Reviewed, UniProtKB/Swiss-Prot P17635 (FMO2_RABIT)

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

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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 protein 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. Magnesium By similarity.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane By similarity.
Tissue specificity	Lung.
Polymorphism	There are two allelic forms.
Sequence similarities	Belongs to the FMO family.

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	Direct protein sequencing
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 535	534	Dimethylaniline monooxygenase [N-oxide-forming] 2		PRO_0000147650
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3
Natural variations
	Natural variant	120	1	A → S in PFMO-2 and PFMO-4.
	Natural variant	136	1	Q → E in PFMO-2 and PFMO-4.

Sequences

	Sequence		Length	Mass (Da)
	P17635-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D51910BDA41C55C2	FASTA	535	61,144
	10 20 30 40 50 60 MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYQSVIT 70 80 90 100 110 120 NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA 130 140 150 160 170 180 SSGQWEVVTQ SNSKQQSAVF DAVMVCSGHH ILPNIPLKSF PGIEKFKGQY FHSRQYKHPA 190 200 210 220 230 240 GLEGKRILVI GIGNSASDIA VELSKKAAQV YISTRKGSWV MSRISEDGYP WDMVFHTRFS 250 260 270 280 290 300 SMLRNVLPRM IVKWMMEQQM NRWFNHENYG LAPENKYLMK EPVLNDDLPS RILYGTIKVK 310 320 330 340 350 360 RRVKELTESA AIFEDGTVEE DIDVIVFATG YTFAFPFLEE SLVKIEDNMV SLYKYMFPPQ 370 380 390 400 410 420 LEKSTFACLG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SKETMMADII KRNENRIALF 430 440 450 460 470 480 GESLSQKLQT NYIDYLDELA LEIGAKPDLV SFLFKDPKLA VKLYFGPCNS YQYRLVGPGQ 490 500 510 520 530 WEGARNAIFT QKQRILKPLK TRTLKASSNF PVSFLLKFLG LFALVLAFLF QLQWF

References

[1]	"The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes." Lawton M.P., Gasser R., Tynes R.E., Hodgson E., Philpot R.M. J. Biol. Chem. 265:5855-5861(1990) [PubMed: 2318837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: New Zealand white.
[2]	"Guinea pig or rabbit lung flavin-containing monooxygenases with distinct mobilities in SDS-PAGE are allelic variants that differ at only two positions." Nikbakht K.N., Lawton M.P., Philpot R.M. Pharmacogenetics 2:207-216(1992) [PubMed: 1306120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Lung.
[3]	"Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin." Guan S., Falick A.M., Williams D.E., Cashman J.R. Biochemistry 30:9892-9900(1991) [PubMed: 1911780] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2. Tissue: Lung.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M32029 mRNA. Translation: AAA31442.1.
PIR	B35182.
RefSeq	NP_001075753.1.
UniGene	Ocu.1946
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSOCUG00000005177. Oryctolagus cuniculus. [Contig view]
GeneID	100009119.
Phylogenomic databases
HOVERGEN	P17635.
Enzyme and pathway databases
BRENDA	1.14.13.8. 255.
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...

Entry information

Entry name

FMO2_RABIT

Accession

Primary (citable) accession number: P17635

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)