ACOT2_HUMAN
ID ACOT2_HUMAN Reviewed; 483 AA.
AC P49753; Q3I5F8; Q53EK4; Q9NUX4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 6.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Acyl-coenzyme A thioesterase 2, mitochondrial;
DE Short=Acyl-CoA thioesterase 2;
DE EC=3.1.2.2 {ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:16940157};
DE AltName: Full=Acyl-coenzyme A thioester hydrolase 2a;
DE AltName: Full=CTE-Ia;
DE AltName: Full=Long-chain acyl-CoA thioesterase 2;
DE AltName: Full=ZAP128;
DE Flags: Precursor;
GN Name=ACOT2; Synonyms=PTE2, PTE2A;
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M.,
RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F.,
RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L.,
RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W.,
RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D.,
RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND CAUTION.
RX PubMed=16940157; DOI=10.1096/fj.06-6042com;
RA Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.;
RT "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters
RT shows that convergent, functional evolution results in a reduced number of
RT human peroxisomal ACOTs.";
RL FASEB J. 20:1855-1864(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-475.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-475.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-475.
RC TISSUE=Lung, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-483 (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, CAUTION, AND VARIANT ARG-475.
RX PubMed=10944470; DOI=10.1006/bbrc.2000.3285;
RA Jones J.M., Gould S.J.;
RT "Identification of PTE2, a human peroxisomal long-chain acyl-CoA
RT thioesterase.";
RL Biochem. Biophys. Res. Commun. 275:233-240(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 46-483, AND ACTIVE SITE.
RX PubMed=19497300; DOI=10.1016/j.bbrc.2009.05.122;
RA Mandel C.R., Tweel B., Tong L.;
RT "Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2).";
RL Biochem. Biophys. Res. Commun. 385:630-633(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:16940157, PubMed:10944470). Displays higher activity
CC toward long chain acyl CoAs (C14-C20) (PubMed:16940157,
CC PubMed:10944470). The enzyme is involved in enhancing the hepatic fatty
CC acid oxidation in mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:10944470,
CC ECO:0000269|PubMed:16940157}.
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:10944470, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:16940157};
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:10944470, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:16940157};
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:10944470, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:16940157};
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:10944470, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000305|PubMed:16940157};
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:10944470, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:16940157};
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:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:16940157};
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:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000305|PubMed:16940157};
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:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000305|PubMed:16940157};
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:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724;
CC Evidence={ECO:0000305|PubMed:16940157};
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=40.3 uM for C10-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=8.9 uM for C12-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=1.6 uM for C14-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=2.0 uM for C16-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=2.8 uM for C18-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=4.8 uM for C20-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=4.5 uM for C16:1-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=6.1 uM for C18:1-acyl-CoA {ECO:0000269|PubMed:16940157};
CC KM=4.3 uM for C18:1-trans-acyl-CoA {ECO:0000269|PubMed:16940157};
CC Vmax=212 nmol/min/mg enzyme with C10-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=681 nmol/min/mg enzyme with C12-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=766 nmol/min/mg enzyme with C14-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=656 nmol/min/mg enzyme with C16-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=488 nmol/min/mg enzyme with C18-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=408 nmol/min/mg enzyme with C20-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=661 nmol/min/mg enzyme with C16:1-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=304 nmol/min/mg enzyme with C18:1-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC Vmax=418 nmol/min/mg enzyme with C18:1-trans-acyl-CoA as substrate
CC {ECO:0000269|PubMed:16940157};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:16940157}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9QYR9}.
CC -!- INTERACTION:
CC P49753; Q9NZ94-2: NLGN3; NbExp=2; IntAct=EBI-1052865, EBI-16423037;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16940157}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49753-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49753-2; Sequence=VSP_012225, VSP_012226;
CC -!- TISSUE SPECIFICITY: Strongest expression in heart, liver, muscle and
CC kidney. Weak in placenta and pancreas. {ECO:0000269|PubMed:16940157}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:10944470) thought to be peroxisomal but
CC was later shown (PubMed:16940157) to be mitochondrial.
CC {ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:16940157}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42007.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L40401; AAC42007.1; ALT_FRAME; mRNA.
DR EMBL; DQ082755; AAZ31237.1; -; mRNA.
DR EMBL; AK001939; BAA91989.1; -; mRNA.
DR EMBL; AK223635; BAD97355.1; -; mRNA.
DR EMBL; BC004436; AAH04436.2; -; mRNA.
DR EMBL; BC006335; AAH06335.1; -; mRNA.
DR EMBL; BC006500; AAH06500.4; -; mRNA.
DR EMBL; AY005822; AAF97985.1; -; mRNA.
DR CCDS; CCDS9816.1; -. [P49753-1]
DR PIR; JC7367; JC7367.
DR RefSeq; NP_006812.3; NM_006821.5. [P49753-1]
DR PDB; 3HLK; X-ray; 2.10 A; A/B=46-483.
DR PDBsum; 3HLK; -.
DR AlphaFoldDB; P49753; -.
DR SMR; P49753; -.
DR BioGRID; 116164; 119.
DR IntAct; P49753; 15.
DR MINT; P49753; -.
DR STRING; 9606.ENSP00000238651; -.
DR ChEMBL; CHEMBL2189135; -.
