Acetyl-CoA acetyltransferase, cytosolic (ACAT2)
The protein contains 397 amino acids for an estimated molecular weight of 41351 Da.
Involved in the biosynthetic pathway of cholesterol. (updated: July 3, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs25683 |
Biological Process
Cholesterol biosynthetic process
Ergosterol biosynthetic process
Fatty acid beta-oxidation
Lipid metabolic process
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Mitochondrion
Nucleolus
Nucleoplasm
Nucleus
The reference OMIM entry for this protein is 100678
Acetyl-coa acetyltransferase 2; acat2
Acetocoenzyme a acetyltransferase 2
Acetoacetyl-coa thiolase, cytosolic
DESCRIPTION
The ACAT2 gene encodes cytosolic acetoacetyl-CoA thiolase (EC 2.3.1.9), which is important in the utilization of ketone bodies (de Groot et al., 1977). Mitochondrial acetoacetyl-CoA thiolase is encoded by the ACAT1 gene (607809).CLONING
Song et al. (1994) cloned an ACAT2 cDNA by use of an antibody against the human enzyme. The deduced amino acid sequence had 34 to 57% homology with 4 other human thiolases and 4 acetoacetyl-CoA thiolases of microorganisms.MAPPING
The TCP1 gene (186980) is located on 6p in the vicinity of the major histocompatibility complex, and the murine homolog, Tcp1, is located in the t-complex region of mouse chromosome 17. In the mouse, a related gene, Tcp1x, is tightly linked to Tcp1. Ashworth (1993) showed that 2 genes located 3-prime to the murine Tcp1 and Tcp1x genes code for proteins highly homologous to acetyl-CoA acetyltransferases. These Acat genes are in opposite orientation to the Tcp1 genes, and transcription results in mRNA species that contain the last exon of Tcp1 or Tcp1x within the 3-prime untranslated region of the respective Acat mRNA. Willison et al. (1987) showed that in humans the TCP1 and ACAT2 genes also overlap. Retention of this close linkage during mammalian evolution suggests the possibility of some functional significance. Transcription of both DNA strands at a given locus is common in prokaryotic and viral systems. For examples of overlapping transcriptional units in humans, see Morel et al. (1989) and Laudet et al. (1991). As the human TCP1 gene had been assigned to 6q25-q27 by study of somatic cell hybrids and by in situ hybridization, the ACAT2 gene was suspected to be localized to the same chromosome region. By fluorescence in situ hybridization, Masuno et al. (1996) demonstrated that the ACAT2 gene is located on 6q25.3-q26. ... More on the omim web site
July 4, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 100678 was added.