ACOX1

Protein-coding gene in the species Homo sapiens
ACOX1
Identifiers
AliasesACOX1, ACOX, PALMCOX, SCOX, acyl-CoA oxidase 1, palmitoyl, acyl-CoA oxidase 1, MITCH
External IDsOMIM: 609751; MGI: 1330812; HomoloGene: 38299; GeneCards: ACOX1; OMA:ACOX1 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for ACOX1
Genomic location for ACOX1
Band17q25.1Start75,941,507 bp[1]
End75,979,177 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for ACOX1
Genomic location for ACOX1
Band11|11 E2Start116,062,714 bp[2]
End116,089,871 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • jejunal mucosa

  • buccal mucosa cell

  • duodenum

  • mucosa of transverse colon

  • liver

  • right lobe of liver

  • internal globus pallidus

  • oral cavity

  • mucosa of ileum

  • rectum
Top expressed in
  • left lobe of liver

  • right kidney

  • proximal tubule

  • human kidney

  • tunica adventitia of aorta

  • brown adipose tissue

  • pyloric antrum

  • epithelium of stomach

  • jejunum

  • white adipose tissue
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • signaling receptor binding
  • PDZ domain binding
  • palmitoyl-CoA oxidase activity
  • protein N-terminus binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • acyl-CoA oxidase activity
  • FAD binding
  • acyl-CoA dehydrogenase activity
  • flavin adenine dinucleotide binding
  • fatty acid binding
Cellular component
  • nucleolus
  • nucleoplasm
  • cytoplasm
  • mitochondrion
  • nucleus
  • peroxisomal membrane
  • intracellular membrane-bounded organelle
  • peroxisome
  • membrane
  • peroxisomal matrix
  • plasma membrane
  • cytosol
Biological process
  • spermatogenesis
  • generation of precursor metabolites and energy
  • lipid metabolism
  • fatty acid beta-oxidation
  • alpha-linolenic acid metabolic process
  • metabolism
  • peroxisome fission
  • fatty acid metabolic process
  • very long-chain fatty acid metabolic process
  • prostaglandin metabolic process
  • lipid homeostasis
  • fatty acid oxidation
  • fatty acid beta-oxidation using acyl-CoA oxidase
  • regulation of lipid metabolic process
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase
  • protein targeting to peroxisome
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51

11430

Ensembl

ENSG00000161533

ENSMUSG00000020777

UniProt

Q15067

Q9R0H0

RefSeq (mRNA)

NM_001185039
NM_004035
NM_007292

NM_001271898
NM_015729
NM_001377521
NM_001377522

RefSeq (protein)

NP_001171968
NP_004026
NP_009223

NP_001258827
NP_056544
NP_001364450
NP_001364451

Location (UCSC)Chr 17: 75.94 – 75.98 MbChr 11: 116.06 – 116.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Peroxisomal acyl-coenzyme A oxidase 1 is an enzyme that in humans is encoded by the ACOX1 gene.[5][6]

The protein encoded by this gene is the first enzyme of the fatty acid beta-oxidation pathway, which catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. It donates electrons directly to molecular oxygen, thereby producing hydrogen peroxide. Defects in this gene result in pseudoneonatal adrenoleukodystrophy, a disease that is characterized by accumulation of very long chain fatty acids. Alternatively spliced transcript variants encoding different isoforms have been identified.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000161533 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020777 – 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. ^ Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK (May 1994). "Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization". Proc Natl Acad Sci U S A. 91 (8): 3107–11. Bibcode:1994PNAS...91.3107V. doi:10.1073/pnas.91.8.3107. PMC 43524. PMID 8159712.
  6. ^ a b "Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl".

Further reading

  • Seedorf U, Ellinghaus P, Roch Nofer J (2000). "Sterol carrier protein-2". Biochim. Biophys. Acta. 1486 (1): 45–54. doi:10.1016/s1388-1981(00)00047-0. PMID 10856712.
  • Singh H, Brogan M, Johnson D, Poulos A (1993). "Peroxisomal beta-oxidation of branched chain fatty acids in human skin fibroblasts". J. Lipid Res. 33 (11): 1597–605. doi:10.1016/S0022-2275(20)41382-3. PMID 1464743.
  • Watkins PA, McGuinness MC, Raymond GV, et al. (1995). "Distinction between peroxisomal bifunctional enzyme and acyl-CoA oxidase deficiencies". Ann. Neurol. 38 (3): 472–7. doi:10.1002/ana.410380322. PMID 7668838. S2CID 8189860.
  • Chu R, Varanasi U, Chu S, et al. (1995). "Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells". J. Biol. Chem. 270 (9): 4908–15. doi:10.1074/jbc.270.9.4908. PMID 7876265.
  • Fournier B, Saudubray JM, Benichou B, et al. (1994). "Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy". J. Clin. Invest. 94 (2): 526–31. doi:10.1172/JCI117365. PMC 296126. PMID 8040306.
  • Aoyama T, Tsushima K, Souri M, et al. (1994). "Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase". Biochem. Biophys. Res. Commun. 198 (3): 1113–8. doi:10.1006/bbrc.1994.1158. PMID 8117268.
  • 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.
  • Pacot C, Latruffe N (1993). "Biochemical properties of liver peroxisomes from rat, guinea pig and human species and the influence of hormonal status on rat liver acyl-CoA oxidase mRNA content". Biochimie. 75 (3–4): 235–42. doi:10.1016/0300-9084(93)90082-4. PMID 8507686.
  • Fan CY, Pan J, Chu R, et al. (1996). "Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene". J. Biol. Chem. 271 (40): 24698–710. doi:10.1074/jbc.271.40.24698. PMID 8798738.
  • 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.
  • Fujiwara C, Imamura A, Hashiguchi N, et al. (2001). "Catalase-less peroxisomes. Implication in the milder forms of peroxisome biogenesis disorder". J. Biol. Chem. 275 (47): 37271–7. doi:10.1074/jbc.M006347200. PMID 10960480.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Suzuki Y, Iai M, Kamei A, et al. (2002). "Peroxisomal acyl CoA oxidase deficiency". J. Pediatr. 140 (1): 128–30. doi:10.1067/mpd.2002.120511. PMID 11815777. S2CID 36469133.
  • 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.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • 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.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.


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