ACOT8 acyl-CoA thioesterase 8 [Homo sapiens (human)] - Gene

Summary

Official Symbol: ACOT8provided by HGNC
Official Full Name: acyl-CoA thioesterase 8provided by HGNC
Primary source: HGNC:HGNC:15919
See related: Ensembl:ENSG00000101473 MIM:608123; AllianceGenome:HGNC:15919
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: hTE; NAP1; PTE1; PTE2; PTE-1; PTE-2; HNAACTE; hACTE-III
Summary: The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. [provided by RefSeq, Oct 2010]
Expression: Ubiquitous expression in adrenal (RPKM 10.6), brain (RPKM 10.3) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 20q13.12

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	20	NC_000020.11 (45841721..45857392, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	20	NC_060944.1 (47578222..47593911, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	20	NC_000020.10 (44470360..44486031, complement)

Chromosome 20 - NC_000020.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

In summary, lipolytic enzyme ACOT8 is frequently upregulated in HCC clinical specimens. More importantly, ACOT8 silencing leads to inhibition of cell growth in HCC in vitro.
Title: Fatty acid metabolic enzyme acyl-CoA thioesterase 8 promotes the development of hepatocellular carcinoma.
Acyl-CoA thioesterase 8 is a specific protein related to nodal metastasis and prognosis of lung adenocarcinoma.
Title: Acyl-CoA thioesterase 8 is a specific protein related to nodal metastasis and prognosis of lung adenocarcinoma.
An isoform of long-chain acyl-CoA hydrolase may be responsible for the nafamostat hydrolysis in human liver cytosol.
Title: Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase.
SREBP2 modulates brain palmitoyl-coa hydrolase gene transcription.
Title: Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription.
ACOT4 and ACOT8 are responsible for the termination of beta-oxidation of dicarboxylic acids of medium-chain length with the concomitant release of the corresponding free acids
Title: The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes.

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Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Nef	nef	HIV-1 Nef (from strains NA7 and NL4-3 only) directly interacts with ACOT8 in 293T cells and this interaction is mediated by residues in the Nef core domain as shown by FACS-Forster resonance energy transfer (FRET)-based methods	PubMed
	nef	HIV-1 Nef is identified to have a physical interaction with acyl-CoA thioesterase 8 (ACOT8) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed
	nef	Point mutations in HIV-1 Nef at amino acids Asp108, Leu121, Pro122, and Asp123 abrogate the ability of Nef to bind hTE , downregulate CD4 and MHC class I, and dimerize, indicating a key role for this region of Nef in mediating most of its known functions	PubMed
	nef	Amino acids 108-152 mediate binding of HIV-1 Nef to the human Thioesterase II protein (hTE/ACOT8), an interaction that enhances hTE enzymatic activity	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:485908

RH12567 (e-PCR)
- UniSTS:48204

D20S569E (e-PCR)
- UniSTS:26224

RH71172 (e-PCR)
- UniSTS:16760

RH80960 (e-PCR)
- UniSTS:85694

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables acetoacetyl-CoA hydrolase activity	IEA Inferred from Electronic Annotation more info
enables acetyl-CoA hydrolase activity	TAS Traceable Author Statement more info
enables acyl-CoA hydrolase activity	TAS Traceable Author Statement more info
enables carboxylic ester hydrolase activity	IEA Inferred from Electronic Annotation more info
enables choloyl-CoA hydrolase activity	IEA Inferred from Electronic Annotation more info
enables fatty acyl-CoA hydrolase activity	IBA Inferred from Biological aspect of Ancestor more info
enables fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables fatty acyl-CoA hydrolase activity	TAS Traceable Author Statement more info
enables hydroxymethylglutaryl-CoA hydrolase activity	IEA Inferred from Electronic Annotation more info
NOT enables long-chain fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables long-chain fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables medium-chain fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables succinyl-CoA hydrolase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in acyl-CoA metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in acyl-CoA metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in acyl-CoA metabolic process	TAS Traceable Author Statement more info
involved_in alpha-linolenic acid metabolic process	TAS Traceable Author Statement more info
involved_in bile acid biosynthetic process	TAS Traceable Author Statement more info
involved_in dicarboxylic acid catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in fatty acid beta-oxidation using acyl-CoA oxidase	TAS Traceable Author Statement more info
involved_in fatty acid catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of CD4 production	IDA Inferred from Direct Assay more info	PubMed
involved_in peroxisome fission	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytosol	TAS Traceable Author Statement more info
is_active_in peroxisomal matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisomal matrix	IDA Inferred from Direct Assay more info	PubMed
located_in peroxisomal matrix	IMP Inferred from Mutant Phenotype more info	PubMed
located_in peroxisomal matrix	TAS Traceable Author Statement more info

