDbi P97501.
PRIDEi P97501.

Protocols and materials databases

DNASUi 14262.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028010 ; ENSMUSP00000028010 ; ENSMUSG00000026691 .
GeneIDi 14262.
KEGGi mmu:14262.
UCSCi uc007dhe.1. mouse.

Organism-specific databases

CTDi 2328.
MGIi MGI:1100496. Fmo3.

Phylogenomic databases

eggNOGi COG2072.
HOGENOMi HOG000076537.
HOVERGENi HBG002037.
InParanoidi P97501.
KOi K00485.
OMAi FMHNSKL.
OrthoDBi EOG7GXPB6.
PhylomeDBi P97501.
TreeFami TF105285.

Enzyme and pathway databases

Reactomei REACT_244058. FMO oxidises nucleophiles.

Miscellaneous databases

NextBioi 285607.
PROi P97501.
SOURCEi Search...

Gene expression databases

Bgeei P97501.
CleanExi MM_FMO3.
ExpressionAtlasi P97501. baseline and differential.
Genevestigatori P97501.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00743. FMO-like. 1 hit.
[Graphical view ]
PIRSFi PIRSF000332. FMO. 1 hit.
PRINTSi PR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): comparison with the human isoform."
    Falls J.G., Cherrington N.J., Clements K.M., Philpot R.M., Levi P.E., Rose R.L., Hodgson E.
    Arch. Biochem. Biophys. 347:9-18(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Liver.
  2. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  3. "Synchronous evolution of an odor biosynthesis pathway and behavioral response."
    Li Q., Korzan W.J., Ferrero D.M., Chang R.B., Roy D.S., Buchi M., Lemon J.K., Kaur A.W., Stowers L., Fendt M., Liberles S.D.
    Curr. Biol. 23:11-20(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiFMO3_MOUSE
AccessioniPrimary (citable) accession number: P97501
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 26, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Trimethylamine is a bacterial metabolite found in some animal odors, and is a repulsive odor associated with bad breath and spoiled food for most organisms, except for M.musculus, where it acts as an attractant.1 Publication

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