Reviewed, UniProtKB/Swiss-Prot Q04799 (FMO5_RABIT)

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 5
    EC=1.14.13.8
Alternative name(s):
    Hepatic flavin-containing monooxygenase 5
      Short name=FMO 5
    FMO form 3
    FMO 1C1
    Dimethylaniline oxidase 5

Gene names

Name:

FMO5

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	533 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	In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.
Catalytic activity	N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.
Cofactor	FAD.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Kidney and 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 Methylation
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
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 – 533	532	Dimethylaniline monooxygenase [N-oxide-forming] 5		PRO_0000147667
Regions
	Nucleotide binding	10 – 15	6	FAD Potential
	Nucleotide binding	192 – 197	6	NADP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	5	1	Omega-N-methylated arginine By similarity
Natural variations
	Natural variant	132	1	C → V
	Natural variant	241	1	S → Q
	Natural variant	390	1	T → V
	Natural variant	419	1	R → F
	Natural variant	451	1	S → P
	Natural variant	509	1	S → L
Experimental info
	Sequence conflict	5	1	R → K AA sequence Ref.2
	Sequence conflict	160	1	S → K AA sequence Ref.2
	Sequence conflict	306	1	E → ELKE AA sequence Ref.2
	Sequence conflict	512	1	Missing AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q04799-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 188617ACA56E9286	FASTA	533	59,845
	10 20 30 40 50 60 MAGKRVAVIG AGASGLACIK CCLEEGLEPV CFERTDDIGG LWRFQESPDE GRASIYKSVI 70 80 90 100 110 120 INTSKEMMCF SDYPIPDHFP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKRPDF 130 140 150 160 170 180 STSGQWEVLT ECEGKKESAV FDGVLVCTGH HTSAHLPLES FPGIEKFKGQ YLHSRDYKNP 190 200 210 220 230 240 EKFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW IMNRVGDHGY PIDILLSSRF 250 260 270 280 290 300 SQFLKKITGE TIANSFLERK MNQRFDHAMF GLKPKHRALS QHPTVNDDLP NRIISGSVKI 310 320 330 340 350 360 KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFSFPFLE DSVKVVKNKV SLYKKVFPPN 370 380 390 400 410 420 LEKPTLAIIG LIQPLGAIMP ISELQARWAT LVFKGLKTLP SQSEMMTEIS QVQEKMAKRY 430 440 450 460 470 480 VESQRHTIQG DYIETMEEIA DLVGVRPNLL SLAFTDPRLA LQLLLGPCTP VHYRLQGRGK 490 500 510 520 530 WDGARKTILT VEDRIRKPLM TRVTESSNSV TSMMTMGKFM LAIAFLAIAV VYF

References

[1]	"Cloning, sequencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1. Evidence for a third gene subfamily in rabbits." Atta-Asafo-Adjei E., Lawton M.P., Philpot R.M. J. Biol. Chem. 268:9681-9689(1993) [PubMed: 8486656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Isolation and structure of a third form of liver microsomal flavin monooxygenase." Ozols J. Biochemistry 33:3751-3757(1994) [PubMed: 8142375] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-514. Strain: New Zealand white. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L08449 mRNA. Translation: AAA31235.1.
PIR	A45912. A46677.
RefSeq	NP_001075714.1.
UniGene	Ocu.1864
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100009064.
Phylogenomic databases
HOVERGEN	Q04799.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR012143. dManiline_mOase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000960. Flavin_mOase. IPR002257. Flavin_mOase_5. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00419. ADXRDTASE. PR00368. FADPNR. PR00370. FMOXYGENASE. PR01125. FMOXYGENASE5.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

FMO5_RABIT

Accession

Primary (citable) accession number: Q04799

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 4, 2008
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)