ACO12_RAT
ID ACO12_RAT Reviewed; 556 AA.
AC Q99NB7;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acetyl-coenzyme A thioesterase {ECO:0000305};
DE EC=3.1.2.1 {ECO:0000269|PubMed:11322891};
DE AltName: Full=Acyl-CoA thioester hydrolase 12;
DE AltName: Full=Acyl-coenzyme A thioesterase 12;
DE Short=Acyl-CoA thioesterase 12;
DE AltName: Full=Cytoplasmic acetyl-CoA hydrolase 1;
DE Short=CACH-1;
DE Short=rACH;
DE Short=rCACH-1;
GN Name=Acot12; Synonyms=Cach, Cach1;
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], PROTEIN SEQUENCE OF 161-174 AND 352-364,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=Donryu; TISSUE=Liver;
RX PubMed=11322891; DOI=10.1046/j.1432-1327.2001.02162.x;
RA Suematsu N., Okamoto K., Shibata K., Nakanishi Y., Isohashi F.;
RT "Molecular cloning and functional expression of rat liver cytosolic acetyl-
RT CoA hydrolase.";
RL Eur. J. Biochem. 268:2700-2709(2001).
RN [2]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=6136404; DOI=10.1111/j.1432-1033.1983.tb07587.x;
RA Isohashi F., Nakanishi Y., Sakamoto Y.;
RT "Factors affecting the cold inactivation of an acetyl-coenzyme-A hydrolase
RT purified from the supernatant fraction of rat liver.";
RL Eur. J. Biochem. 134:447-452(1983).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels. Preferentially hydrolyzes acetyl-CoA.
CC {ECO:0000269|PubMed:11322891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC Evidence={ECO:0000269|PubMed:11322891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC Evidence={ECO:0000305|PubMed:11322891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+);
CC Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000269|PubMed:11322891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000305|PubMed:11322891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate;
CC Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:11322891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000305|PubMed:11322891};
CC -!- ACTIVITY REGULATION: Allosterically regulated by ATP (activator) and
CC ADP (inhibitor) (PubMed:11322891). Cold labile, it dissociates into
CC inactive monomers at low temperature (PubMed:6136404).
CC {ECO:0000269|PubMed:11322891, ECO:0000269|PubMed:6136404}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=153 uM for acetyl-CoA {ECO:0000269|PubMed:11322891};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:11322891}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:6136404}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11322891}.
CC -!- INDUCTION: By 2-(p-chlorophenoxy)isobutyric acid (CPIB).
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DR EMBL; AB040609; BAB39852.1; -; mRNA.
DR RefSeq; NP_570103.1; NM_130747.1.
DR AlphaFoldDB; Q99NB7; -.
DR SMR; Q99NB7; -.
DR STRING; 10116.ENSRNOP00000021675; -.
DR PaxDb; Q99NB7; -.
DR GeneID; 170570; -.
DR KEGG; rno:170570; -.
DR UCSC; RGD:619752; rat.
DR CTD; 134526; -.
DR RGD; 619752; Acot12.
DR eggNOG; KOG2763; Eukaryota.
DR InParanoid; Q99NB7; -.
DR OrthoDB; 776852at2759; -.
DR PhylomeDB; Q99NB7; -.
DR BRENDA; 3.1.2.1; 5301.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SABIO-RK; Q99NB7; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q99NB7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IDA:HGNC-UCL.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:BHF-UCL.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 1.
DR Pfam; PF03061; 4HBT; 2.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Cytoplasm; Direct protein sequencing;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Reference proteome;
KW Repeat; Serine esterase.
FT CHAIN 1..556
FT /note="Acetyl-coenzyme A thioesterase"
FT /id="PRO_0000053811"
FT DOMAIN 6..118
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 180..295
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 341..550
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT BINDING 54..56
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 83..85
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT MOD_RES 97
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT MOD_RES 160
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT MOD_RES 229
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
SQ SEQUENCE 556 AA; 62018 MW; 81E592F066AB0C9E CRC64;
MEPTVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI SCVTASMDDI
LFEDTARIGQ IVTIRAKVTR AFSTSMEISI KVRVQDKFTG IQKLLCVAFS TFVVKPLGKE
KVHLKPVLLQ TEQEQVEHRL ASERRKVRLQ HENTFSNIMK ESNWLRDPVC NEEEGTATTM
ATSVQSIELV LPPHANHHGN TFGGQIMAWM ETVATISASR LCHGHPFLKS VDMFKFRGPS
TVGDRLVFNA IVNNTFQNSV EVGVRVEAFD CREWAEGQGR HINSAFLIYN AVDDQEELIT
FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL GTQWDISKKG SISNTNVEAL
KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKQVGSP ARVAYHLLSD FTKRPLWDPH
YISCEVIDQV SEDDQIYYIT CSVVNGDKPK DFVVLVSQRK PLKDDNTYIV ALMSVVLPSV
PPSPQYIRSQ VICAGFLIQP VDSSSCTVAY LNQMSDSILP YFAGNIGGWS KSIEEAAASC
IKFIENATHD GLKSVL