General protein information

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Preferred Names: acyl-coenzyme A thioesterase 8

Names: HIV-Nef associated acyl-CoA thioesterase; Nef (lentivirus myristoylated factor) associated protein 1; choloyl-CoA hydrolase; choloyl-coenzyme A thioesterase; long-chain fatty-acyl-CoA hydrolase; palmitoyl-CoA hydrolase; peroxisomal acyl-CoA thioesterase 1; peroxisomal acyl-CoA thioesterase 2; peroxisomal acyl-coenzyme A thioester hydrolase 1; peroxisomal long-chain acyl-CoA thioesterase 1; thioesterase II; thioesterase III

NP_005460.2

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_005260296.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_047295765.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_047295766.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_047295767.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_054178783.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_054178784.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_054178785.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

XP_054178786.1

EC 3.1.2.1

EC 3.1.2.11

EC 3.1.2.2

EC 3.1.2.27

EC 3.1.2.3

EC 3.1.2.5

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_005469.4 → NP_005460.2 acyl-coenzyme A thioesterase 8

See identical proteins and their annotated locations for NP_005460.2

Status: REVIEWED

Source sequence(s)

BC117157, BM986979, DB470803, X86032

Consensus CDS

CCDS13378.1

UniProtKB/Swiss-Prot

O14734, O15261, Q17RX4

UniProtKB/TrEMBL

Q6FHI2

Related

ENSP00000217455.4, ENST00000217455.9

Conserved Domains (1) summary

TIGR00189
Location:35 → 309

tesB; acyl-CoA thioesterase II

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000020.11 Reference GRCh38.p14 Primary Assembly

Range

45841721..45857392 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_005260239.4 → XP_005260296.1 acyl-coenzyme A thioesterase 8 isoform X1

See identical proteins and their annotated locations for XP_005260296.1

Conserved Domains (3) summary

cd03444
Location:152 → 255

Thioesterase_II_repeat1; Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) ...

TIGR00189
Location:32 → 256

tesB; acyl-CoA thioesterase II

cl00509
Location:35 → 77

hot_dog; The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated ...
XM_047439810.1 → XP_047295766.1 acyl-coenzyme A thioesterase 8 isoform X3

UniProtKB/TrEMBL

A0A494C0N6

Related

ENSP00000498636.1, ENST00000652771.1
XM_047439811.1 → XP_047295767.1 acyl-coenzyme A thioesterase 8 isoform X4
XM_047439809.1 → XP_047295765.1 acyl-coenzyme A thioesterase 8 isoform X2

UniProtKB/TrEMBL

E9PJN0

Related

ENSP00000435581.1, ENST00000461272.5

Alternate T2T-CHM13v2.0

Genomic

NC_060944.1 Alternate T2T-CHM13v2.0

Range

47578222..47593911 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054322808.1 → XP_054178783.1 acyl-coenzyme A thioesterase 8 isoform X1
XM_054322810.1 → XP_054178785.1 acyl-coenzyme A thioesterase 8 isoform X3

UniProtKB/TrEMBL

A0A494C0N6
XM_054322811.1 → XP_054178786.1 acyl-coenzyme A thioesterase 8 isoform X4
XM_054322809.1 → XP_054178784.1 acyl-coenzyme A thioesterase 8 isoform X2

UniProtKB/TrEMBL

E9PJN0

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_183385.1: Suppressed sequence

Description

NM_183385.1: This RefSeq was temporary suppressed because insufficient evidence exists for the exon combination of this transcript variant, and because it is nonsense-mediated decay (NMD) candidate.
NM_183386.1: Suppressed sequence

Description

NM_183386.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript and the protein.