Reviewed, UniProtKB/Swiss-Prot Q95LA1 (FMO3_CANFA)

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 3
    EC=1.14.13.8
Alternative name(s):
    Hepatic flavin-containing monooxygenase 3
      Short name=FMO 3
    Dimethylaniline oxidase 3

Gene names

Name:

FMO3

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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	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 By similarity.
Catalytic activity	N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
Cofactor	FAD By similarity.
Subcellular location	Microsome membrane By similarity. Endoplasmic reticulum membrane By similarity.
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
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
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] 3		PRO_0000147653
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Amino acid modifications
	Modified residue	401	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q95LA1-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 75897C1AB7C51578	FASTA	532	60,070
	10 20 30 40 50 60 MGKRVAIIGA GVSGLASIRS CLEEGLEPTC FERSEDIGGL WKFSEHAEEG RASIYQSVFT 70 80 90 100 110 120 NSSKEMMCFP DFPYPDDFPN FMHNSKLQEY ITVFSKEKNL LKYIQFKTLV CSVNKRPDFS 130 140 150 160 170 180 VSGQWDITTE RDGKRESATF DAVLICSGHH VYPNLPEESF PGLKLFKGKC FHSREYKEPG 190 200 210 220 230 240 IFKGKRVLVI GLGNSGCDIA TELSHTAEQV IISSRSGSWV MSRVWDDGYP WDMMFITRFE 250 260 270 280 290 300 TFLKNSLPTI ISDWWYMKQM NARFKHENYG LMPLNGTLRK EPVFNDELPA CILCGTVSIK 310 320 330 340 350 360 PNVKAFTETS AIFEDGTVFE AIDCVIFATG YNYAYPFLDE SIIKSKNNEI TLFKGIFPPK 370 380 390 400 410 420 LEKPTMAVIG FVQSLGATIP TTDLQARWAV QVIKGTCTLP SVTDMMNDID KKREGKLKWF 430 440 450 460 470 480 GTSETVQTDY ISYMDELASF IGAKPNIPWL FLTDPKLAVE VFFGPCSPYQ FRLVGPGKWP 490 500 510 520 530 GARNAILTQW DRTLKPMKTR AVGNPQKPCM LCHLVKLFVL PVLFIAVFLA LI

References

[1]

"Cloning, sequencing, and tissue-dependent expression of flavin-containing monooxygenase (FMO) 1 and FMO3 in the dog." Lattard V., Longin-Sauvageon C., Lachuer J., Delatour P., Benoit E. Drug Metab. Dispos. 30:119-128(2002) [PubMed: 11792679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF384054 mRNA. Translation: AAK97434.1.
RefSeq	NP_001003060.1.
UniGene	Cfa.770
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSCAFT00000023776; ENSCAFP00000022069; ENSCAFG00000014992; Canis familiaris. [Genome view]
GeneID	403603.
KEGG	cfa:403603.
Organism-specific databases
CTD	403603.
Phylogenomic databases
HOVERGEN	Q95LA1.
OMA	WFGKSET.
Enzyme and pathway databases
BRENDA	1.14.13.8. 463.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR000960. Flavin_mOase. IPR002255. Flavin_mOase_3. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01123. FMOXYGENASE3.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

FMO3_CANFA

Accession

Primary (citable) accession number: Q95LA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 51 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)