ACOT1_RAT
ID ACOT1_RAT Reviewed; 419 AA.
AC O88267; O55161;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acyl-coenzyme A thioesterase 1 {ECO:0000305|PubMed:7906114};
DE Short=Acyl-CoA thioesterase 1 {ECO:0000305|PubMed:7906114};
DE EC=3.1.2.- {ECO:0000269|PubMed:7906114};
DE AltName: Full=CTE-I;
DE AltName: Full=Inducible cytosolic acyl-coenzyme A thioester hydrolase;
DE AltName: Full=LACH2;
DE Short=ACH2;
DE AltName: Full=Long chain acyl-CoA thioester hydrolase;
DE Short=Long chain acyl-CoA hydrolase;
DE AltName: Full=Palmitoyl-coenzyme A thioesterase {ECO:0000305|PubMed:7906114};
DE EC=3.1.2.2 {ECO:0000269|PubMed:7906114};
GN Name=Acot1; Synonyms=Cte1;
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 13-34; 85-107; 187-198;
RP 312-324 AND 374-338.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 106-122.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9490035; DOI=10.1046/j.1432-1327.1998.2510631.x;
RA Lindquist P.J.G., Svensson L.T., Alexson S.E.H.;
RT "Molecular cloning of the peroxisome proliferator-induced 46-kDa cytosolic
RT acyl-CoA thioesterase from mouse and rat liver --recombinant expression in
RT Escherichia coli, tissue expression, and nutritional regulation.";
RL Eur. J. Biochem. 251:631-640(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=7906114; DOI=10.1006/abbi.1994.1017;
RA Yamada J., Matsumoto I., Furihata T., Sakuma M., Suga T.;
RT "Purification and properties of long-chain acyl-CoA hydrolases from the
RT liver cytosol of rats treated with peroxisome proliferator.";
RL Arch. Biochem. Biophys. 308:118-125(1994).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels. More active towards saturated and unsaturated long chain fatty
CC acyl-CoAs (C12-C20). {ECO:0000269|PubMed:7906114}.
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:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:7906114};
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:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:7906114};
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:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000250|UniProtKB:Q86TX2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000250|UniProtKB:Q86TX2};
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:0000250|UniProtKB:Q86TX2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q86TX2};
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:0000250|UniProtKB:Q86TX2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000250|UniProtKB:Q86TX2};
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:Q86TX2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000250|UniProtKB:Q86TX2};
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:Q86TX2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000250|UniProtKB:Q86TX2};
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:Q86TX2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724;
CC Evidence={ECO:0000250|UniProtKB:Q86TX2};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:7906114}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9490035}.
CC -!- TISSUE SPECIFICITY: Expressed in liver.
CC -!- INDUCTION: In the liver, by peroxisome proliferator (Clofibrate)
CC treatment, via the peroxisome proliferator-activated receptors (PPARs)
CC or fasting for 24 hours.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AB010428; BAA32434.1; -; mRNA.
DR EMBL; Y09334; CAA70514.1; -; mRNA.
DR PIR; JE0267; JE0267.
DR RefSeq; NP_112605.1; NM_031315.2.
DR AlphaFoldDB; O88267; -.
DR SMR; O88267; -.
DR STRING; 10116.ENSRNOP00000013729; -.
DR SwissLipids; SLP:000000588; -.
DR ESTHER; ratno-acot1; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A53; -.
DR iPTMnet; O88267; -.
DR PhosphoSitePlus; O88267; -.
DR PaxDb; O88267; -.
DR PRIDE; O88267; -.
DR GeneID; 50559; -.
DR KEGG; rno:50559; -.
DR UCSC; RGD:70894; rat.
DR CTD; 641371; -.
DR RGD; 70894; Acot1.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR InParanoid; O88267; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; O88267; -.
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:O88267; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
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; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP: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 Cytoplasm; Direct protein sequencing; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Serine esterase.
FT CHAIN 1..419
FT /note="Acyl-coenzyme A thioesterase 1"
FT /id="PRO_0000202157"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 8
FT /note="E -> G (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="I -> L (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> K (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="D -> N (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46013 MW; 6A0E828A08CEC7C9 CRC64;
MEATLSLEPA GRSCWDEPLS ITVRGLVPEQ PVTLRAALRD EKGALFRARA LYRADAHGEL
DLARAPALGG SFTGLEPMGL IWAMEPERPF WRLVKRDVQT PFVVELEVLD GHEPDGGRLL
ARAVHERHFM APGVRRVPVR EGRVRATLFL PPEPGPFPGI IDLFGVGGGL LEYRASLLAG
KGFAVMALAY YNYDDLPKTM ETMRIEYFEE AVNYLRGHPE VKGPGIGLLG ISKGGELGLA
MASFLKGITA AVVINGSVAA VGNTICYKDE TIPPVTILRN QVKMTKDGLK DVVDALQSPL
VEQKSFIPVE RSDTTFLFLV GQDDHNWKSE FYANEISKRL QAHGKEKPQI ICYPEAGHYI
EPPYFPLCSA GMHLLVGANI TFGGEPKPHS VAQLDAWQQL QTFFHKQLGG KSHGVSPKI
