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O14734 (ACOT8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A thioesterase 8

Short name=Acyl-CoA thioesterase 8
EC=3.1.2.27
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 names
Name:ACOT8
Synonyms:ACTEIII, PTE1, PTE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

Choloyl-CoA + H2O = cholate + CoA.

Subunit structure

Interacts with HIV-1 Nef. Ref.1

Subcellular location

Peroxisome.

Tissue specificity

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

Induction

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

Sequence similarities

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

Ontologies

Keywords
   Biological processHost-virus interaction
Peroxisome biogenesis
   Cellular componentPeroxisome
   Molecular functionHydrolase
Serine esterase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacyl-CoA metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

alpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

bile acid biosynthetic process

Traceable author statement. Source: Reactome

bile acid metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

dicarboxylic acid catabolic process

Inferred from direct assay PubMed 16141203. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

peroxisome fission

Inferred from direct assay Ref.6. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionacyl-CoA hydrolase activity

Inferred from direct assay Ref.3Ref.6. Source: UniProtKB

choloyl-CoA hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

medium-chain acyl-CoA hydrolase activity

Inferred from direct assay Ref.1. Source: UniProtKB

palmitoyl-CoA hydrolase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.1. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nefP046015EBI-1237371,EBI-6164028From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Acyl-coenzyme A thioesterase 8
PRO_0000202152

Regions

Motif317 – 3193Microbody targeting signal Potential

Sites

Active site2321Charge relay system By similarity
Active site2541Charge relay system By similarity
Active site3041Charge relay system By similarity

Experimental info

Sequence conflict291 – 2933LWR → VWS in CAA60024. Ref.2
Sequence conflict3191L → R in CAA60024. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O14734 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8345C6E5EABF3326

FASTA31935,914
        10         20         30         40         50         60 
MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV 

        70         80         90        100        110        120 
GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP 

       130        140        150        160        170        180 
IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA 

       190        200        210        220        230        240 
QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL 

       250        260        270        280        290        300 
LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV 

       310 
TCAQEGVIRV KPQVSESKL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13378.1.
PIRJC5644.
RefSeqNP_005460.2. NM_005469.3.
UniGeneHs.444776.

3D structure databases

ProteinModelPortalO14734.
SMRO14734. Positions 37-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115323. 7 interactions.
IntActO14734. 5 interactions.
MINTMINT-2998229.
STRING9606.ENSP00000217455.

PTM databases

PhosphoSiteO14734.

Proteomic databases

MaxQBO14734.
PaxDbO14734.
PRIDEO14734.

Protocols and materials databases

DNASU10005.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217455; ENSP00000217455; ENSG00000101473.
GeneID10005.
KEGGhsa:10005.
UCSCuc002xqa.2. human.

Organism-specific databases

CTD10005.
GeneCardsGC20M044470.
HGNCHGNC:15919. ACOT8.
HPACAB010261.
MIM608123. gene.
neXtProtNX_O14734.
PharmGKBPA33941.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1946.
HOGENOMHOG000246495.
HOVERGENHBG019167.
InParanoidO14734.
KOK11992.
OMAHAYFLLI.
OrthoDBEOG7VTDNQ.
PhylomeDBO14734.
TreeFamTF315124.

Enzyme and pathway databases

BRENDA3.1.2.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO14734.
BgeeO14734.
CleanExHS_ACOT8.
GenevestigatorO14734.

Family and domain databases

Gene3D3.10.129.10. 2 hits.
InterProIPR003703. Acyl_CoA_thio.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERPTHR11066. PTHR11066. 1 hit.
SUPFAMSSF54637. SSF54637. 2 hits.
TIGRFAMsTIGR00189. tesB. 1 hit.
ProtoNetSearch...

Other

GeneWikiACOT8.
GenomeRNAi10005.
NextBio37789.
PROO14734.
SOURCESearch...

Entry information

Entry nameACOT8_HUMAN
AccessionPrimary (citable) accession number: O14734
Secondary accession number(s): O15261, Q17RX4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM