O55137 (ACOT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A thioesterase 1
Short name=Acyl-CoA thioesterase 1
EC=3.1.2.2

Alternative name(s):
CTE-I
Inducible cytosolic acyl-coenzyme A thioester hydrolase
Long chain acyl-CoA thioester hydrolase
Short name=Long chain acyl-CoA hydrolase

Gene names

Name:	Acot1
Synonyms:	Cte1

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 › Mus

Protein attributes

Sequence length	419 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. True acyl-CoA thioesterase being highly specific for saturated C12-C20 acyl-CoAs, with only a very low activity with decanoyl-CoA as substrate. Most active on myristoyl- and palmitoyl-CoA. Introduction of one or two double bonds decreases the activity to about half. No detectable activity with bile acid CoAs such as choloyl-CoA and chenodeoxycholoyl-CoA. Ref.1
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in heart, kidney, brown adipose tissue, white adipose tissue, adrenal gland and muscle. Ref.1 Ref.2
Induction	In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours. Ref.2
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.
Biophysicochemical properties	Kinetic parameters: KM=2.6 µM for palmitoyl-CoA Ref.5 Vmax=1.2 µmol/min/mg enzyme with palmitoyl-CoA as substrate

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Serine esterase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Traceable author statement Ref.1. Source: MGI long-chain fatty acid metabolic process Inferred from direct assay Ref.5. Source: MGI
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-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 – 419	419	Acyl-coenzyme A thioesterase 1		PRO_0000202156
Sites
	Active site	232	1	Charge relay system Ref.5
	Active site	324	1	Charge relay system Ref.5
	Active site	358	1	Charge relay system Ref.5
Experimental info
	Mutagenesis	232	1	S → A: Abolishes activity. Ref.5
	Mutagenesis	232	1	S → C: Retains 2% of the initial activity; deacylation of the acyl-enzyme intermediate becomes rate-limiting. Ref.5
	Mutagenesis	324	1	D → A: Abolishes activity. Ref.5
	Mutagenesis	358	1	H → Q: Abolishes activity. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O55137 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 57346B6177471CFB	FASTA	419	46,136
	10 20 30 40 50 60 MEATLNLEPS GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGALFRAHA RYRADSHGEL 70 80 90 100 110 120 DLARTPALGG SFSGLEPMGL LWAMEPDRPF WRLVKRDVQT PFVVELEVLD GHEPDGGQRL 130 140 150 160 170 180 AHAVHERHFL APGVRRVPVR EGRVRATLFL PPEPGPFPGI IDLFGVGGGL LEYRASLLAG 190 200 210 220 230 240 KGFAVMALAY YNYDDLPKNM ETMHMEYFEE AVNYLRSHPE VKGPGIGLLG ISKGGELGLA 250 260 270 280 290 300 MASFLKGITA AVVINGSVAA VGNTISYKDE TIPPVTILRN QVKMTKDGLK DVVDALQSPL 310 320 330 340 350 360 VDKKSFIPVE RSDTTFLFLV GQDDHNWKSE FYADEISKRL QAHGKEKPQI ICYPAAGHYI 370 380 390 400 410 EPPYFPLCSA GMHLLVGANI TFGGEPKPHA MAQLDAWQQL QTFFHKQLGS ECLHVSPKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism." Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Alexson S.E.H. J. Biol. Chem. 274:34317-34326(1999) [PubMed: 10567408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY. Strain: C57BL/6.
[2]	"Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism." Hunt M.C., Lindquist P.J.G., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Aoyama T., Hashimoto T., Diczfalusy U., Alexson S.E.H. Cell Biochem. Biophys. 32:317-324(2000) [PubMed: 11330065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INDUCTION, TISSUE SPECIFICITY.
[3]	"Molecular cloning of the peroxisome proliferator-induced 46-kDa cytosolic acyl-CoA thioesterase from mouse and rat liver --recombinant expression in Escherichia coli, tissue expression, and nutritional regulation." Lindquist P.J.G., Svensson L.T., Alexson S.E.H. Eur. J. Biochem. 251:631-640(1998) [PubMed: 9490035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Liver.
[4]	"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]. Strain: FVB/N. Tissue: Liver.
[5]	"The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta hydrolase." Huhtinen K., O'Byrne J., Lindquist P.J.G., Contreras J.A., Alexson S.E.H. J. Biol. Chem. 277:3424-3432(2002) [PubMed: 11694534] [Abstract] Cited for: ACTIVE SITES, MUTAGENESIS OF SER-232; ASP-324 AND HIS-358, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF180795, AF180793, AF180794 Genomic DNA. Translation: AAF13870.1. Y14004 mRNA. Translation: CAA74327.1. BC028261 mRNA. Translation: AAH28261.1.
IPI	IPI00115871.
RefSeq	NP_036136.1. NM_012006.2.
UniGene	Mm.1978.
3D structure databases
ProteinModelPortal	O55137.
SMR	O55137. Positions 1-408.
ModBase	Search...
Protein-protein interaction databases
STRING	O55137.
PTM databases
PhosphoSite	O55137.
2D gel databases
UCD-2DPAGE	O55137.
Proteomic databases
PRIDE	O55137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000168120; ENSMUSP00000126448; ENSMUSG00000072949.
GeneID	26897.
KEGG	mmu:26897.
Organism-specific databases
CTD	641371.
MGI	MGI:1349396. Acot1.
Phylogenomic databases
eggNOG	roNOG10401.
HOVERGEN	HBG000331.
InParanoid	O55137.
OMA	IPPVTIL.
OrthoDB	EOG4QC15F.
Enzyme and pathway databases
BRENDA	3.1.2.2. 3474.
Gene expression databases
ArrayExpress	O55137.
Bgee	O55137.
CleanEx	MM_ACOT1.
Genevestigator	O55137.
GermOnline	ENSMUSG00000021226. Mus musculus.
Family and domain databases
InterPro	IPR016662. Acyl-CoA_thioEstase_long-chain. IPR014940. BAAT_C. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view]
KO	K01068.
Pfam	PF08840. BAAT_C. 1 hit. PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view]
PIRSF	PIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNet	Search...
Other
NextBio	304741.
SOURCE	Search...

Entry information

Entry name

ACOT1_MOUSE

Accession

Primary (citable) accession number: O55137
Secondary accession number(s): Q549A9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	November 16, 2011
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program