ACOT2_RAT
ID ACOT2_RAT Reviewed; 453 AA.
AC O55171; O88268;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Acyl-coenzyme A thioesterase 2, mitochondrial;
DE Short=Acyl-CoA thioesterase 2;
DE EC=3.1.2.2 {ECO:0000269|PubMed:7744868};
DE AltName: Full=ARTISt/p43;
DE AltName: Full=Acyl coenzyme A thioester hydrolase;
DE AltName: Full=MTE-I {ECO:0000303|PubMed:7744868};
DE AltName: Full=Very-long-chain acyl-CoA thioesterase {ECO:0000303|PubMed:7744868};
DE Flags: Precursor;
GN Name=Acot2; Synonyms=Mte1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 147-166 AND 168-178.
RC STRAIN=Sprague-Dawley;
RX PubMed=9445388; DOI=10.1042/bj3290601;
RA Svensson L.T., Engberg S.T., Aoyama T., Usuda N., Alexson S.E.H.,
RA Hashimoto T.;
RT "Molecular cloning and characterization of a mitochondrial peroxisome
RT proliferator-induced acyl-CoA thioesterase from rat liver.";
RL Biochem. J. 329:601-608(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-197.
RC TISSUE=Liver;
RX PubMed=9703974; DOI=10.1006/bbrc.1998.9048;
RA Yamada J., Suga K., Furihata T., Kitahara M., Watanabe T., Hosokawa M.,
RA Satoh T., Suga T.;
RT "cDNA cloning and genomic organization of peroxisome proliferator-inducible
RT long-chain acyl-CoA hydrolase from rat liver cytosol.";
RL Biochem. Biophys. Res. Commun. 248:608-612(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION BY
RP DI(2-ETHYLHEXYL)PHTALATE, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7744868; DOI=10.1074/jbc.270.20.12177;
RA Svensson L.T., Alexson S.E., Hiltunen J.K.;
RT "Very long chain and long chain acyl-CoA thioesterases in rat liver
RT mitochondria. Identification, purification, characterization, and induction
RT by peroxisome proliferators.";
RL J. Biol. Chem. 270:12177-12183(1995).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (By similarity). Displays higher activity toward long chain acyl
CC CoAs (C14-C20) (PubMed:7744868). The enzyme is involved in enhancing
CC the hepatic fatty acid oxidation in mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:7744868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:7744868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:7744868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:7744868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:7744868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000269|PubMed:7744868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:7744868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC Evidence={ECO:0000269|PubMed:7744868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000305|PubMed:7744868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:7744868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:7744868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:7744868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:7744868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000250|UniProtKB:P49753};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000250|UniProtKB:P49753};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540;
CC Evidence={ECO:0000250|UniProtKB:P49753};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000250|UniProtKB:P49753};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537;
CC Evidence={ECO:0000250|UniProtKB:P49753};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724;
CC Evidence={ECO:0000250|UniProtKB:P49753};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate
CC + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:Q9QYR9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC Evidence={ECO:0000250|UniProtKB:Q9QYR9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for C10-acyl-CoA {ECO:0000269|PubMed:7744868};
CC KM=5 uM for C12-acyl-CoA {ECO:0000269|PubMed:7744868};
CC KM=3 uM for C14-acyl-CoA {ECO:0000269|PubMed:7744868};
CC KM=6 uM for C16-acyl-CoA {ECO:0000269|PubMed:7744868};
CC KM=3 uM for C18-acyl-CoA {ECO:0000269|PubMed:7744868};
CC KM=2 uM for C20-acyl-CoA {ECO:0000269|PubMed:7744868};
CC Vmax=1 umol/min/mg enzyme with C10-acyl-CoA as substrate
CC {ECO:0000269|PubMed:7744868};
CC Vmax=2.2 umol/min/mg enzyme with C12-acyl-CoA as substrate
CC {ECO:0000269|PubMed:7744868};
CC Vmax=4.2 umol/min/mg enzyme with C14-acyl-CoA as substrate
CC {ECO:0000269|PubMed:7744868};
CC Vmax=4.5 umol/min/mg enzyme with C16-acyl-CoA as substrate
CC {ECO:0000269|PubMed:7744868};
CC Vmax=3.3 umol/min/mg enzyme with C18-acyl-CoA as substrate
CC {ECO:0000269|PubMed:7744868};
CC Vmax=3.1 umol/min/mg enzyme with C20-acyl-CoA as substrate
CC {ECO:0000269|PubMed:7744868};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:7744868};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:7744868}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7744868}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:7744868}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in heart and brown fat.
CC Strongly induced in liver, and weakly in kidney, in peroxisome
CC proliferator treated rat. {ECO:0000269|PubMed:7744868}.
CC -!- INDUCTION: Regulated by peroxisome proliferator, via the peroxisome
CC proliferator-activated receptors (PPARs). {ECO:0000269|PubMed:7744868}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; Y09333; CAA70513.1; -; mRNA.
DR EMBL; AB010429; BAA32539.1; -; mRNA.
DR AlphaFoldDB; O55171; -.
DR SMR; O55171; -.
DR STRING; 10116.ENSRNOP00000013515; -.
DR ESTHER; ratno-acot2; Acyl-CoA_Thioesterase.
DR iPTMnet; O55171; -.
DR PhosphoSitePlus; O55171; -.
DR jPOST; O55171; -.
DR PaxDb; O55171; -.
DR PRIDE; O55171; -.
DR UCSC; RGD:621055; rat.
DR RGD; 621055; Acot2.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR InParanoid; O55171; -.
DR PhylomeDB; O55171; -.
DR BRENDA; 3.1.2.2; 5301.
DR BRENDA; 3.1.2.20; 5301.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00199; -.
DR PRO; PR:O55171; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:RGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:RGD.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:HGNC-UCL.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Mitochondrion; Reference proteome; Serine esterase;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..453
FT /note="Acyl-coenzyme A thioesterase 2, mitochondrial"
FT /id="PRO_0000034066"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49753"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49753"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49753"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR9"
FT MOD_RES 447
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR9"
FT CONFLICT 51..52
FT /note="GS -> AG (in Ref. 2; BAA32539)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..92
FT /note="HAR -> RAL (in Ref. 2; BAA32539)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="W -> R (in Ref. 2; BAA32539)"
FT /evidence="ECO:0000305"
SQ 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