DR SwissLipids; SLP:000000590; -.
DR ESTHER; human-ACOT2; Acyl-CoA_Thioesterase.
DR MEROPS; S09.942; -.
DR CarbonylDB; P49753; -.
DR GlyGen; P49753; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49753; -.
DR PhosphoSitePlus; P49753; -.
DR SwissPalm; P49753; -.
DR BioMuta; ACOT2; -.
DR DMDM; 269849771; -.
DR EPD; P49753; -.
DR jPOST; P49753; -.
DR MassIVE; P49753; -.
DR MaxQB; P49753; -.
DR PaxDb; P49753; -.
DR PeptideAtlas; P49753; -.
DR PRIDE; P49753; -.
DR ProteomicsDB; 56066; -. [P49753-1]
DR ProteomicsDB; 56067; -. [P49753-2]
DR Antibodypedia; 25399; 149 antibodies from 27 providers.
DR DNASU; 10965; -.
DR Ensembl; ENST00000238651.10; ENSP00000238651.5; ENSG00000119673.16. [P49753-1]
DR GeneID; 10965; -.
DR KEGG; hsa:10965; -.
DR MANE-Select; ENST00000238651.10; ENSP00000238651.5; NM_006821.6; NP_006812.3.
DR UCSC; uc001xon.6; human. [P49753-1]
DR CTD; 10965; -.
DR DisGeNET; 10965; -.
DR GeneCards; ACOT2; -.
DR HGNC; HGNC:18431; ACOT2.
DR HPA; ENSG00000119673; Tissue enhanced (liver).
DR MIM; 609972; gene.
DR neXtProt; NX_P49753; -.
DR OpenTargets; ENSG00000119673; -.
DR PharmGKB; PA142672653; -.
DR VEuPathDB; HostDB:ENSG00000119673; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR InParanoid; P49753; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; P49753; -.
DR TreeFam; TF314911; -.
DR BioCyc; MetaCyc:HS04318-MON; -.
DR BRENDA; 3.1.2.2; 2681.
DR PathwayCommons; P49753; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; P49753; -.
DR SignaLink; P49753; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 10965; 18 hits in 1067 CRISPR screens.
DR ChiTaRS; ACOT2; human.
DR EvolutionaryTrace; P49753; -.
DR GeneWiki; ACOT2; -.
DR GenomeRNAi; 10965; -.
DR Pharos; P49753; Tbio.
DR PRO; PR:P49753; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49753; protein.
DR Bgee; ENSG00000119673; Expressed in apex of heart and 99 other tissues.
DR ExpressionAtlas; P49753; baseline and differential.
DR Genevisible; P49753; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:HGNC-UCL.
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; IDA:HGNC-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:HGNC-UCL.
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 3D-structure; Acetylation; Alternative splicing; Fatty acid metabolism;
KW Hydrolase; Lipid metabolism; Mitochondrion; Reference proteome;
KW Serine esterase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..483
FT /note="Acyl-coenzyme A thioesterase 2, mitochondrial"
FT /id="PRO_0000202147"
FT MOTIF 481..483
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 294
FT /note="Charge relay system"
FT /evidence="ECO:0000303|PubMed:19497300"
FT ACT_SITE 388
FT /note="Charge relay system"
FT /evidence="ECO:0000303|PubMed:19497300"
FT ACT_SITE 422
FT /note="Charge relay system"
FT /evidence="ECO:0000303|PubMed:19497300"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR9"
FT MOD_RES 470
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR9"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7596406"
FT /id="VSP_012225"
FT VAR_SEQ 53..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7596406"
FT /id="VSP_012226"
FT VARIANT 16
FT /note="R -> S (in dbSNP:rs11545741)"
FT /id="VAR_057271"
FT VARIANT 475
FT /note="H -> R (in dbSNP:rs7494)"
FT /evidence="ECO:0000269|PubMed:10944470,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_016136"
FT CONFLICT 167
FT /note="E -> V (in Ref. 2; AAZ31237 and 3; BAA91989)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="H -> R (in Ref. 2; AAZ31237, 3; BAA91989, 4;
FT BAD97355, 5; AAH04436/AAH06335/AAH06500 and 6; AAF97985)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="A -> V (in Ref. 5; AAH06335)"
FT /evidence="ECO:0000305"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:3HLK"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 181..192
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:3HLK"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 393..406
FT /evidence="ECO:0007829|PDB:3HLK"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:3HLK"
FT HELIX 450..471
FT /evidence="ECO:0007829|PDB:3HLK"
SQ SEQUENCE 483 AA; 53218 MW; FAEDD42BBBD935E4 CRC64;
MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL RQVGQIIRVP
ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL RDEKGALFQA HARYRADTLG
ELDLERAPAL GGSFAGLEPM GLLWALEPEK PLVRLVKRDV RTPLAVELEV LDGHDPDPGR
LLCQTRHERY FLPPGVRREP VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL
AGKGFAVMAL AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC
LSMASFLKGI TAAVVINGSV ANVGGTLHYK GETLPPVGVN RNRIKVTKDG YADIVDVLNS
PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA CKRLQAHGRR KPQIICYPET
GHYIEPPYFP LCRASLHALV GSPIIWGGEP RAHAMAQVDA WKQLQTFFHK HLGGHEGTIP
SKV
