ACOX3

Protein-coding gene in the species Homo sapiens
ACOX3
Identifiers
AliasesACOX3, acyl-CoA oxidase 3, pristanoyl
External IDsOMIM: 603402; MGI: 1933156; HomoloGene: 37792; GeneCards: ACOX3; OMA:ACOX3 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for ACOX3
Genomic location for ACOX3
Band4p16.1Start8,366,282 bp[1]
End8,440,723 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for ACOX3
Genomic location for ACOX3
Band5|5 B3Start35,740,384 bp[2]
End35,772,696 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 5: 35.74 – 35.77 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Peroxisomal acyl-coenzyme A oxidase 3 is an enzyme that in humans is encoded by the ACOX3 gene.[5][6]

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.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000087008 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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


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