Cytosolic acyl coenzyme A thioester hydrolase (ACOT7)
The protein contains 380 amino acids for an estimated molecular weight of 41796 Da.
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:10578051). Acyl-coenzyme A thioesterase 7/ACOT7 preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (PubMed:10578051). May play an important physiological function in brain (PubMed:10578051). (updated: May 8, 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.
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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Biological Process
Acyl-CoA metabolic process
Coenzyme A biosynthetic process
Fatty acid catabolic process
Fatty acid metabolic process
Long-chain fatty-acyl-CoA catabolic process
Medium-chain fatty acid biosynthetic process
Medium-chain fatty-acyl-CoA catabolic process
Palmitic acid biosynthetic process
Cellular Component
Cell body
Cytoplasm
Cytosol
Extracellular exosome
Mitochondrion
Neuron projection
Nucleoplasm
The reference OMIM entry for this protein is 602587
Acyl-coa thioesterase 7; acot7
Acyl-coa thioesterase, long-chain, cytosolic
Cte-ii
Acyl-coa thioester hydrolase, long-chain, 2
Acyl-coa hydrolase, long-chain, brain; bach
Acyl-coa hydrolase, long-chain, liver; lach
Acyl-coa thioesterase 2
DESCRIPTION
Long-chain acyl-CoA thioesterases (EC 3.1.2.2), such as ACOT7, are found in all organisms and cleave fatty acyl-CoAs into free fatty acids and CoA.CLONING
Engberg et al. (1997) purified a liver cytosolic isoform of long-chain acyl-CoA thioesterase from peroxisome proliferator-treated rats and named it CTE-II for 'cytosolic long-chain acyl-CoA thioesterase.' Antibodies against CTE-II were used to screen an expression library of peroxisome proliferator-induced rat liver cDNA. The predicted 338-amino acid protein migrated at 40 kD on SDS-PAGE. Engberg et al. (1997) observed many evenly distributed nucleotide differences and pronounced differences in the C-terminal regions between CTE-II and the closely related ACT (602586) and suggested that the 2 enzymes are encoded by different genes. Engberg et al. (1997) noted that there are human ESTs homologous to CTE-II. Yamada et al. (1997) isolated cDNAs encoding long-chain acyl-CoA hydrolases from rat brain and liver cDNA libraries and designated the clones Bach and Lach, respectively. Since the nucleotide sequences of the N-terminal regions were entirely different but the downstream sequences were virtually identical, Yamada et al. (1997) suggested that Bach and Lach are derived from the same gene by alternative splicing. Using a rat Bach cDNA to screen a human brain cDNA library, Yamada et al. (1999) cloned BACH. The deduced protein contains 338 amino acids and shares 95% identity with rat Bach. Northern blot analysis detected a 1.9-kb BACH transcript in human brain RNA. Biochemical analysis of human brain homogenates showed that BACH is a cytosolic enzyme. SDS-PAGE detected BACH at 43 kD, but gel filtration detected BACH at about 100 kD, indicating that the protein forms multimers. By 5-prime RACE and RT-PCR of human brain total RNA, Yamada et al. (2002) identified 6 BACH splice variants. Four variants, designated BACHa to BACHd, differ in their use of 1 of 4 alternate first exons (exons 1a through 1d, respectively) and encode proteins of 329 to 380 amino acids. All 4 of these proteins contain the hydrolase domain and a bipartite nuclear localization signal (NLS) in their C-terminal halves, and BACHb and BACHc have N-terminal mitochondrial localization signals. The 2 remaining variants contain exon X, an alternatively spliced exon between exons 7 and 8 that causes a frameshift and introduces a premature stop codon. These C-terminally truncated proteins of 246 and 283 amino acids lack the hydrolase domain and NLS. The BACH proteins containing the mitochondrial localization signal were detected in mitochondria of transfected mouse neuroblastoma cells, but those containing only the NLS did not localize to nuclei, even though the isolated NLS was functional when fused to a test protein. Immunohistochemical analysis of human brain detected BACHa in the cytosol of neurons such as pyramidal cells in the cerebral cortex and Purkinje cells in the cerebellum. In mouse brain, Bacha was also detected in nuclei as well as cytosol of certain large neurons in the cerebellum, medulla oblongata, and spinal cord. Yamada et al. (2002) suggested that the NLS of BACH may be masked by the full-length protein as a regulatory mechanism.GENE FUNCTION
Yamada et al. (1997) found that bacterial extracts of E. coli expressing either rat Bach or Lach cDNAs had 100-fold higher acyl-CoA hydrolase activity, demonstrating that both cDNAs encode long-chain acyl-CoA hydrolases. By a ... More on the omim web site
May 11, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602587 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed