THIM_HUMAN
ID THIM_HUMAN Reviewed; 397 AA.
AC P42765; Q9BUT6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=3-ketoacyl-CoA thiolase, mitochondrial {ECO:0000305};
DE EC=2.3.1.16 {ECO:0000269|PubMed:25478839};
DE AltName: Full=Acetyl-CoA acetyltransferase {ECO:0000305};
DE EC=2.3.1.9 {ECO:0000269|PubMed:25478839};
DE AltName: Full=Acetyl-CoA acyltransferase;
DE AltName: Full=Acyl-CoA hydrolase, mitochondrial {ECO:0000305};
DE EC=3.1.2.- {ECO:0000269|PubMed:25478839};
DE EC=3.1.2.1 {ECO:0000269|PubMed:25478839};
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:P13437};
DE AltName: Full=Beta-ketothiolase;
DE AltName: Full=Mitochondrial 3-oxoacyl-CoA thiolase;
DE AltName: Full=T1;
GN Name=ACAA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8241273; DOI=10.1016/0167-4781(93)90160-f;
RA Abe H., Ohtake A., Yamamoto S., Satoh Y., Takayanagi M., Amaya Y.,
RA Takiguchi M., Sakuraba H., Suzuki Y., Mori M., Niimi H.;
RT "Cloning and sequence analysis of a full length cDNA encoding human
RT mitochondrial 3-oxoacyl-CoA thiolase.";
RL Biochim. Biophys. Acta 1216:304-306(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 15-25; 46-71 AND 341-360.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BNIP3.
RX PubMed=18371312; DOI=10.1016/j.bbagen.2008.02.007;
RA Cao W., Liu N., Tang S., Bao L., Shen L., Yuan H., Zhao X., Lu H.;
RT "Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic effects of
RT BNIP3 in two human cell lines.";
RL Biochim. Biophys. Acta 1780:873-880(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-121 AND TYR-127, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COENZYME A,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-92 AND CYS-382.
RX PubMed=25478839; DOI=10.1107/s1399004714023827;
RA Kiema T.R., Harijan R.K., Strozyk M., Fukao T., Alexson S.E.,
RA Wierenga R.K.;
RT "The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1):
RT insight into the reaction mechanism of its thiolase and thioesterase
RT activities.";
RL Acta Crystallogr. D 70:3212-3225(2014).
CC -!- FUNCTION: In the production of energy from fats, this is one of the
CC enzymes that catalyzes the last step of the mitochondrial beta-
CC oxidation pathway, an aerobic process breaking down fatty acids into
CC acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the
CC thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs
CC into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms
CC (Probable). Also catalyzes the condensation of two acetyl-CoA molecules
CC into acetoacetyl-CoA and could be involved in the production of ketone
CC bodies (Probable). Also displays hydrolase activity on various fatty
CC acyl-CoAs (PubMed:25478839). Thereby, could be responsible for the
CC production of acetate in a side reaction to beta-oxidation (Probable).
CC Abolishes BNIP3-mediated apoptosis and mitochondrial damage
CC (PubMed:18371312). {ECO:0000269|PubMed:18371312,
CC ECO:0000269|PubMed:25478839, ECO:0000305|PubMed:25478839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000269|PubMed:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21565;
CC Evidence={ECO:0000305|PubMed:25478839};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000305|PubMed:25478839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000269|PubMed:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037;
CC Evidence={ECO:0000305|PubMed:25478839};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC Evidence={ECO:0000305|PubMed:25478839};
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:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC Evidence={ECO:0000305|PubMed:25478839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate;
CC Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000269|PubMed:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104;
CC Evidence={ECO:0000305|PubMed:25478839};
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:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000305|PubMed:25478839};
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:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000305|PubMed:25478839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
CC Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000269|PubMed:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000305|PubMed:25478839};
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:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:25478839};
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:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:25478839};
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:25478839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:25478839};
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:0000250|UniProtKB:P13437};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:P13437};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.2 uM for acetoacetyl-CoA {ECO:0000269|PubMed:25478839};
CC KM=250 uM for acetyl-CoA {ECO:0000269|PubMed:25478839};
CC KM=35 uM for octanoyl-CoA {ECO:0000269|PubMed:25478839};
CC Note=kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-
CC oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the
CC synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1)
CC for octanoyl-CoA hydrolysis (PubMed:25478839).
CC {ECO:0000269|PubMed:25478839};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:25478839}.
CC -!- SUBUNIT: Homotetramer (PubMed:25478839). Interacts with BNIP3.
CC {ECO:0000269|PubMed:18371312, ECO:0000269|PubMed:25478839}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18371312}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D16294; BAA03800.1; -; mRNA.
DR EMBL; BC001918; AAH01918.1; -; mRNA.
DR CCDS; CCDS11939.1; -.
DR PIR; S43440; S43440.
DR RefSeq; NP_006102.2; NM_006111.2.
DR PDB; 4C2J; X-ray; 2.00 A; A/B/C/D=1-397.
DR PDB; 4C2K; X-ray; 2.00 A; A/B/C/D=1-397.
DR PDBsum; 4C2J; -.
DR PDBsum; 4C2K; -.
DR AlphaFoldDB; P42765; -.
DR SMR; P42765; -.
