Reviewed, UniProtKB/Swiss-Prot P32417 (FMO3_RABIT)

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
    FMO form 2
    FMO II
    FMO 1D1
    Dimethylaniline oxidase 3

Gene names

Name:

FMO3

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	531 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	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.
Catalytic activity	N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
Cofactor	FAD.
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
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2 Ref.3
	Chain	2 – 531	530	Dimethylaniline monooxygenase [N-oxide-forming] 3		PRO_0000147658
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Natural variations
	Natural variant	279	1	R → M
	Natural variant	405	1	M → V
Experimental info
	Sequence conflict	76	1	D → P AA sequence Ref.2
	Sequence conflict	81	1	F → N AA sequence Ref.2
	Sequence conflict	128 – 130	3	STE → ATC AA sequence Ref.2
	Sequence conflict	172 – 173	2	HS → RQ AA sequence Ref.2
	Sequence conflict	197	1	C → E AA sequence Ref.2
	Sequence conflict	306	1	F → FKEF AA sequence Ref.2
	Sequence conflict	419	1	W → T AA sequence Ref.2
	Sequence conflict	423	1	S → W AA sequence Ref.2
	Sequence conflict	514 – 516	3	WLK → ELW AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P32417-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A4505481077C6CC8	FASTA	531	59,815
	10 20 30 40 50 60 MGKKVAIIGA GISGLASIRS CLEEGLEPTC FEMSDDIGGL WKFSDHAEEG RASIYQSVFT 70 80 90 100 110 120 NSSKEMMCFP DFPFPDDFPN FMHNSKLQEY ITTFAREKNL LKYIQFKTLV SSIKKHPDFS 130 140 150 160 170 180 VTGQWYVSTE RNGKKETAVF DAVMICSGHH VYPNLPKDSF PGLKHFKGKS FHSREYKEPG 190 200 210 220 230 240 IFKGKRVLVI GLGNSGCDIA TELSHTAEQV VISSRSGSWV MSRVWDDGYP WDMLYVTRFQ 250 260 270 280 290 300 TFLKNNLPTA ISDWWYVKQM NAKFKHENYS LMPLNGTLRK EPVFNDDLPA RILCGTVSIK 310 320 330 340 350 360 PNVKEFTETS AIFEDGTVFE AIDSVIFATG YGYAYPFLDD SIIKSENNKV TLFKGIFPPQ 370 380 390 400 410 420 LEKPTMAVIG LVQSLGAAIP TTDLQARWAA QVIKGTCTLP PVKDMMNDIH EKMGTKLKWF 430 440 450 460 470 480 GKSETIQTDY INYMDELASF IGVKLNIPWL FLTDPRLALE VFFGPCSPYQ FRLVGPGKWP 490 500 510 520 530 GARQAILTQW DRSLKPMKTR AVGHLQKPAL FSPWLKLLAI AVLLIAAVLV F

References

[1]	"Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3." Burnett V.L., Lawton M.P., Philpot R.M. J. Biol. Chem. 269:14314-14322(1994) [PubMed: 8188717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Liver.
[2]	"Multiple forms of liver microsomal flavin-containing monooxygenases: complete covalent structure of form 2." Ozols J. Arch. Biochem. Biophys. 290:103-115(1991) [PubMed: 1898080] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-531.
[3]	"Liver microsomes contain two distinct NADPH-Monooxygenases with NH2-terminal segments homologous to the flavin containing NADPH-monooxygenase of Pseudomonas fluorescens." Ozols J. Biochem. Biophys. Res. Commun. 163:49-55(1989) [PubMed: 2505769] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-33. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L10391 mRNA. Translation: AAA21178.1.
PIR	B54096. S18380.
RefSeq	NP_001075715.1.
UniGene	Ocu.1821
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100009065.
Organism-specific databases
CTD	100009065.
Phylogenomic databases
HOVERGEN	P32417.
Enzyme and pathway databases
BRENDA	1.14.13.8. 255.
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_RABIT

Accession

Primary (citable) accession number: P32417

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	September 1, 2009
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)