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ACOX3
Identifiers
Aliases	ACOX3, acyl-CoA oxidase 3, pristanoyl
External IDs	OMIM: 603402; MGI: 1933156; HomoloGene: 37792; GeneCards: ACOX3; OMA:ACOX3 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4p16.1 Start 8,366,282 bp End 8,440,723 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 B3 Start 35,740,384 bp End 35,772,696 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pancreatic ductal cell gingival epithelium right auricle apex of heart right lobe of liver olfactory zone of nasal mucosa skin of leg skin of abdomen minor salivary glands sural nerve Top expressed in right kidney granulocyte spermatocyte zygote secondary oocyte proximal tubule spermatid lip muscle of thigh primary visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function oxidoreductase activity, acting on the CH-CH group of donors acyl-CoA oxidase activity oxidoreductase activity signaling receptor binding pristanoyl-CoA oxidase activity FAD binding acyl-CoA dehydrogenase activity flavin adenine dinucleotide binding fatty acid binding Cellular component membrane peroxisome peroxisomal matrix mitochondrion cytosol Biological process lipid metabolism fatty acid metabolic process fatty acid beta-oxidation using acyl-CoA oxidase fatty acid beta-oxidation metabolism fatty acid beta-oxidation using acyl-CoA dehydrogenase protein targeting to peroxisome lipid homeostasis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8310 80911 Ensembl ENSG00000087008 ENSMUSG00000029098 UniProt O15254 Q9EPL9 RefSeq (mRNA) NM_001101667 NM_003501 NM_030721 NM_001357018 NM_001357019 NM_001357020 RefSeq (protein) NP_001095137 NP_003492 NP_001362712 NP_001362713 NP_001362714 NP_001362715 NP_001362716 NP_001362717 NP_001362718 NP_001362719 NP_109646 NP_001343947 NP_001343948 NP_001343949 Location (UCSC) Chr 4: 8.37 – 8.44 Mb Chr 5: 35.74 – 35.77 Mb PubMed search
Wikidata
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Peroxisomal acyl-coenzyme A oxidase 3 is an enzyme that in humans is encoded by the ACOX3 gene.

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.

See also

• ACOX1
• Acyl-CoA oxidase

References

1. ^ GRCh38: Ensembl release 89: ENSG00000087008 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029098 – 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. 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. doi:10.1042/bj3250593. PMC 1218600. PMID 9271077.
6. ^ "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. doi:10.1016/S0021-9258(18)82206-2. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 44702394.
• 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.

External links

• Human ACOX3 genome location and ACOX3 gene details page in the UCSC Genome Browser.

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