DR BioGRID; 115713; 169.
DR IntAct; P42765; 21.
DR MINT; P42765; -.
DR STRING; 9606.ENSP00000285093; -.
DR DrugBank; DB09069; Trimetazidine.
DR SwissLipids; SLP:000001273; -.
DR GlyGen; P42765; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P42765; -.
DR PhosphoSitePlus; P42765; -.
DR SwissPalm; P42765; -.
DR BioMuta; ACAA2; -.
DR DMDM; 57015371; -.
DR REPRODUCTION-2DPAGE; IPI00001539; -.
DR UCD-2DPAGE; P42765; -.
DR CPTAC; CPTAC-158; -.
DR CPTAC; CPTAC-159; -.
DR EPD; P42765; -.
DR jPOST; P42765; -.
DR MassIVE; P42765; -.
DR MaxQB; P42765; -.
DR PaxDb; P42765; -.
DR PeptideAtlas; P42765; -.
DR PRIDE; P42765; -.
DR ProteomicsDB; 55548; -.
DR TopDownProteomics; P42765; -.
DR Antibodypedia; 22617; 379 antibodies from 30 providers.
DR DNASU; 10449; -.
DR Ensembl; ENST00000285093.15; ENSP00000285093.8; ENSG00000167315.18.
DR GeneID; 10449; -.
DR KEGG; hsa:10449; -.
DR MANE-Select; ENST00000285093.15; ENSP00000285093.8; NM_006111.3; NP_006102.2.
DR UCSC; uc002ldw.5; human.
DR CTD; 10449; -.
DR DisGeNET; 10449; -.
DR GeneCards; ACAA2; -.
DR HGNC; HGNC:83; ACAA2.
DR HPA; ENSG00000167315; Tissue enhanced (liver).
DR MIM; 604770; gene.
DR neXtProt; NX_P42765; -.
DR OpenTargets; ENSG00000167315; -.
DR PharmGKB; PA24420; -.
DR VEuPathDB; HostDB:ENSG00000167315; -.
DR eggNOG; KOG1391; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR InParanoid; P42765; -.
DR OMA; GIWEINE; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; P42765; -.
DR TreeFam; TF105696; -.
DR BioCyc; MetaCyc:HS09539-MON; -.
DR BRENDA; 2.3.1.16; 2681.
DR PathwayCommons; P42765; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; P42765; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 10449; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; ACAA2; human.
DR GeneWiki; ACAA2; -.
DR GenomeRNAi; 10449; -.
DR Pharos; P42765; Tbio.
DR PRO; PR:P42765; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P42765; protein.
DR Bgee; ENSG00000167315; Expressed in right lobe of liver and 177 other tissues.
DR ExpressionAtlas; P42765; baseline and differential.
DR Genevisible; P42765; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IMP:UniProtKB.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:BHF-UCL.
DR GO; GO:0006695; P:cholesterol biosynthetic process; NAS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT CHAIN 1..397
FT /note="3-ketoacyl-CoA thiolase, mitochondrial"
FT /id="PRO_0000223299"
FT TRANSIT 1..16
FT /note="Mitochondrion; not cleaved"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:25478839"
FT ACT_SITE 382
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:25478839"
FT BINDING 224
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:25478839,
FT ECO:0007744|PDB:4C2J"
FT BINDING 227
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:25478839,
FT ECO:0007744|PDB:4C2J"
FT BINDING 251
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:25478839,
FT ECO:0007744|PDB:4C2J"
FT SITE 352
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000305|PubMed:25478839"
FT MOD_RES 25
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 25
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 45
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 137
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 137
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 143
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 171
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 171
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 209
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 209
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 211
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 212
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 214
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 234
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 234
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 240
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 270
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 305
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 305
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 312
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 312
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT VARIANT 217
FT /note="M -> V (in dbSNP:rs11549285)"
FT /id="VAR_052577"
FT MUTAGEN 92
FT /note="C->A: Decreased acyl-CoA hydrolase activity."
FT /evidence="ECO:0000269|PubMed:25478839"
FT MUTAGEN 92
FT /note="C->S: Decreased acyl-CoA hydrolase activity; when
FT associated with A-382."
FT /evidence="ECO:0000269|PubMed:25478839"
FT MUTAGEN 382
FT /note="C->S: Decreased acyl-CoA hydrolase activity; when
FT associated with S-92."
FT /evidence="ECO:0000269|PubMed:25478839"
FT CONFLICT 2
FT /note="A -> R (in Ref. 1; BAA03800)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> T (in Ref. 1; BAA03800)"
FT /evidence="ECO:0000305"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:4C2J"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:4C2J"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 176..196
FT /evidence="ECO:0007829|PDB:4C2J"
FT TURN 197..202
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4C2J"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:4C2J"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:4C2J"
FT HELIX 357..372
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:4C2J"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:4C2J"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:4C2J"
SQ SEQUENCE 397 AA; 41924 MW; 380CC8262ACF6D01 CRC64;
MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET VDSVIMGNVL
QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV NGCQEICVKE AEVVLCGGTE
SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV SLTDQHVQLP MAMTAENLAV KHKISREECD
KYALQSQQRW KAANDAGYFN DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK
KDGTVTAGNA SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI
SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL GHPLGGSGSR
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA
