UniProt Accession

 FMO5_MOUSE; P97872; Q8R1W6 

Genbank Protein ID

 U90535; AK133675; CH466620; BC022991 

Genbank Nucleotide ID

 AAB50013.1; BAE21778.1; EDL38939.1; AAH22991.1 

Protein Name

 Dimethylaniline monooxygenase [N-oxide-forming] 5 

Protein Synonyms/Alias

 Dimethylaniline oxidase 5; Hepatic flavin-containing monooxygenase 5; FMO 5 

Gene Name

 Fmo5 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
97	EYFRMYAKEFDLLKY	ubiquitination	[1]
103	AKEFDLLKYIQFKTT	ubiquitination	[1]
108	LLKYIQFKTTVCSVK	ubiquitination	[1]
115	KTTVCSVKKQPDFST	ubiquitination	[1]
170	GIEKFKGKYFHSRDY	acetylation	[2, 3]
178	YFHSRDYKNPVEFTG	acetylation	[2]
178	YFHSRDYKNPVEFTG	ubiquitination	[1]
186	NPVEFTGKRVIVIGI	ubiquitination	[1]
227	WILNRVGKHGYPIDL	ubiquitination	[1]
253	RICGPSLKNNYMEKQ	ubiquitination	[1]
259	LKNNYMEKQMNQRFD	ubiquitination	[1]
273	DHEMFGLKPKHRALS	acetylation	[2]
273	DHEMFGLKPKHRALS	ubiquitination	[1]
275	EMFGLKPKHRALSQH	ubiquitination	[1]
299	RIIAGLVKVKGNVKE	ubiquitination	[1]
349	SVKVVKNKVSLYKKV	acetylation	[2, 3]
394	RWATQVFKGLKKLPS	acetylation	[3]
394	RWATQVFKGLKKLPS	ubiquitination	[1]
398	QVFKGLKKLPSQSEM	ubiquitination	[1]
411	EMMAEINKAREEMAK	ubiquitination	[1]
480	YRLQGPGKWAGARKT	acetylation	[2]
480	YRLQGPGKWAGARKT	ubiquitination	[1]
486	GKWAGARKTILTTED	ubiquitination	[1]
497	TTEDRVRKPLMTRVV	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme (By similarity). 

Sequence Annotation

 NP_BIND 10 15 FAD (Potential).
 NP_BIND 192 197 NADP (By similarity).
 MOD_RES 5 5 Omega-N-methylated arginine (By  

Keyword

 Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 533 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:EC.
 GO:0050661; F:NADP binding; IEA:InterPro. 

Interpro

 IPR012143; DiMe-aniline_mOase.
 IPR000960; Flavin_mOase.
 IPR020946; Flavin_mOase-like.
 IPR002257; Flavin_mOase_5.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF00743; FMO-like 

SMART

  

PROSITE

  

PRINTS

 PR00370; FMOXYGENASE.
 PR01125; FMOXYGENASE5.