ID ACO13_HUMAN Reviewed; 140 AA. AC Q9NPJ3; F5H2L4; O95549; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 184. DE RecName: Full=Acyl-coenzyme A thioesterase 13 {ECO:0000303|PubMed:19170545}; DE Short=Acyl-CoA thioesterase 13 {ECO:0000303|PubMed:19170545}; DE EC=3.1.2.- {ECO:0000269|PubMed:19170545}; DE AltName: Full=Hotdog-fold thioesterase superfamily member 2 {ECO:0000303|PubMed:19170545}; DE AltName: Full=Palmitoyl-CoA hydrolase {ECO:0000303|PubMed:19170545}; DE EC=3.1.2.2 {ECO:0000269|PubMed:19170545}; DE AltName: Full=Thioesterase superfamily member 2 {ECO:0000303|PubMed:16934754}; DE Short=THEM2 {ECO:0000303|PubMed:16934754}; DE Contains: DE RecName: Full=Acyl-coenzyme A thioesterase 13, N-terminally processed; GN Name=ACOT13 {ECO:0000312|HGNC:HGNC:20999}; Synonyms=THEM2; GN ORFNames=HT012, PNAS-27; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adrenal gland, and Hypothalamus; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Promyelocytic leukemia; RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., RA Yang H., Zhao Z.-L.; RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related RT genes."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Teratocarcinoma; 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 GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; 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 ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP 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 [12] {ECO:0007744|PDB:2F0X} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS RP SPECTROMETRY, MUTAGENESIS OF ASP-65, AND SUBUNIT. RX PubMed=16934754; DOI=10.1016/j.bbrc.2006.08.025; RA Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D., Gong W.; RT "Crystal structure of human thioesterase superfamily member 2."; RL Biochem. Biophys. Res. Commun. 349:172-177(2006). RN [13] {ECO:0007744|PDB:3F5O} RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; RP ASP-65 AND SER-83, SUBUNIT, AND CATALYTIC ACTIVITY. RX PubMed=19170545; DOI=10.1021/bi801879z; RA Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.; RT "The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate RT recognition and catalysis illuminated by a structure and function based RT analysis."; RL Biochemistry 48:1293-1304(2009). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RG Structural genomics consortium (SGC); RT "The crystal structure of human thioesterase superfamily member 2."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids CC and coenzyme A (CoASH), regulating their respective intracellular CC levels (PubMed:16934754, PubMed:19170545). Has acyl-CoA thioesterase CC activity towards medium (C12) and long-chain (C18) fatty acyl-CoA CC substrates (By similarity) (PubMed:16934754, PubMed:19170545). Can also CC hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA CC (in vitro) (By similarity) (PubMed:16934754, PubMed:19170545). May play CC a role in controlling adaptive thermogenesis (By similarity). CC {ECO:0000250|UniProtKB:Q9CQR4, ECO:0000269|PubMed:16934754, CC ECO:0000269|PubMed:19170545}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); CC Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; CC Evidence={ECO:0000269|PubMed:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; CC Evidence={ECO:0000303|PubMed:19170545}; 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:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; CC Evidence={ECO:0000303|PubMed:19170545}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)- CC eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; CC Evidence={ECO:0000269|PubMed:19170545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; CC Evidence={ECO:0000303|PubMed:19170545}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.9 uM for n-decanoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=26 uM for n-octanoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=70 uM for n-hexanoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=600 uM for n-butyryl-CoA {ECO:0000269|PubMed:19170545}; CC KM=220 uM for 