ACAA1

Protein-coding gene in the species Homo sapiens
ACAA1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2IIK

Identifiers
AliasesACAA1, ACAA, PTHIO, THIO, acetyl-CoA acyltransferase 1, Lnc-Myd88
External IDsOMIM: 604054; MGI: 2148491; HomoloGene: 37497; GeneCards: ACAA1; OMA:ACAA1 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for ACAA1
Genomic location for ACAA1
Band3p22.2Start38,103,129 bp[1]
End38,137,242 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for ACAA1
Genomic location for ACAA1
Band9 F3|9 71.33 cMStart119,168,742 bp[2]
End119,179,365 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • jejunal mucosa

  • right lobe of liver

  • mucosa of transverse colon

  • duodenum

  • kidney tubule

  • human kidney

  • renal medulla

  • apex of heart

  • granulocyte

  • body of pancreas
Top expressed in
  • Ileal epithelium

  • lip

  • right kidney

  • choroid plexus of fourth ventricle

  • motor neuron

  • aortic valve

  • interventricular septum

  • corneal stroma

  • ascending aorta

  • fossa
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • acyltransferase activity, transferring groups other than amino-acyl groups
  • protein binding
  • catalytic activity
  • palmitoyl-CoA oxidase activity
  • acyltransferase activity
  • acetate CoA-transferase activity
  • acetyl-CoA C-acyltransferase activity
Cellular component
  • membrane
  • intracellular membrane-bounded organelle
  • peroxisome
  • peroxisomal matrix
  • extracellular region
  • specific granule lumen
  • cytosol
Biological process
  • lipid metabolism
  • bile acid metabolic process
  • alpha-linolenic acid metabolic process
  • very long-chain fatty acid metabolic process
  • fatty acid metabolic process
  • fatty acid beta-oxidation using acyl-CoA oxidase
  • fatty acid beta-oxidation
  • metabolism
  • neutrophil degranulation
  • protein targeting to peroxisome
  • phenylacetate catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

30

113868

Ensembl

ENSG00000060971

ENSMUSG00000036138

UniProt

P09110

Q921H8

RefSeq (mRNA)

NM_001130410
NM_001607

NM_130864
NM_001357516

RefSeq (protein)

NP_001123882
NP_001598
NP_001598.1

NP_570934
NP_001344445

Location (UCSC)Chr 3: 38.1 – 38.14 MbChr 9: 119.17 – 119.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

3-Ketoacyl-CoA thiolase, peroxisomal also known as acetyl-Coenzyme A acyltransferase 1 is an enzyme that in humans is encoded by the ACAA1 gene.[5][6][7]

Acetyl-Coenzyme A acyltransferase 1 is an acetyl-CoA C-acyltransferase enzyme.

Function

This gene encodes an enzyme operative in the beta oxidation system of the peroxisomes.[5]

Clinical significance

Deficiency of this enzyme leads to pseudo-Zellweger syndrome.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000060971 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036138 – 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. ^ a b c "Entrez Gene: acetyl-Coenzyme A acyltransferase 1".
  6. ^ Bout A, Hoovers JM, Bakker E, Mannens MM, Geurts van Kessel A, Westerveld A, Tager JM, Benne R (1989). "Assignment of the gene coding for human peroxisomal 3-oxoacyl-CoA thiolase (ACAA) to chromosome region 3p22----p23". Cytogenet. Cell Genet. 52 (3–4): 147–50. doi:10.1159/000132865. PMID 2630187.
  7. ^ Bout A, Franse MM, Collins J, Blonden L, Tager JM, Benne R (August 1991). "Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient". Biochim. Biophys. Acta. 1090 (1): 43–51. doi:10.1016/0167-4781(91)90035-k. PMID 1679347.

External links

Further reading

  • Lawrence JW, Li Y, Chen S, et al. (2001). "Differential gene regulation in human versus rodent hepatocytes by peroxisome proliferator-activated receptor (PPAR) alpha. PPAR alpha fails to induce peroxisome proliferation-associated genes in human cells independently of the level of receptor expression". J. Biol. Chem. 276 (34): 31521–7. doi:10.1074/jbc.M103306200. PMID 11418601.
  • Patel S, Woods DR, Macleod NJ, et al. (2003). "Angiotensin-converting enzyme genotype and the ventilatory response to exertional hypoxia". Eur. Respir. J. 22 (5): 755–60. doi:10.1183/09031936.03.00086402. PMID 14621081.
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Fujiwara C, Imamura A, Hashiguchi N, et al. (2000). "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.
  • Bout A, Teunissen Y, Hashimoto T, et al. (1988). "Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase". Nucleic Acids Res. 16 (21): 10369. doi:10.1093/nar/16.21.10369. PMC 338871. PMID 3194209.
  • Barbe L, Lundberg E, Oksvold P, et al. (2008). "Toward a confocal subcellular atlas of the human proteome". Mol. Cell. Proteomics. 7 (3): 499–508. doi:10.1074/mcp.M700325-MCP200. PMID 18029348.
  • Ottone F, Raimondi E, Rocchi M, et al. (1995). "Refined localization of human peroxisomal 3-oxoacyl-CoA thiolase (ACAA) to 3p22". Hum. Hered. 45 (2): 75–9. doi:10.1159/000154263. PMID 7750978.
  • Park HC, Choi SR, Kim BS, et al. (2005). "Polymorphism of the ACE Gene in Dialysis Patients: Overexpression of DD Genotype in Type 2 Diabetic End-Stage Renal Failure Patients". Yonsei Med. J. 46 (6): 779–87. doi:10.3349/ymj.2005.46.6.779. PMC 2810591. PMID 16385653.
  • Daigo Y, Isomura M, Nishiwaki T, et al. (1999). "Characterization of a 1200-kb genomic segment of chromosome 3p22-p21.3". DNA Res. 6 (1): 37–44. doi:10.1093/dnares/6.1.37. PMID 10231028.
  • 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.
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Schram AW, Goldfischer S, van Roermund CW, et al. (1987). "Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency". Proc. Natl. Acad. Sci. U.S.A. 84 (8): 2494–6. Bibcode:1987PNAS...84.2494S. doi:10.1073/pnas.84.8.2494. PMC 304678. PMID 2882519.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
  • Wanders RJ, Waterham HR (2006). "Biochemistry of mammalian peroxisomes revisited". Annu. Rev. Biochem. 75: 295–332. doi:10.1146/annurev.biochem.74.082803.133329. PMID 16756494.
  • Fairbairn LJ, Tanner MJ (1989). "Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase". Nucleic Acids Res. 17 (9): 3588. doi:10.1093/nar/17.9.3588. PMC 317802. PMID 2726492.
  • Omi S, Nakata R, Okamura-Ikeda K, et al. (2008). "Contribution of peroxisome-specific isoform of Lon protease in sorting PTS1 proteins to peroxisomes". J. Biochem. 143 (5): 649–60. doi:10.1093/jb/mvn020. PMID 18281296.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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