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Acyl-coenzyme A thioesterase 2, mitochondrial (Acyl-CoA thioesterase 2) (EC 3.1.2.2) (ARTISt/p43) (Acyl coenzyme A thioester hydrolase) (MTE-I) (Very-long-chain acyl-CoA thioesterase)

 ACOT2_RAT               Reviewed;         453 AA.
O55171; O88268;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
10-MAY-2017, entry version 112.
RecName: Full=Acyl-coenzyme A thioesterase 2, mitochondrial;
Short=Acyl-CoA thioesterase 2;
EC=3.1.2.2 {ECO:0000269|PubMed:7744868};
AltName: Full=ARTISt/p43;
AltName: Full=Acyl coenzyme A thioester hydrolase;
AltName: Full=MTE-I {ECO:0000303|PubMed:7744868};
AltName: Full=Very-long-chain acyl-CoA thioesterase {ECO:0000303|PubMed:7744868};
Flags: Precursor;
Name=Acot2; Synonyms=Mte1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 147-166 AND
168-178.
STRAIN=Sprague-Dawley;
PubMed=9445388; DOI=10.1042/bj3290601;
Svensson L.T., Engberg S.T., Aoyama T., Usuda N., Alexson S.E.H.,
Hashimoto T.;
"Molecular cloning and characterization of a mitochondrial peroxisome
proliferator-induced acyl-CoA thioesterase from rat liver.";
Biochem. J. 329:601-608(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-197.
TISSUE=Liver;
PubMed=9703974; DOI=10.1006/bbrc.1998.9048;
Yamada J., Suga K., Furihata T., Kitahara M., Watanabe T.,
Hosokawa M., Satoh T., Suga T.;
"cDNA cloning and genomic organization of peroxisome proliferator-
inducible long-chain acyl-CoA hydrolase from rat liver cytosol.";
Biochem. Biophys. Res. Commun. 248:608-612(1998).
[3]
FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY DI(2-ETHYLHEXYL)PHTALATE,
SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7744868; DOI=10.1074/jbc.270.20.12177;
Svensson L.T., Alexson S.E., Hiltunen J.K.;
"Very long chain and long chain acyl-CoA thioesterases in rat liver
mitochondria. Identification, purification, characterization, and
induction by peroxisome proliferators.";
J. Biol. Chem. 270:12177-12183(1995).
-!- 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.
{ECO:0000269|PubMed:7744868}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
{ECO:0000269|PubMed:7744868}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=16 uM for C10-acyl-CoA {ECO:0000269|PubMed:7744868};
KM=5 uM for C12-acyl-CoA {ECO:0000269|PubMed:7744868};
KM=3 uM for C14-acyl-CoA {ECO:0000269|PubMed:7744868};
KM=6 uM for C16-acyl-CoA {ECO:0000269|PubMed:7744868};
KM=3 uM for C18-acyl-CoA {ECO:0000269|PubMed:7744868};
KM=2 uM for C20-acyl-CoA {ECO:0000269|PubMed:7744868};
Vmax=1 umol/min/mg enzyme for C10-acyl-CoA
{ECO:0000269|PubMed:7744868};
Vmax=2.2 umol/min/mg enzyme for C12-acyl-CoA
{ECO:0000269|PubMed:7744868};
Vmax=4.2 umol/min/mg enzyme for C14-acyl-CoA
{ECO:0000269|PubMed:7744868};
Vmax=4.5 umol/min/mg enzyme for C16-acyl-CoA
{ECO:0000269|PubMed:7744868};
Vmax=3.3 umol/min/mg enzyme for C18-acyl-CoA
{ECO:0000269|PubMed:7744868};
Vmax=3.1 umol/min/mg enzyme for C20-acyl-CoA
{ECO:0000269|PubMed:7744868};
pH dependence:
Optimum pH is 8-9. {ECO:0000269|PubMed:7744868};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7744868}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:7744868}.
-!- TISSUE SPECIFICITY: Constitutively expressed in heart and brown
fat. Strongly induced in liver, and weakly in kidney, in
peroxisome proliferator treated rat. {ECO:0000269|PubMed:7744868}.
-!- INDUCTION: Regulated by peroxisome proliferator, via the
peroxisome proliferator-activated receptors (PPARs).
{ECO:0000269|PubMed:7744868}.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y09333; CAA70513.1; -; mRNA.
EMBL; AB010429; BAA32539.1; -; mRNA.
UniGene; Rn.37524; -.
ProteinModelPortal; O55171; -.
SMR; O55171; -.
STRING; 10116.ENSRNOP00000013515; -.
ESTHER; ratno-acot2; Acyl-CoA_Thioesterase.
iPTMnet; O55171; -.
PhosphoSitePlus; O55171; -.
PaxDb; O55171; -.
PRIDE; O55171; -.
UCSC; RGD:621055; rat.
RGD; 621055; Acot2.
eggNOG; ENOG410II3X; Eukaryota.
eggNOG; COG1073; LUCA.
HOGENOM; HOG000116219; -.
HOVERGEN; HBG000331; -.
InParanoid; O55171; -.
PhylomeDB; O55171; -.
BRENDA; 3.1.2.2; 5301.
BRENDA; 3.1.2.20; 5301.
PRO; PR:O55171; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:RGD.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:RGD.
GO; GO:0006637; P:acyl-CoA metabolic process; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:HGNC.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:RGD.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
InterPro; IPR014940; BAAT_C.
InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
Pfam; PF08840; BAAT_C; 1.
Pfam; PF04775; Bile_Hydr_Trans; 1.
PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
SUPFAM; SSF53474; SSF53474; 2.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Hydrolase;
Mitochondrion; Reference proteome; Serine esterase; Transit peptide.
TRANSIT 1 42 Mitochondrion. {ECO:0000255}.
CHAIN 43 453 Acyl-coenzyme A thioesterase 2,
mitochondrial.
/FTId=PRO_0000034066.
ACT_SITE 273 273 Charge relay system.
{ECO:0000250|UniProtKB:P49753}.
ACT_SITE 365 365 Charge relay system.
{ECO:0000250|UniProtKB:P49753}.
ACT_SITE 399 399 Charge relay system.
{ECO:0000250|UniProtKB:P49753}.
MOD_RES 83 83 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9QYR9}.
MOD_RES 447 447 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9QYR9}.
CONFLICT 51 52 GS -> AG (in Ref. 2; BAA32539).
{ECO:0000305}.
CONFLICT 90 92 HAR -> RAL (in Ref. 2; BAA32539).
{ECO:0000305}.
CONFLICT 123 123 W -> R (in Ref. 2; BAA32539).
{ECO:0000305}.
SEQUENCE 453 AA; 49701 MW; F48C2C61475072B2 CRC64;
MVASSFAVLR ASRLCQWGWK SWTQLSGPPP LSTGGRTTFA RTNATLSLEP GSRSCWDEPL
SITVRGLAPE QPVTLRAALR DEKGALFRAH ARYRADAGGE LDLARAPALG GSFTGLEPMG
LIWAMEPERP LWRLVKRDVQ KPYVVELEVL DGHEPDGGQR LAQAVHERHF MAPGVRRVPV
RDGRVRATLF LPPEPGPFPE IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKT
METMRIEYFE EAVNYLRGHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA
AVGNTVCYKD ETIPPVSLLR DKVKMTKDGL LDVVEALQSP LVDKKSFIPV ERSDTTFLFL
VGQDDHNWKS EFYAREASKR LQAHGKEKPQ IICYPEAGHY IEPPYFPLCS AGMHLLVGAN
ITFGGEPKPH SVAQLDAWQQ LQTFFHKQLS GKS


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