ACOX3

Acyl-CoA oxidase 3, pristanoyl
Identifiers
Symbol	ACOX3
External IDs	OMIM: 603402 MGI: 1933156 HomoloGene: 37792 GeneCards: ACOX3 Gene
EC number	1.3.3.6
Gene ontology Molecular function • fatty-acyl-CoA binding • acyl-CoA dehydrogenase activity • receptor binding • electron carrier activity • pristanoyl-CoA oxidase activity • flavin adenine dinucleotide binding • oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor Cellular component • mitochondrion • peroxisome • peroxisomal matrix • membrane Biological process • fatty acid beta-oxidation using acyl-CoA dehydrogenase • fatty acid beta-oxidation using acyl-CoA oxidase • cellular lipid metabolic process • small molecule metabolic process • lipid homeostasis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8310	80911
Ensembl	ENSG00000087008	ENSMUSG00000029098
UniProt	O15254	Q9EPL9
RefSeq (mRNA)	NM_001101667	NM_030721
RefSeq (protein)	NP_001095137	NP_109646
Location (UCSC)	Chr 4: 8.37 – 8.44 Mb	Chr 5: 35.58 – 35.61 Mb
PubMed search

Peroxisomal acyl-coenzyme A oxidase 3 is an enzyme that in humans is encoded by the ACOX3 gene.^[1][2]

Acyl-Coenzyme A oxidase 3 also known as pristanoyl -CoA oxidase (ACOX3)is involved in the desaturation of 2-methyl branched fatty acids in peroxisomes. Unlike the rat homolog, the human gene is expressed in very low amounts in the liver such that its mRNA was undetectable by routine Northern-blot analysis, by immunoblotting for its product, or by enzyme activity measurements. However the human cDNA encoding a 700 amino acid protein with a peroxisomal targeting C-terminal tripeptide S-K-L was isolated and is thought to be expressed under special conditions such as specific developmental stages or in a tissue specific manner in tissues that have not yet been examined.^[2]

See Also

• ACOX1
• Acyl-CoA oxidase

References

1. Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP (Sep 1997). "Evidence for the existence of a pristanoyl-CoA oxidase gene in man". Biochem J 325 (3): 593–9. PMC 1218600. PMID 9271077.
2. "Entrez Gene: ACOX3 acyl-Coenzyme A oxidase 3, pristanoyl".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Vanhove GF, Van Veldhoven PP, Fransen M; et al. (1993). "The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney". J. Biol. Chem. 268 (14): 10335–44. PMID 8387517.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Colland F, Jacq X, Trouplin V; et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Zha S, Ferdinandusse S, Hicks JL; et al. (2005). "Peroxisomal branched chain fatty acid beta-oxidation pathway is upregulated in prostate cancer". Prostate 63 (4): 316–23. doi:10.1002/pros.20177. PMID 15599942.
• Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.