FMO4

Dimethylaniline monooxygenase [N-oxide-forming] 4 is an enzyme that in humans is encoded by the FMO4 gene.[5][6]

FMO4
Identifiers
Aliases	FMO4, FMO2, flavin containing monooxygenase 4, flavin containing dimethylaniline monoxygenase 4
External IDs	OMIM: 136131 MGI: 2429497 HomoloGene: 68219 GeneCards: FMO4
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q24.3 Start 171,314,183 bp[1] End 171,342,084 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 H2.1|1 70.34 cM Start 162,793,188 bp[2] End 162,813,972 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • oxidoreductase activity • NADP binding • flavin adenine dinucleotide binding • monooxygenase activity • N,N-dimethylaniline monooxygenase activity Cellular component • organelle membrane • integral component of membrane • endoplasmic reticulum membrane • endoplasmic reticulum • membrane • intracellular membrane-bounded organelle Biological process • drug catabolic process • oxidation-reduction process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2329	226564
Ensembl	ENSG00000076258	ENSMUSG00000026692
UniProt	P31512	Q8VHG0
RefSeq (mRNA)	NM_002022	NM_144878
RefSeq (protein)	NP_002013	NP_659127
Location (UCSC)	Chr 1: 171.31 – 171.34 Mb	Chr 1: 162.79 – 162.81 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.[6]

Cancer

FMO4 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. [7] For this reason, FMO4 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression. [7]

References

1. GRCh38: Ensembl release 89: ENSG00000076258 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026692 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Lawton MP, Cashman JR, Cresteil T, Dolphin CT, Elfarra AA, Hines RN, Hodgson E, Kimura T, Ozols J, Phillips IR (Mar 1994). "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities". Arch Biochem Biophys. 308 (1): 254–7. doi:10.1006/abbi.1994.1035. PMID 8311461.
6. "Entrez Gene: FMO4 flavin containing monooxygenase 4".
7. Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. PMID 25205602.

Further reading

• Hines RN, Cashman JR, Philpot RM, Williams DE, Ziegler DM (1994). "The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression". Toxicol. Appl. Pharmacol. 125 (1): 1–6. doi:10.1006/taap.1994.1042. PMID 8128486.
• Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR (1992). "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". Biochem. J. 287 ( Pt 1) (Pt 1): 261–7. PMC 1133153. PMID 1417778.
• Phillips IR, Dolphin CT, Clair P, Hadley MR, Hutt AJ, McCombie RR, Smith RL, Shephard EA (1995). "The molecular biology of the flavin-containing monooxygenases of man". Chem. Biol. Interact. 96 (1): 17–32. doi:10.1016/0009-2797(94)03580-2. PMID 7720101.
• Itagaki K, Carver GT, Philpot RM (1996). "Expression and characterization of a modified flavin-containing monooxygenase 4 from humans". J. Biol. Chem. 271 (33): 20102–7. doi:10.1074/jbc.271.33.20102. PMID 8702731.
• Janmohamed A, Dolphin CT, Phillips IR, Shephard EA (2001). "Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450". Biochem. Pharmacol. 62 (6): 777–86. doi:10.1016/S0006-2952(01)00718-3. PMID 11551524.
• Furnes B, Feng J, Sommer SS, Schlenk D (2003). "Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans". Drug Metab. Dispos. 31 (2): 187–93. doi:10.1124/dmd.31.2.187. PMID 12527699.