Acyl-CoA thioesterase 3

mammalian protein found in Mus musculus
Protein protein Q21424675
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Acyl-CoA thioesterase 3

Summary

Acyl-CoA thioesterase 3 is a protein[1].

Key Facts

  • Acyl-CoA thioesterase 3's instance of is recorded as protein[2].
  • Acyl-CoA thioesterase 3's subclass of is recorded as protein[3].
  • Acyl-CoA thioesterase 3's UniProt protein ID is recorded as Q9QYR7[4].
  • Acyl-CoA thioesterase 3's part of is recorded as Acyl-CoA thioesterase, long chain[5].
  • Acyl-CoA thioesterase 3's part of is recorded as Alpha/Beta hydrolase fold[6].
  • Acyl-CoA thioesterase 3's part of is recorded as Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase family[7].
  • Acyl-CoA thioesterase 3's part of is recorded as BAAT/Acyl-CoA thioester hydrolase C-terminal domain, protein family[8].
  • Acyl-CoA thioesterase 3's has part is recorded as Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase[9].
  • Acyl-CoA thioesterase 3's has part is recorded as BAAT/Acyl-CoA thioester hydrolase C-terminal[10].
  • Acyl-CoA thioesterase 3's RefSeq protein ID is recorded as NP_001333630[11].
  • Acyl-CoA thioesterase 3's RefSeq protein ID is recorded as NP_599007[12].
  • Acyl-CoA thioesterase 3's molecular function is recorded as palmitoyl-CoA hydrolase activity[13].
  • Acyl-CoA thioesterase 3's molecular function is recorded as acyl-CoA hydrolase activity[14].
  • Acyl-CoA thioesterase 3's molecular function is recorded as carboxylic ester hydrolase activity[15].
  • Acyl-CoA thioesterase 3's molecular function is recorded as hydrolase activity[16].
  • Acyl-CoA thioesterase 3's molecular function is recorded as thiolester hydrolase activity[17].
  • Acyl-CoA thioesterase 3's molecular function is recorded as myristoyl-CoA hydrolase activity[18].
  • Acyl-CoA thioesterase 3's molecular function is recorded as acyl-CoA hydrolase activity[19].
  • Acyl-CoA thioesterase 3's cell component is recorded as cytosol[20].
  • Acyl-CoA thioesterase 3's cell component is recorded as peroxisome[21].
  • Acyl-CoA thioesterase 3's cell component is recorded as peroxisome[22].
  • Acyl-CoA thioesterase 3's biological process is recorded as saturated monocarboxylic acid metabolic process[23].
  • Acyl-CoA thioesterase 3's biological process is recorded as unsaturated monocarboxylic acid metabolic process[24].
  • Acyl-CoA thioesterase 3's biological process is recorded as very long-chain fatty acid metabolic process[25].
  • Acyl-CoA thioesterase 3's biological process is recorded as long-chain fatty acid metabolic process[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] ↑ . Q905695. Retrieved . wikidata.org.
  2. [3] ↑ . Q905695. Retrieved . wikidata.org.
  3. [4] ↑ . Q905695. Retrieved . wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Q20641742. Retrieved . wikidata.org.
  11. [12] ↑ . Q20641742. Retrieved . wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Acyl-CoA thioesterase 3. Retrieved May 3, 2026, from https://4ort.xyz/entity/acyl-coa-thioesterase-3
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BibTeX @misc{4ortxyz_acyl-coa-thioesterase-3_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Acyl-CoA thioesterase 3}}, year = {2026}, url = {https://4ort.xyz/entity/acyl-coa-thioesterase-3}, note = {Accessed: 2026-05-03}}
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