UniProt:O14734 ACOT8

chain
  • chain:1-319
checksum 8345C6E5EABF3326
comment
  • FUNCTION Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:15194431, PubMed:9153233, PubMed:9299485). Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:9153233, PubMed:9299485). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431).FUNCTION (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233).CATALYTIC ACTIVITY choloyl-CoA + H2O = cholate + CoA + H(+)CATALYTIC ACTIVITY chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+)CATALYTIC ACTIVITY acetyl-CoA + H2O = acetate + CoA + H(+)CATALYTIC ACTIVITY butanoyl-CoA + H2O = butanoate + CoA + H(+)CATALYTIC ACTIVITY 2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA + H(+)CATALYTIC ACTIVITY hexanoyl-CoA + H2O = hexanoate + CoA + H(+)CATALYTIC ACTIVITY octanoyl-CoA + H2O = octanoate + CoA + H(+)CATALYTIC ACTIVITY decanoyl-CoA + H2O = decanoate + CoA + H(+)CATALYTIC ACTIVITY dodecanoyl-CoA + H2O = dodecanoate + CoA + H(+)CATALYTIC ACTIVITY tetradecanoyl-CoA + H2O = tetradecanoate + CoA + H(+)CATALYTIC ACTIVITY hexadecanoyl-CoA + H2O = hexadecanoate + CoA + H(+)CATALYTIC ACTIVITY octadecanoyl-CoA + H2O = octadecanoate + CoA + H(+)CATALYTIC ACTIVITY malonyl-CoA + H2O = malonate + CoA + H(+)CATALYTIC ACTIVITY acetoacetyl-CoA + H2O = acetoacetate + CoA + H(+)CATALYTIC ACTIVITY propanoyl-CoA + H2O = propanoate + CoA + H(+)CATALYTIC ACTIVITY succinyl-CoA + H2O = succinate + CoA + H(+)CATALYTIC ACTIVITY glutaryl-CoA + H2O = glutarate + CoA + H(+)CATALYTIC ACTIVITY hexanedioyl-CoA + H2O = hexanedioate + CoA + H(+)CATALYTIC ACTIVITY octanedioyl-CoA + H2O = octanedioate + CoA + H(+)CATALYTIC ACTIVITY decanedioyl-CoA + H2O = decanedioate + CoA + H(+)CATALYTIC ACTIVITY dodecanedioyl-CoA + H2O = dodecanedioate + CoA + H(+)CATALYTIC ACTIVITY (9Z)-tetradecenoyl-CoA + H2O = (9Z)-tetradecenoate + CoA + H(+)CATALYTIC ACTIVITY (9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+)CATALYTIC ACTIVITY (9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+)CATALYTIC ACTIVITY (9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+)CATALYTIC ACTIVITY eicosanoyl-CoA + H2O = eicosanoate + CoA + H(+)CATALYTIC ACTIVITY (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+)CATALYTIC ACTIVITY 4,8-dimethylnonanoyl-CoA + H2O = 4,8-dimethylnonanoate + CoA + H(+)CATALYTIC ACTIVITY 2,6-dimethylheptanoyl-CoA + H2O = 2,6-dimethylheptanoate + CoA + H(+)CATALYTIC ACTIVITY (3S)-3-hydroxy-3-methylglutaryl-CoA + H2O = 3-hydroxy-3-methylglutarate + CoA + H(+)CATALYTIC ACTIVITY 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA + H(+)CATALYTIC ACTIVITY 2-methyloctadecanoyl-CoA + H2O = 2-methyloctadecanoate + CoA + H(+)CATALYTIC ACTIVITY prostaglandin F2alpha-CoA + H2O = prostaglandin F2alpha + CoA + H(+)ACTIVITY REGULATION Inhibited by CoASH (IC(50)=10-15 uM). Also inhibited by cysteine-reactive agents.BIOPHYSICOCHEMICAL PROPERTIES Lipid metabolism; fatty acid metabolism.SUBUNIT Homodimer (By similarity).SUBUNIT (Microbial infection) Interacts with human immunodeficiency virus (HIV-1) Nef (via middle region); this interaction enhances ACOT8 Acyl-CoA thioesterase activity and occurs in a Nef myristoylation-independent manner (PubMed:9299485). According to a second report, the interaction with HIV-1 Nef occurs in a Nef myristoylation-independent manner but does not enhance ACOT8 Acyl-CoA thioesterase activity (PubMed:9153233).INTERACTION Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded.TISSUE SPECIFICITY Detected in a T-cell line (at protein level). Ubiquitous (PubMed:9153233, PubMed:9299485).INDUCTION Regulated by peroxisome proliferator (such as Clofibrate), via the peroxisome proliferator-activated receptors (PPARs).SIMILARITY Belongs to the C/M/P thioester hydrolase family.
