Reviewed, UniProtKB/Swiss-Prot Q8K4C0 (FMO5_RAT)

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
    Dimethylaniline oxidase 5

Gene names

Name:

Fmo5

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 By similarity.
Catalytic activity	N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
Cofactor	FAD.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
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
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 direct assay. Source: RGD
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_0000147668
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 Ref.3
Experimental info
	Sequence conflict	34	1	R → M in AAH70883. Ref.2
	Sequence conflict	50	1	K → E in AAH70883. Ref.2
	Sequence conflict	136	1	Q → E in AAH70883. Ref.2
	Sequence conflict	228	1	R → H in AAH70883. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8K4C0-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A16A10779E91A8F8	FASTA	533	60,056
	10 20 30 40 50 60 MAKKRIAVIG SGASGLTCIK CCLEEGLEPV CFERSDDIGG LWRYQENPEK GRASIYKSVI 70 80 90 100 110 120 INTSKEMMCF SDYPIPDHYP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKQPDF 130 140 150 160 170 180 STSGQWQVVT EHEGKQQVDV FDGVLVCTGH HTDPHLPLDS FPGIEKFKGK YFHSREYKNP 190 200 210 220 230 240 VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKRGY PIDILLSSRI 250 260 270 280 290 300 TNYLSKICGS ALKNRYMEKQ LNQRFDHEMF GLKPKHSALG QHPTINDDLP NRIISGLVKV 310 320 330 340 350 360 KGNVKEFTET AAIFEDGSRE DDIDVVIFAT GYSFAFPFLE DSVKVVQNKV SLYKKVFPPN 370 380 390 400 410 420 LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KTREEMAKRY 430 440 450 460 470 480 VDSQRHTIQG DYIDTMEEIA DLVGVRPNLL SLAFTDPKLA FQLLVGPCTP VQYRLQGPGK 490 500 510 520 530 WAGARKTILT TEDRIRKPLM TRVVERDSSG TSLVTVRVLM LAVTFLAVIL AYF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing of flavin-containing monooxygenase 5 (FMO5) in the rat." Lattard V., Benoit E. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[3]	"Organellar proteomics reveals Golgi arginine dimethylation." Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S., Yates J.R. III, Howell K.E. Mol. Biol. Cell 15:2907-2919(2004) [PubMed: 15047867] [Abstract] Cited for: METHYLATION AT ARG-5, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF458413 mRNA. Translation: AAM46761.1. BC070883 mRNA. Translation: AAH70883.1.
IPI	IPI00203106.
RefSeq	NP_653340.1.
UniGene	Rn.7038
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8K4C0.
PTM databases
PhosphoSite	Q8K4C0.
Proteomic databases
PRIDE	Q8K4C0.
Genome annotation databases
Ensembl	ENSRNOT00000024423; ENSRNOP00000024423; ENSRNOG00000018076; Rattus norvegicus. [Genome view]
GeneID	246248.
KEGG	rno:246248.
UCSC	NM_144739. rat.
Organism-specific databases
CTD	246248.
RGD	628602. Fmo5.
Phylogenomic databases
HOVERGEN	Q8K4C0.
Enzyme and pathway databases
BRENDA	1.14.13.8. 248.
Gene expression databases
Genevestigator	Q8K4C0.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR000960. Flavin_mOase. IPR002257. Flavin_mOase_5. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01125. FMOXYGENASE5.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	623578.

Entry information

Entry name

FMO5_RAT

Accession

Primary (citable) accession number: Q8K4C0
Secondary accession number(s): Q6IRL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 52 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)