Reviewed, UniProtKB/Swiss-Prot P58137 (ACOT8_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	320 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. 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. May be involved in the metabolic regulation of peroxisome proliferation.
Catalytic activity	Choloyl-CoA + H2O = cholate + CoA.
Enzyme regulation	Inhibited by CoASH (IC50= 10-15uM). Also inhibited by cysteine-reactive agents.
Subcellular location	Peroxisome.
Tissue specificity	Ubiquitous.
Induction	Induced in the liver, by peroxisome proliferator or fasting via the peroxisome proliferator-activated receptors (PPARs). Diurnal regulation of its expression.
Miscellaneous	Constitutes about 1% of total peroxisomal protein.
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.
Biophysicochemical properties	Kinetic parameters: In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 µM, and with short-chain acyl CoAs range from 8 to 30 µM. KM for bile acid-CoA esters is in the range 6-15 µM. KM=29.4 µM for acetyl-CoA KM=8.0 µM for propionyl-CoA KM=22.6 µM for butyryl-CoA KM=23.4 µM for hexanoyl-CoA KM=6.9 µM for octanoyl-CoA KM=2.9 µM for decanoyl-CoA KM=2.5 µM for miristoyl-CoA KM=1.7 µM for palmitoyl-CoA KM=1.4 µM for palmitoleoyl-CoA KM=1.6 µM for oleoyl-CoA KM=4.2 µM for arachidoyl-CoA KM=6.7 µM for arachidonoyl-CoA KM=6.3 µM for trihydroxycoprostanoyl-CoA KM=14.6 µM for choloyl-CoA KM=8.8 µM for chenodeoxycholoyl-CoA

Ontologies

Keywords
Biological process	Peroxisome biogenesis
Cellular component	Peroxisome
Molecular function	Hydrolase Serine esterase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Ref.1 Inferred from direct assay. Source: MGI peroxisome organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI peroxisome Inferred from direct assay. Source: HGNC
Molecular function	acyl-CoA thioesterase activity Ref.1 Inferred from direct assay. Source: MGI 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_0000202153
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 Ref.3
	Modified residue	319	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	284	1	S → F in AAL35333. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P58137-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 94F6AFCFEEE2FA23	FASTA	320	35,827
	10 20 30 40 50 60 MSAPEGLGDA HGDADRGDLS GDLRSVLVTS VLNLEPLDED LYRGRHYWVP TSQRLFGGQI 70 80 90 100 110 120 MGQALVAAAK SVSEDVHVHS LHCYFVRAGD PKVPVLYHVE RIRTGASFSV RAVKAVQHGK 130 140 150 160 170 180 AIFICQASFQ QMQPSPLQHQ FSMPSVPPPE DLLDHEALID QYLRDPNLHK KYRVGLNRVA 190 200 210 220 230 240 AQEVPIEIKV VNPPTLTQLQ ALEPKQMFWV RARGYIGEGD IKMHCCVAAY ISDYAFLGTA 250 260 270 280 290 300 LLPHQSKYKV NFMASLDHSM WFHAPFRADH WMLYECESPW AGGSRGLVHG RLWRRDGVLA 310 320 VTCAQEGVIR LKPQVSESKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of an acyl-CoA thioesterase that functions as a major regulator of peroxisomal lipid metabolism." Hunt M.C., Solaas K., Kase B.F., Alexson S.E.H. J. Biol. Chem. 277:1128-1138(2002) [PubMed: 11673457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Strain: 129/Sv.
[2]	"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].
[3]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF441166 mRNA. Translation: AAL35333.1. BC005792 mRNA. Translation: AAH05792.1.
IPI	IPI00309365.
RefSeq	NP_573503.2.
UniGene	Mm.277878
3D structure databases
SMR	P58137. Positions 29-312.
ModBase	Search...
Protein-protein interaction databases
STRING	P58137.
PTM databases
PhosphoSite	P58137.
Proteomic databases
PRIDE	P58137.
Genome annotation databases
Ensembl	ENSMUST00000103094; ENSMUSP00000099383; ENSMUSG00000017307; Mus musculus. [Genome view]
GeneID	170789.
KEGG	mmu:170789.
Organism-specific databases
CTD	170789.
MGI	MGI:2158201. Acot8.
Phylogenomic databases
eggNOG	roNOG06020.
HOGENOM	HBG736737.
HOVERGEN	P58137.
InParanoid	P58137.
OMA	KYRVGLN.
PhylomeDB	P58137.
Enzyme and pathway databases
BRENDA	3.1.2.2. 244. 3.1.2.20. 244. 3.1.2.27. 244.
Gene expression databases
ArrayExpress	P58137.
Bgee	P58137.
CleanEx	MM_ACOT8.
Genevestigator	P58137.
GermOnline	ENSMUSG00000017307. Mus musculus.
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	370427.
SOURCE	Search...

Entry information

Entry name

ACOT8_MOUSE

Accession

Primary (citable) accession number: P58137
Secondary accession number(s): Q8VHM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)