2-butenoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=120 uM for beta-methylcrotonyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=180 uM for crotonyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=250 uM for tiglyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=190 uM for n-propionyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=290 uM for acetyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=9.9 uM for lauroyl-CoA/dodecanoyl-CoA CC {ECO:0000269|PubMed:19170545}; CC KM=5 uM for myristoyl-CoA/tetradecanoyl-CoA (at 25 degrees Celsius) CC {ECO:0000269|PubMed:19170545}; CC KM=9 uM for myristoyl-CoA/tetradecanoyl-CoA (at 37 degrees Celsius) CC {ECO:0000269|PubMed:19170545}; CC KM=16 uM for n-palmitoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=9 uM for palmitoleoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=20 uM for stearoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=9 uM for oleoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=310 uM for linoleoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=20 uM for arachidonoyl-CoA/(5Z,8Z,11Z,14Z)-eicosatetraenoate CC {ECO:0000269|PubMed:19170545}; CC KM=41 uM for 3-hydroxyphenylacetyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=10 uM for 3,4-dihydroxyphenylacetyl-CoA CC {ECO:0000269|PubMed:19170545}; CC KM=25 uM for 3,5-dihydroxyphenylacetyl-CoA CC {ECO:0000269|PubMed:19170545}; CC KM=49 uM for 4-hydroxyphenylacetyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=240 uM for phenylacetyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=32 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=13 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=110 uM for beta-hydroxybutyryl-CoA {ECO:0000269|PubMed:19170545}; CC KM=670 uM for glutaryl-CoA {ECO:0000269|PubMed:19170545}; CC KM=2900 uM for 3-hydroxy-3-methylglutaryl-CoA CC {ECO:0000269|PubMed:19170545}; CC KM=280 uM for malonyl-CoA {ECO:0000269|PubMed:19170545}; CC KM=210 uM for methylmalonyl-CoA {ECO:0000269|PubMed:19170545}; CC Note=kcat is 0.016 sec(-1) for n-decanoyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.0047 sec(-1) for n-octanoyl-CoA CC hydrolase activity (PubMed:19170545). kcat is 0.022 sec(-1) for CC n-hexanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.047 CC sec(-1) for n-butyryl-CoA hydrolase activity (PubMed:19170545). kcat CC is 0.014 sec(-1) for 2-butenoyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.023 sec(-1) for beta-methylcrotonyl-CoA CC hydrolase activity (PubMed:19170545). kcat is 0.0076 sec(-1) for CC crotonyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.02 CC sec(-1) for tiglyl-CoA hydrolase activity (PubMed:19170545). kcat is CC 0.036 sec(-1) for n-propionyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.054 sec(-1) for acetyl-CoA hydrolase CC activity (PubMed:19170545). kcat is 0.019 sec(-1) for lauroyl-CoA CC hydrolase activity (PubMed:19170545). kcat is 0.02 sec(-1) for CC myristoyl-CoA (at 25 degrees Celsius) hydrolase activity CC (PubMed:19170545). kcat is 0.07 sec(-1) for myristoyl-CoA (at 37 CC degrees Celsius) hydrolase activity (PubMed:19170545). kcat is 0.0044 CC sec(-1) for n-palmitoyl-CoA hydrolase activity (PubMed:19170545). CC kcat is 0.017 sec(-1) for palmitoleoyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.011 sec(-1) for stearoyl-CoA hydrolase CC activity (PubMed:19170545). kcat is 0.011 sec(-1) for oleoyl-CoA CC hydrolase activity (PubMed:19170545). kcat is 0.017 sec(-1) for CC linoleoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.022 CC sec(-1) for arachidonoyl-CoA hydrolase activity (PubMed:19170545). CC kcat is 1.4 sec(-1) for 3-hydroxyphenylacetyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.19 sec(-1) for CC 3,4-dihydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). CC kcat is 0.19 sec(-1) for 3,5-dihydroxyphenylacetyl-CoA hydrolase CC activity (PubMed:19170545). kcat is 0.14 sec(-1) for CC 4-hydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat CC is 0.084 sec(-1) for phenylacetyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.011 sec(-1) for 3-hydroxybenzoyl-CoA CC hydrolase activity (PubMed:19170545). kcat is 0.032 sec(-1) for CC 4-chlorobenzoyl-CoA hydrolase activity (PubMed:19170545). kcat is CC 0.18 sec(-1) for beta-hydroxybutyryl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.05 sec(-1) for glutaryl-CoA hydrolase CC activity (PubMed:19170545). kcat is 0.079 sec(-1) for CC 3-hydroxy-3-methylglutaryl-CoA hydrolase activity (PubMed:19170545). CC kcat is 0.066 sec(-1) for malonyl-CoA hydrolase activity CC (PubMed:19170545). kcat is 0.083 sec(-1) for methylmalonyl-CoA CC hydrolase activity (PubMed:19170545). {ECO:0000269|PubMed:19170545}; CC -!