Reviewed, UniProtKB/Swiss-Prot Q8VHK0 (ACOT8_RAT)

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
    Peroxisomal acyl-CoA thioesterase 2
      Short name=PTE-2

Gene names

Name:	Acot8
Synonyms:	Pte1, Pte2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA (chenodeoxycholoyl-CoA) substrate. Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation. Ref.1
Catalytic activity	Choloyl-CoA + H2O = cholate + CoA.
Subcellular location	Peroxisome.
Induction	In the liver, by peroxisome proliferator or fasting via the peroxisome proliferator-activated receptors (PPARs). Ref.1
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.

Ontologies

Keywords
Biological process	Peroxisome biogenesis
Cellular component	Peroxisome
Molecular function	Hydrolase Serine esterase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	peroxisome organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW choloyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 320	320	Acyl-coenzyme A thioesterase 8		PRO_0000202154
Regions
	Motif	318 – 320	3	Microbody targeting signal Potential
Sites
	Active site	233	1	Charge relay system By similarity
	Active site	255	1	Charge relay system By similarity
	Active site	305	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	319	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8VHK0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: E0EAB4B7D26C79C0	FASTA	320	36,003
	10 20 30 40 50 60 MSKPEDLGDA NGDADRGDLS GDLRSVLVTS VLNLEPLDED LYRGRHYWVP TSQRLFGGQI 70 80 90 100 110 120 VGQALVAAAK SVSEDVHVHS LHCYFVRAGD PKVPVLYHVE RTRTGASFSV RAVKAVQHGK 130 140 150 160 170 180 AIFICQASFQ QMQPSPLQHQ FSMPTVPPPE ELLDHEALID QYLRDPNLHE KYRVGLNRIA 190 200 210 220 230 240 AREVPIEIKL VNPPALNQLQ TLEPKQMFWV RARGYIGEGD IKMHCCVAAY ISDYAFLGTA 250 260 270 280 290 300 LLPHQSKYKV NFMVSLDHSM WFHAPFRADH WMLYECESPW AGGSRGLVHG RLWRRDGVLA 310 320 VTCAQEGVIR SKPRVSESKL

References

[1]	"Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved." Ofman R., el Mrabet L., Dacremont G., Spijer D., Wanders R.J. Biochem. Biophys. Res. Commun. 290:629-634(2002) [PubMed: 11785945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF452100 mRNA. Translation: AAL66289.1.
IPI	IPI00207110.
UniGene	Rn.161868
3D structure databases
HSSP	HSSP built from PDB template 1C8U based on UniProtKB P23911.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8VHK0.
Genome annotation databases
Ensembl	ENSRNOT00000020740; ENSRNOP00000020740; ENSRNOG00000015187; Rattus norvegicus. [Genome view]
UCSC	NM_130756. rat.
Organism-specific databases
RGD	70368. Pte1.
Phylogenomic databases
HOVERGEN	Q8VHK0.
Enzyme and pathway databases
BRENDA	3.1.2.2. 248. 3.1.2.20. 248. 3.1.2.27. 248.
Gene expression databases
ArrayExpress	Q8VHK0.
Genevestigator	Q8VHK0.
GermOnline	ENSRNOG00000015187. Rattus norvegicus.
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...

Entry information

Entry name

ACOT8_RAT

Accession

Primary (citable) accession number: Q8VHK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	March 1, 2002
Last modified:	October 13, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)