Reviewed, UniProtKB/Swiss-Prot O55171 (ACOT2_RAT)

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
    ARTISt/p43

Gene names

Name:	Acot2
Synonyms:	Mte1

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	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.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Constitutively expressed in heart and brown fat. Strongly induced in liver, and weakly in kidney, in peroxisome proliferator treated rat.
Induction	Regulated by peroxisome proliferator, via the peroxisome proliferator-activated receptors (PPARs).
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8-9.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro response to hypoxia Inferred from direct assay. Source: HGNC
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_0000034066
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
Experimental info
	Sequence conflict	51 – 52	2	GS → AG in BAA32539. Ref.2
	Sequence conflict	90 – 92	3	HAR → RAL in BAA32539. Ref.2
	Sequence conflict	123	1	W → R in BAA32539. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O55171-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F48C2C61475072B2	FASTA	453	49,701
	10 20 30 40 50 60 MVASSFAVLR ASRLCQWGWK SWTQLSGPPP LSTGGRTTFA RTNATLSLEP GSRSCWDEPL 70 80 90 100 110 120 SITVRGLAPE QPVTLRAALR DEKGALFRAH ARYRADAGGE LDLARAPALG GSFTGLEPMG 130 140 150 160 170 180 LIWAMEPERP LWRLVKRDVQ KPYVVELEVL DGHEPDGGQR LAQAVHERHF MAPGVRRVPV 190 200 210 220 230 240 RDGRVRATLF LPPEPGPFPE IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKT 250 260 270 280 290 300 METMRIEYFE EAVNYLRGHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA 310 320 330 340 350 360 AVGNTVCYKD ETIPPVSLLR DKVKMTKDGL LDVVEALQSP LVDKKSFIPV ERSDTTFLFL 370 380 390 400 410 420 VGQDDHNWKS EFYAREASKR LQAHGKEKPQ IICYPEAGHY IEPPYFPLCS AGMHLLVGAN 430 440 450 ITFGGEPKPH SVAQLDAWQQ LQTFFHKQLS GKS

References

[1]	"Molecular cloning and characterization of a mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver." Svensson L.T., Engberg S.T., Aoyama T., Usuda N., Alexson S.E.H., Hashimoto T. Biochem. J. 329:601-608(1998) [PubMed: 9445388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 147-166 AND 168-178. Strain: Sprague-Dawley.
[2]	"cDNA cloning and genomic organization of peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol." Yamada J., Suga K., Furihata T., Kitahara M., Watanabe T., Hosokawa M., Satoh T., Suga T. Biochem. Biophys. Res. Commun. 248:608-612(1998) [PubMed: 9703974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-197. Tissue: Liver.
[3]	"Very long chain and long chain acyl-CoA thioesterases in rat liver mitochondria. Identification, purification, characterization, and induction by peroxisome proliferators." Svensson L.T., Alexson S.E., Hiltunen J.K. J. Biol. Chem. 270:12177-12183(1995) [PubMed: 7744868] [Abstract] Cited for: CHARACTERIZATION. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y09333 mRNA. Translation: CAA70513.1. AB010429 mRNA. Translation: BAA32539.1.
IPI	IPI00421885.
UniGene	Rn.37524
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O55171.
Genome annotation databases
Ensembl	ENSRNOT00000013515; ENSRNOP00000013515; ENSRNOG00000010134; Rattus norvegicus. [Genome view]
UCSC	NM_138907. rat.
Organism-specific databases
RGD	621055. Mte1.
Phylogenomic databases
HOVERGEN	O55171.
Enzyme and pathway databases
BRENDA	3.1.2.2. 248. 3.1.2.20. 248.
Gene expression databases
ArrayExpress	O55171.
Genevestigator	O55171.
GermOnline	ENSRNOG00000010134. Rattus norvegicus.
Family and domain databases
InterPro	IPR016662. Acyl-CoA_thioEstase_long-chain. IPR014940. BAAT_C. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view]
Pfam	PF08840. BAAT_C. 1 hit. PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view]
PIRSF	PIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACOT2_RAT

Accession

Primary (citable) accession number: O55171
Secondary accession number(s): O88268

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	October 13, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)