FMO4

FMO4
Identifiers
Aliases	FMO4, FMO2, flavin containing monooxygenase 4, flavin containing dimethylaniline monoxygenase 4
External IDs	OMIM: 136131; MGI: 2429497; HomoloGene: 68219; GeneCards: FMO4; OMA:FMO4 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	171,342,084 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	162,641,541 bp
RNA expression pattern
	Top expressed in
	kidney tubule; ; right lobe of liver; ; mucosa of ileum; ; gonad; ; human kidney; ; testicle; ; glomerulus; ; metanephric glomerulus; ; ascending aorta; ; Descending thoracic aorta;
	Top expressed in
	right kidney; ; yolk sac; ; jejunum; ; proximal tubule; ; zygote; ; duodenum; ; embryo; ; ileum; ; secondary oocyte; ; human kidney;
	More reference expression data
	More reference expression data
Orthologs
	2329
	226564
	ENSG00000076258
	ENSMUSG00000026692
	P31512
	Q8VHG0
	NM_002022
	NM_144878
	NP_002013
	NP_659127
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000076258 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026692 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: FMO4 flavin containing monooxygenase 4".
^ ^a ^b 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. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

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. doi:10.1042/bj2870261. 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. Bibcode:1995CBI....96...17P. 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. S2CID 6619389.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000076258 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8311461-5] 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.

[entrez-6] "Entrez Gene: FMO4 flavin containing monooxygenase 4".

[Rotondo_2015-7] 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. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

[1]

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

Function

Cancer

References

Further reading