- SUBUNIT: Homotetramer (PubMed:16934754, PubMed:19170545). Interacts CC with PCTP (By similarity). {ECO:0000250|UniProtKB:Q9CQR4, CC ECO:0000269|PubMed:16934754, ECO:0000269|PubMed:19170545}. CC -!- INTERACTION: CC Q9NPJ3; Q92993: KAT5; NbExp=3; IntAct=EBI-1045357, EBI-399080; CC Q9NPJ3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1045357, EBI-11742507; CC Q9NPJ3; Q969H8: MYDGF; NbExp=3; IntAct=EBI-1045357, EBI-718622; CC Q9NPJ3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1045357, EBI-741158; CC Q9NPJ3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1045357, EBI-9090795; CC Q9NPJ3; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1045357, EBI-742688; CC Q9NPJ3; P61981: YWHAG; NbExp=3; IntAct=EBI-1045357, EBI-359832; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9CQR4}. Mitochondrion CC {ECO:0000250|UniProtKB:Q9CQR4}. Nucleus {ECO:0000250|UniProtKB:Q9CQR4}. CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9CQR4}. CC Note=During interphase, found both in the nucleus and in the cytoplasm. CC At mitosis, localizes to the spindle. Colocalizes with tubulin. CC {ECO:0000250|UniProtKB:Q9CQR4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NPJ3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NPJ3-2; Sequence=VSP_046101; CC -!- SIMILARITY: Belongs to the thioesterase PaaI family. {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; AF155649; AAF67006.1; -; mRNA. DR EMBL; AF220186; AAF67651.1; -; mRNA. DR EMBL; AF274952; AAK07529.1; -; mRNA. DR EMBL; AK000508; BAA91215.1; -; mRNA. DR EMBL; AK309738; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL031775; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000894; AAH00894.1; -; mRNA. DR CCDS; CCDS4558.1; -. [Q9NPJ3-1] DR CCDS; CCDS54972.1; -. [Q9NPJ3-2] DR RefSeq; NP_001153566.1; NM_001160094.1. [Q9NPJ3-2] DR RefSeq; NP_060943.1; NM_018473.3. [Q9NPJ3-1] DR PDB; 2F0X; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-140. DR PDB; 2H4U; X-ray; 2.20 A; A/B/C/D=19-140. DR PDB; 3F5O; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-140. DR PDBsum; 2F0X; -. DR PDBsum; 2H4U; -. DR PDBsum; 3F5O; -. DR AlphaFoldDB; Q9NPJ3; -. DR SMR; Q9NPJ3; -. DR BioGRID; 120958; 45. DR IntAct; Q9NPJ3; 12. DR STRING; 9606.ENSP00000230048; -. DR ChEMBL; CHEMBL4295957; -. DR DrugBank; DB08688; 2-Undecanone. DR iPTMnet; Q9NPJ3; -. DR PhosphoSitePlus; Q9NPJ3; -. DR SwissPalm; Q9NPJ3; -. DR BioMuta; ACOT13; -. DR EPD; Q9NPJ3; -. DR jPOST; Q9NPJ3; -. DR MassIVE; Q9NPJ3; -. DR MaxQB; Q9NPJ3; -. DR PaxDb; 9606-ENSP00000230048; -. DR PeptideAtlas; Q9NPJ3; -. DR ProteomicsDB; 26006; -. DR ProteomicsDB; 82025; -. [Q9NPJ3-1] DR Pumba; Q9NPJ3; -. DR TopDownProteomics; Q9NPJ3-1; -. [Q9NPJ3-1] DR Antibodypedia; 10661; 225 antibodies from 33 providers. DR DNASU; 55856; -. DR Ensembl; ENST00000230048.5; ENSP00000230048.3; ENSG00000112304.11. [Q9NPJ3-1] DR Ensembl; ENST00000537591.5; ENSP00000445552.1; ENSG00000112304.11. [Q9NPJ3-2] DR GeneID; 55856; -. DR KEGG; hsa:55856; -. DR MANE-Select; ENST00000230048.5; ENSP00000230048.3; NM_018473.4; NP_060943.1. DR UCSC; uc003nek.4; human. [Q9NPJ3-1] DR AGR; HGNC:20999; -. DR CTD; 55856; -. DR DisGeNET; 55856; -. DR GeneCards; ACOT13; -. DR HGNC; HGNC:20999; ACOT13. DR HPA; ENSG00000112304; Tissue enhanced (liver). DR MIM; 615652; gene. DR neXtProt; NX_Q9NPJ3; -. DR OpenTargets; ENSG00000112304; -. DR PharmGKB; PA165617655; -. DR VEuPathDB; HostDB:ENSG00000112304; -. DR eggNOG; KOG3328; Eukaryota. DR GeneTree; ENSGT00390000013934; -. DR