Reviewed, UniProtKB/Swiss-Prot Q9QYR9 (ACOT2_MOUSE)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A thioesterase 2, mitochondrial
      Short name=Acyl-CoA thioesterase 2
    EC=3.1.2.2
Alternative name(s):
    Acyl coenzyme A thioester hydrolase
    Very-long-chain acyl-CoA thioesterase
    MTE-I

Gene names

Name:	Acot2
Synonyms:	Mte1

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	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Most active on substrates with chain lengths ranging from C14-C20 By similarity.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Monomer.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Highly expressed in brown and white adipose tissue, muscle, heart, kidney, lung, adrenal gland and spleen; weakly expressed in intestine, testis and brain. 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Ref.1 Traceable author statement. Source: MGI
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Transit peptide	1 – 42	42	Mitochondrion Potential
	Chain	43 – 453	411	Acyl-coenzyme A thioesterase 2, mitochondrial		PRO_0000034065
Sites
	Active site	273	1	Charge relay system By similarity
	Active site	365	1	Charge relay system By similarity
	Active site	399	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	83	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9QYR9-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 305007E9F51CD9D4	FASTA	453	49,652
	10 20 30 40 50 60 MVASSFAVLR ASRLCQQDWK SWARLFVPPP LSTGGRTTWA RTNATLSVEP EGRSCWDEPL 70 80 90 100 110 120 SIAVRGLAPE QPVTLRSALR DEKGALFRAH ARYRADAGGE LNLARAPALG GSFSGLEPMG 130 140 150 160 170 180 LLWAMEPERP LWRLIKRDVQ TPFLVELEVL DGHEPDGGQR LAHAVHERHF LAPGVRRVPV 190 200 210 220 230 240 REGRVRATLF LPPEPGPFPG IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKS 250 260 270 280 290 300 IETMHMEYFE EAVNYLRSHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA 310 320 330 340 350 360 AVGNTISYKD ETIPPVSLVR NQVKMTKDGL LDVVEALQSP LVDKKSFIPV ERSDTTFLFL 370 380 390 400 410 420 VGQDDHNWKS EFYADEISKR LQAHGKEKPQ IICYPAAGHY IEPPYFPLCS AGMHLLVGAN 430 440 450 ITFGGEPRAH AVAQVDAWQQ LQTFFHKQLG SKS

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], 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 [GENOMIC DNA], CHARACTERIZATION, INDUCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF180798, AF180796, AF180797 Genomic DNA. Translation: AAF13871.1.
IPI	IPI00136683.
UniGene	Mm.1978
3D structure databases
SMR	Q9QYR9. Positions 177-402.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QYR9.
Proteomic databases
PRIDE	Q9QYR9.
Genome annotation databases
Ensembl	ENSMUST00000021649; ENSMUSP00000021649; ENSMUSG00000021226; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:2159605. Acot2.
Phylogenomic databases
HOGENOM	HBG713807.
HOVERGEN	Q9QYR9.
InParanoid	Q9QYR9.
Enzyme and pathway databases
BRENDA	3.1.2.2. 244.
Gene expression databases
ArrayExpress	Q9QYR9.
Bgee	Q9QYR9.
Genevestigator	Q9QYR9.
GermOnline	ENSMUSG00000021226. Mus musculus.
Family and domain databases
InterPro	IPR016662. Acyl-CoA_thioEstase_long-chain. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view]
Pfam	PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view]
PIRSF	PIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ACOT2_MOUSE

Accession

Primary (citable) accession number: Q9QYR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 1, 2000
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)