Reviewed, UniProtKB/Swiss-Prot O14734 (ACOT8_HUMAN)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A thioesterase 8
    EC=3.1.2.27
Alternative name(s):
    Choloyl-coenzyme A thioesterase
    Acyl-CoA thioesterase 8
    Peroxisomal acyl-coenzyme A thioester hydrolase 1
      Short name=PTE-1
    Peroxisomal long-chain acyl-CoA thioesterase 1
    HIV-Nef-associated acyl-CoA thioesterase
    Thioesterase II
      Short name=hTE
      Short name=hACTEIII
      Short name=hACTE-III
    PTE-2

Gene names

Name:	ACOT8
Synonyms:	ACTEIII, PTE1, PTE2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Choloyl-CoA + H(2)O = 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
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW peroxisome organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Ref.3 Traceable author statement. Source: ProtInc
Molecular function	acyl-CoA thioesterase activity Ref.3 Traceable author statement. Source: ProtInc carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW choloyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC protein binding Ref.2 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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
	Modified residue	3	1	Phosphoserine Ref.8
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)
	O14734-1 [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: 9299485] [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: 9153233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphoid.
[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: 10092594] [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: 11780052] [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: 15489334] [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: 15194431] [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: 11755680] [Abstract] Cited for: REVIEW.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	JC5644.
RefSeq	NP_005460.2. NP_899242.1.
UniGene	Hs.444776
3D structure databases
HSSP	HSSP built from PDB template 1C8U based on UniProtKB P23911.
ModBase	Search...
PTM databases
PhosphoSite	O14734.
Proteomic databases
PRIDE	O14734.
Genome annotation databases
Ensembl	ENSG00000101473. Homo sapiens. [Contig view]
GeneID	10005.
KEGG	hsa:10005.
Organism-specific databases
GeneCards	GC20M043904.
H-InvDB	HIX0015865.
HGNC	HGNC:15919. ACOT8.
HPA	CAB010261.
MIM	608123. gene.
PharmGKB	PA33941.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O14734.
HOVERGEN	O14734.
Enzyme and pathway databases
Reactome	REACT_602. Lipid and lipoprotein metabolism.
Gene expression databases
ArrayExpress	O14734.
CleanEx	HS_ACOT8.
GermOnline	ENSG00000101473. Homo sapiens.
Family and domain databases
InterPro	IPR003703. Acyl_CoA_thio. [Graphical view]
PANTHER	PTHR11066. Acyl_CoA_thio. 1 hit.
Pfam	PF02551. Acyl_CoA_thio. 2 hits. [Graphical view]
TIGRFAMs	TIGR00189. tesB. 1 hit.
ProtoNet	Search...
Other Resources
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:	December 16, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)