HOGENOM; CLU_089876_12_2_1; -. DR InParanoid; Q9NPJ3; -. DR OMA; TGRHTKY; -. DR OrthoDB; 316530at2759; -. DR PhylomeDB; Q9NPJ3; -. DR TreeFam; TF315062; -. DR BRENDA; 3.1.2.20; 2681. DR PathwayCommons; Q9NPJ3; -. DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation. DR SABIO-RK; Q9NPJ3; -. DR SignaLink; Q9NPJ3; -. DR BioGRID-ORCS; 55856; 15 hits in 1151 CRISPR screens. DR ChiTaRS; ACOT13; human. DR EvolutionaryTrace; Q9NPJ3; -. DR GenomeRNAi; 55856; -. DR Pharos; Q9NPJ3; Tbio. DR PRO; PR:Q9NPJ3; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9NPJ3; Protein. DR Bgee; ENSG00000112304; Expressed in right lobe of liver and 201 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; 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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB. DR CDD; cd03443; PaaI_thioesterase; 1. DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1. DR InterPro; IPR039298; ACOT13. DR InterPro; IPR029069; HotDog_dom_sf. DR InterPro; IPR003736; PAAI_dom. DR InterPro; IPR006683; Thioestr_dom. DR NCBIfam; TIGR00369; unchar_dom_1; 1. DR PANTHER; PTHR21660:SF1; ACYL-COENZYME A THIOESTERASE 13; 1. DR PANTHER; PTHR21660; THIOESTERASE SUPERFAMILY MEMBER-RELATED; 1. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1. DR Genevisible; Q9NPJ3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; KW Hydrolase; Lipid metabolism; Metal-binding; Mitochondrion; Nucleus; KW Reference proteome. FT CHAIN 1..140 FT /note="Acyl-coenzyme A thioesterase 13" FT /id="PRO_0000156697" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..140 FT /note="Acyl-coenzyme A thioesterase 13, N-terminally FT processed" FT /id="PRO_0000424501" FT BINDING 46 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT BINDING 50 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT BINDING 83 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT BINDING 90..95 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT BINDING 108..113 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT BINDING 137 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:19170545, FT ECO:0007744|PDB:3F5O" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 2 FT /note="N-acetylthreonine; in Acyl-coenzyme A thioesterase FT 13, N-terminally processed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT MOD_RES 27 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQR4" FT MOD_RES 37 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQR4" FT MOD_RES 43 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQR4" FT MOD_RES 108 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQR4" FT MOD_RES 127 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQR4" FT VAR_SEQ 1..26 FT /note="MTSMTQSLREVIKAMTKARNFERVLG -> MVR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046101" FT MUTAGEN 50 FT /note="N->A: Reduced acyl-CoA hydrolase activity." FT /evidence="ECO:0000269|PubMed:19170545" FT MUTAGEN 56 FT /note="H->A: Decreases affinity for substrate." FT /evidence="ECO:0000269|PubMed:19170545" FT MUTAGEN 65 FT /note="D->A: Loss of acyl-CoA hydrolase activity." FT /evidence="ECO:0000269|PubMed:16934754, FT ECO:0000269|PubMed:19170545" FT MUTAGEN 65 FT /note="D->E,N: Reduced acyl-CoA hydrolase activity." FT /evidence="ECO:0000269|PubMed:16934754, FT ECO:0000269|PubMed:19170545" FT MUTAGEN 83 FT /note="S->A: Reduced acyl-CoA hydrolase activity." FT /evidence="ECO:0000269|PubMed:19170545" FT HELIX 3..15 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:3F5O" FT HELIX 21..25 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:3F5O" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:3F5O" FT HELIX 57..73 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 82..90 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 99..109 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 111..122 FT /evidence="ECO:0007829|PDB:3F5O" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:3F5O" FT STRAND 128..137 FT /evidence="ECO:0007829|PDB:3F5O" SQ SEQUENCE 140 AA; 14960 MW; 084E36EFEE715A18 CRC64; MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN //