Q95LA2 (FMO1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 1
EC=1.14.13.8

Alternative name(s):
Dimethylaniline oxidase 1
Hepatic flavin-containing monooxygenase 1
Short name=FMO 1

Gene names

Name:

FMO1

Organism

Canis familiaris (Dog) (Canis lupus familiaris)

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	This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.
Catalytic activity	N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
Cofactor	FAD By similarity.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Liver.
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	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
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	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide 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] 1		PRO_0000147637
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Sites
	Site	208	1	Important for substrate binding By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q95LA2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9F34585CB267592F	FASTA	532	60,059
	10 20 30 40 50 60 MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS 70 80 90 100 110 120 NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANRFSL LKCIRFKTKV CKVTKCPDFT 130 140 150 160 170 180 VTGQWEVVTQ HEGKQESAIF DAVMVCTGFL TNPHLPLDCF PGINTFKGQY FHSRQYKHPD 190 200 210 220 230 240 IFKDKRVLVI GMGNSGTDIA VETSRLAKKV FLSTTGGAWV MSRVFDSGYP WDMVFMTRFQ 250 260 270 280 290 300 NMFRNSLPTP IVTWLMARKM NSWFNHANYG LVPEDRTQLR EPVLNDELPG CIITGKVLIK 310 320 330 340 350 360 PSIKEVKENS VVFNNTPKEE PIDIIVFATG YTFAFPFLDE TVVKVENGQA SLYKYIFPVH 370 380 390 400 410 420 LPKPTLAVIG LIKPLGSMIP TGETQARWAV RVLKGINKLP PQSAMTEEVN ARKENKPSGF 430 440 450 460 470 480 GLCYCKALQS DYITYIDELL TNINAKPNLF SLLLTDPRLA LTIFFGPCTP YQFRLTGPGK 490 500 510 520 530 WKGARNAILT QWDRTFKVTK TRIVQESPTP FASLLKLLSL LALLMAIFLI FL

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
EMBL GenBank DDBJ	AF384053 mRNA. Translation: AAK97433.1.
RefSeq	NP_001003061.1. NM_001003061.1.
UniGene	Cfa.3465.
3D structure databases
ProteinModelPortal	Q95LA2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q95LA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCAFT00000023758; ENSCAFP00000022051; ENSCAFG00000014982. ENSCAFT00000038420; ENSCAFP00000034136; ENSCAFG00000014982.
GeneID	403604.
KEGG	cfa:403604.
Organism-specific databases
CTD	2326.
Phylogenomic databases
eggNOG	maNOG04375.
GeneTree	ENSGT00550000074292.
HOVERGEN	HBG002037.
InParanoid	Q95LA2.
OMA	FLTNPYL.
OrthoDB	EOG42RD71.
PhylomeDB	Q95LA2.
Family and domain databases
InterPro	IPR012143. DiMe-aniline_mOase. IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. IPR002253. Flavin_mOase_1. [Graphical view]
KO	K00485.
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01121. FMOXYGENASE1.
ProtoNet	Search...

Entry information

Entry name

FMO1_CANFA

Accession

Primary (citable) accession number: Q95LA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program