O14734 (ACOT8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Host-virus interaction Peroxisome biogenesis
Cellular component	Peroxisome
Molecular function	Hydrolase Serine esterase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acyl-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 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 virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal matrix Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW choloyl-CoA hydrolase activity Inferred from electronic annotation. Source: 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nef	P04601	5	EBI-1237371,EBI-6164028	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	Acyl-coenzyme A thioesterase 8		PRO_0000202152
Regions
	Motif	317 – 319	3	Microbody targeting signal Potential
Sites
	Active site	232	1	Charge relay system By similarity
	Active site	254	1	Charge relay system By similarity
	Active site	304	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	2	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	291 – 293	3	LWR → VWS in CAA60024. Ref.2
	Sequence conflict	319	1	L → R in CAA60024. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O14734 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 8345C6E5EABF3326	FASTA	319	35,914
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00298202.
PIR	JC5644.
RefSeq	NP_005460.2. NM_005469.3.
UniGene	Hs.444776.
3D structure databases
ProteinModelPortal	O14734.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14734. 5 interactions.
STRING	9606.ENSP00000217455.
PTM databases
PhosphoSite	O14734.
Proteomic databases
PaxDb	O14734.
PRIDE	O14734.
Protocols and materials databases
DNASU	10005.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217455; ENSP00000217455; ENSG00000101473.
GeneID	10005.
KEGG	hsa:10005.
UCSC	uc002xqa.2. human.
Organism-specific databases
CTD	10005.
GeneCards	GC20M044470.
HGNC	HGNC:15919. ACOT8.
HPA	CAB010261.
MIM	608123. gene.
neXtProt	NX_O14734.
PharmGKB	PA33941.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1946.
HOGENOM	HOG000246495.
HOVERGEN	HBG019167.
InParanoid	O14734.
KO	K11992.
OMA	GRIHVWI.
OrthoDB	EOG45B1G0.
PhylomeDB	O14734.
Enzyme and pathway databases
BRENDA	3.1.2.2. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	O14734.
Bgee	O14734.
CleanEx	HS_ACOT8.
Genevestigator	O14734.
GermOnline	ENSG00000101473. Homo sapiens.
Family and domain databases
InterPro	IPR003703. Acyl_CoA_thio. [Graphical view]
PANTHER	PTHR11066. PTHR11066. 1 hit.
TIGRFAMs	TIGR00189. tesB. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10005.
NextBio	37789.
SOURCE	Search...

Entry information

Entry name

ACOT8_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.