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Protein

Acyl-coenzyme A thioesterase 8

Gene

ACOT8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation.By similarity1 Publication

Catalytic activityi

Choloyl-CoA + H2O = cholate + CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321Charge relay systemBy similarity
Active sitei254 – 2541Charge relay systemBy similarity
Active sitei304 – 3041Charge relay systemBy similarity

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: UniProtKB
  • carboxylic ester hydrolase activity Source: UniProtKB-KW
  • choloyl-CoA hydrolase activity Source: UniProtKB-EC
  • medium-chain acyl-CoA hydrolase activity Source: UniProtKB
  • palmitoyl-CoA hydrolase activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Host-virus interaction, Peroxisome biogenesis

Enzyme and pathway databases

BRENDAi3.1.2.2. 2681.
3.1.2.20. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17017. Beta-oxidation of pristanoyl-CoA.
REACT_17062. Beta-oxidation of very long chain fatty acids.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 8 (EC:3.1.2.27)
Short name:
Acyl-CoA thioesterase 8
Alternative name(s):
Choloyl-coenzyme A thioesterase
HIV-Nef-associated acyl-CoA thioesterase
PTE-2
Peroxisomal acyl-coenzyme A thioester hydrolase 1
Short name:
PTE-1
Peroxisomal long-chain acyl-CoA thioesterase 1
Thioesterase II
Short name:
hACTE-III
Short name:
hACTEIII
Short name:
hTE
Gene namesi
Name:ACOT8
Synonyms:ACTEIII, PTE1, PTE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15919. ACOT8.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: Ensembl
  • peroxisomal matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33941.

Polymorphism and mutation databases

BioMutaiACOT8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Acyl-coenzyme A thioesterase 8PRO_0000202152Add
BLAST

Proteomic databases

MaxQBiO14734.
PaxDbiO14734.
PRIDEiO14734.

PTM databases

PhosphoSiteiO14734.

Expressioni

Tissue specificityi

Detected in a T-cell line (at protein level). Ubiquitous.1 Publication

Inductioni

Regulated by peroxisome proliferator (such as Clofibrate), via the peroxisome proliferator-activated receptors (PPARs).By similarity

Gene expression databases

BgeeiO14734.
CleanExiHS_ACOT8.
ExpressionAtlasiO14734. baseline and differential.
GenevisibleiO14734. HS.

Organism-specific databases

HPAiCAB010261.

Interactioni

Subunit structurei

Interacts with HIV-1 Nef.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
nefP046017EBI-1237371,EBI-6164028From a different organism.
PEX5P505423EBI-1237371,EBI-597835
RELQ048643EBI-1237371,EBI-307352

Protein-protein interaction databases

BioGridi115323. 12 interactions.
IntActiO14734. 7 interactions.
MINTiMINT-2998229.
STRINGi9606.ENSP00000217455.

Structurei

3D structure databases

ProteinModelPortaliO14734.
SMRiO14734. Positions 37-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi317 – 3193Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

eggNOGiCOG1946.
GeneTreeiENSGT00390000004207.
HOGENOMiHOG000246495.
HOVERGENiHBG019167.
InParanoidiO14734.
KOiK11992.
OMAiAKEVPIE.
OrthoDBiEOG7VTDNQ.
PhylomeDBiO14734.
TreeFamiTF315124.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR003703. Acyl_CoA_thio.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERiPTHR11066. PTHR11066. 1 hit.
SUPFAMiSSF54637. SSF54637. 2 hits.
TIGRFAMsiTIGR00189. tesB. 1 hit.

Sequencei

Sequence statusi: Complete.

O14734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP
60 70 80 90 100
AKRLFGGQIV GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER
110 120 130 140 150
TRTGSSFSVR SVKAVQHGKP IFICQASFQQ AQPSPMQHQF SMPTVPPPEE
160 170 180 190 200
LLDCETLIDQ YLRDPNLQKR YPLALNRIAA QEVPIEIKPV NPSPLSQLQR
210 220 230 240 250
MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL LPHQWQHKVH
260 270 280 290 300
FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV
310
TCAQEGVIRV KPQVSESKL
Length:319
Mass (Da):35,914
Last modified:January 1, 1998 - v1
Checksum:i8345C6E5EABF3326
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2933LWR → VWS in CAA60024 (PubMed:9153233).Curated
Sequence conflicti319 – 3191L → R in CAA60024 (PubMed:9153233).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014404 mRNA. Translation: AAB71665.1.
X86032 mRNA. Translation: CAA60024.1.
AF124264 mRNA. Translation: AAD27616.1.
AL008726 Genomic DNA. Translation: CAA15502.1.
BC117155 mRNA. Translation: AAI17156.1.
BC117157 mRNA. Translation: AAI17158.1.
CCDSiCCDS13378.1.
PIRiJC5644.
RefSeqiNP_005460.2. NM_005469.3.
UniGeneiHs.444776.

Genome annotation databases

EnsembliENST00000217455; ENSP00000217455; ENSG00000101473.
GeneIDi10005.
KEGGihsa:10005.
UCSCiuc002xqa.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014404 mRNA. Translation: AAB71665.1.
X86032 mRNA. Translation: CAA60024.1.
AF124264 mRNA. Translation: AAD27616.1.
AL008726 Genomic DNA. Translation: CAA15502.1.
BC117155 mRNA. Translation: AAI17156.1.
BC117157 mRNA. Translation: AAI17158.1.
CCDSiCCDS13378.1.
PIRiJC5644.
RefSeqiNP_005460.2. NM_005469.3.
UniGeneiHs.444776.

3D structure databases

ProteinModelPortaliO14734.
SMRiO14734. Positions 37-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115323. 12 interactions.
IntActiO14734. 7 interactions.
MINTiMINT-2998229.
STRINGi9606.ENSP00000217455.

PTM databases

PhosphoSiteiO14734.

Polymorphism and mutation databases

BioMutaiACOT8.

Proteomic databases

MaxQBiO14734.
PaxDbiO14734.
PRIDEiO14734.

Protocols and materials databases

DNASUi10005.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217455; ENSP00000217455; ENSG00000101473.
GeneIDi10005.
KEGGihsa:10005.
UCSCiuc002xqa.2. human.

Organism-specific databases

CTDi10005.
GeneCardsiGC20M044470.
HGNCiHGNC:15919. ACOT8.
HPAiCAB010261.
MIMi608123. gene.
neXtProtiNX_O14734.
PharmGKBiPA33941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1946.
GeneTreeiENSGT00390000004207.
HOGENOMiHOG000246495.
HOVERGENiHBG019167.
InParanoidiO14734.
KOiK11992.
OMAiAKEVPIE.
OrthoDBiEOG7VTDNQ.
PhylomeDBiO14734.
TreeFamiTF315124.

Enzyme and pathway databases

BRENDAi3.1.2.2. 2681.
3.1.2.20. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17017. Beta-oxidation of pristanoyl-CoA.
REACT_17062. Beta-oxidation of very long chain fatty acids.

Miscellaneous databases

GeneWikiiACOT8.
GenomeRNAii10005.
NextBioi37789.
PROiO14734.
SOURCEiSearch...

Gene expression databases

BgeeiO14734.
CleanExiHS_ACOT8.
ExpressionAtlasiO14734. baseline and differential.
GenevisibleiO14734. HS.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR003703. Acyl_CoA_thio.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERiPTHR11066. PTHR11066. 1 hit.
SUPFAMiSSF54637. SSF54637. 2 hits.
TIGRFAMsiTIGR00189. tesB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef."
    Watanabe H., Shiratori T., Shoji H., Miyatake S., Okazaki Y., Ikuta K., Sato T., Saito T.
    Biochem. Biophys. Res. Commun. 238:234-239(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HIV-1 NEF, TISSUE SPECIFICITY.
  2. "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation."
    Liu L.X., Margottin F., Le Gall S., Schwartz O., Selig L., Benarous R., Benichou S.
    J. Biol. Chem. 272:13779-13785(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoid tissue.
  3. "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans."
    Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.
    J. Biol. Chem. 274:9216-9223(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Muscle.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis."
    Ishizuka M., Toyama Y., Watanabe H., Fujiki Y., Takeuchi A., Yamasaki S., Yuasa S., Miyazaki M., Nakajima N., Taki S., Saito T.
    Exp. Cell Res. 297:127-141(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism."
    Hunt M.C., Alexson S.E.H.
    Prog. Lipid Res. 41:99-130(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACOT8_HUMAN
AccessioniPrimary (citable) accession number: O14734
Secondary accession number(s): O15261, Q17RX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.