crossReference
databaseName UniProt
dbId 62401
description
  • recommendedName: Acyl-coenzyme A thioesterase 8 shortName: Acyl-CoA thioesterase 8 ecNumber evidence="7 10"3.1.2.1 ecNumber evidence="2"3.1.2.11 ecNumber evidence="9 10"3.1.2.2 ecNumber evidence="2"3.1.2.3 ecNumber evidence="2"3.1.2.5 alternativeName: Choloyl-coenzyme A thioesterase ecNumber evidence="10"3.1.2.27 alternativeName: HIV-Nef-associated acyl-CoA thioesterase alternativeName: fullName evidence="12"Peroxisomal acyl-CoA thioesterase 2 shortName evidence="12"PTE-2 alternativeName: Peroxisomal acyl-coenzyme A thioester hydrolase 1 shortName: PTE-1 alternativeName: Peroxisomal long-chain acyl-CoA thioesterase 1 alternativeName: Thioesterase II shortName: hACTE-III shortName: hACTEIII shortName: hTE
displayName UniProt:O14734 ACOT8
geneName
  • ACOT8
  • ACTEIII
  • PTE1
identifier O14734
isSequenceChanged false
keyword
  • Fatty acid metabolism
  • Host-virus interaction
  • Hydrolase
  • Lipid metabolism
  • Peroxisome
  • Peroxisome biogenesis
  • Proteomics identification
  • Reference proteome
  • Serine esterase
modified [InstanceEdit:9963647] Weiser, Joel, 2025-08-15
moleculeType Protein
name
  • ACOT8
otherIdentifier
  • 10005
  • 11718690_a_at
  • 11735679_a_at
  • 11760868_a_at
  • 11760869_x_at
  • 11761076_x_at
  • 11762204_a_at
  • 16919673
  • 204212_PM_at
  • 204212_at
  • 236514_PM_at
  • 236514_at
  • 36841_at
  • 3907474
  • 3907475
  • 3907476
  • 3907477
  • 3907478
  • 3907479
  • 3907480
  • 3907481
  • 3907482
  • 3907483
  • 3907489
  • 3907490
  • 3907491
  • 3907492
  • 3907493
  • 3907494
  • 3907495
  • 3907496
  • 3907497
  • 47789_at
  • 8066598
  • A_23_P143218
  • A_33_P3231833
  • A_33_P3352544
  • GE81515
  • GE88147
  • GO:0003824
  • GO:0003986
  • GO:0004778
  • GO:0005515
  • GO:0005777
  • GO:0005782
  • GO:0005829
  • GO:0006629
  • GO:0006631
  • GO:0006636
  • GO:0006637
  • GO:0006699
  • GO:0006790
  • GO:0007031
  • GO:0009062
  • GO:0010561
  • GO:0016289
  • GO:0016559
  • GO:0016787
  • GO:0033540
  • GO:0033882
  • GO:0036109
  • GO:0042759
  • GO:0043649
  • GO:0047603
  • GO:0047617
  • GO:0047994
  • GO:0052689
  • GO:0052815
  • GO:0052816
  • GO:0055086
  • GO:1901570
  • HMNXSV003021848
  • Hs.6511.0.A1_3p_at
  • ILMN_1679600
  • PH_hs_0025996
  • TC20000890.hg
  • g4885564_3p_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • ACOT8_HUMAN
  • O15261
  • Q17RX4
sequenceLength 319
species [Species:48887] Homo sapiens
stId uniprot:O14734
url http://purl.uniprot.org/uniprot/O14734
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