ACO13_HUMAN
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 03-AUG-2022, entry version 175.
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 n-
CC 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 sec(-
CC 1) for tiglyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.036
CC sec(-1) for n-propionyl-CoA hydrolase activity (PubMed:19170545).
CC kcat is 0.054 sec(-1) for acetyl-CoA hydrolase activity
CC (PubMed:19170545). kcat is 0.019 sec(-1) for lauroyl-CoA hydrolase
CC activity (PubMed:19170545). kcat is 0.02 sec(-1) for myristoyl-CoA
CC (at 25 degrees Celsius) hydrolase activity (PubMed:19170545). kcat is
CC 0.07 sec(-1) for myristoyl-CoA (at 37 degrees Celsius) hydrolase
CC activity (PubMed:19170545). kcat is 0.0044 sec(-1) for n-palmitoyl-
CC CoA hydrolase activity (PubMed:19170545). kcat is 0.017 sec(-1) for
CC palmitoleoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.011
CC sec(-1) for stearoyl-CoA hydrolase activity (PubMed:19170545). kcat
CC is 0.011 sec(-1) for oleoyl-CoA hydrolase activity (PubMed:19170545).
CC kcat is 0.017 sec(-1) for linoleoyl-CoA hydrolase activity
CC (PubMed:19170545). kcat is 0.022 sec(-1) for arachidonoyl-CoA
CC hydrolase activity (PubMed:19170545). kcat is 1.4 sec(-1) for 3-
CC hydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat is
CC 0.19 sec(-1) for 3,4-dihydroxyphenylacetyl-CoA hydrolase activity
CC (PubMed:19170545). kcat is 0.19 sec(-1) for 3,5-
CC dihydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat
CC is 0.14 sec(-1) for 4-hydroxyphenylacetyl-CoA hydrolase activity
CC (PubMed:19170545). kcat is 0.084 sec(-1) for phenylacetyl-CoA
CC hydrolase activity (PubMed:19170545). kcat is 0.011 sec(-1) for 3-
CC hydroxybenzoyl-CoA hydrolase activity (PubMed:19170545). kcat is
CC 0.032 sec(-1) for 4-chlorobenzoyl-CoA hydrolase activity
CC (PubMed:19170545). kcat is 0.18 sec(-1) for beta-hydroxybutyryl-CoA
CC hydrolase activity (PubMed:19170545). kcat is 0.05 sec(-1) for
CC glutaryl-CoA hydrolase activity (PubMed:19170545). kcat is 0.079
CC sec(-1) for 3-hydroxy-3-methylglutaryl-CoA hydrolase activity
CC (PubMed:19170545). kcat is 0.066 sec(-1) for malonyl-CoA hydrolase
CC activity (PubMed:19170545). kcat is 0.083 sec(-1) for methylmalonyl-
CC CoA hydrolase activity (PubMed:19170545).
CC {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}.
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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; 39.
DR IntAct; Q9NPJ3; 12.
DR STRING; 9606.ENSP00000230048; -.
DR ChEMBL; CHEMBL4295957; -.
DR DrugBank; DB08688; 2-Undecanone.
DR iPTMnet; Q9NPJ3; -.
DR PhosphoSitePlus; Q9NPJ3; -.
DR BioMuta; ACOT13; -.
DR EPD; Q9NPJ3; -.
DR jPOST; Q9NPJ3; -.
DR MassIVE; Q9NPJ3; -.
DR MaxQB; Q9NPJ3; -.
DR PaxDb; Q9NPJ3; -.
DR PeptideAtlas; Q9NPJ3; -.
DR PRIDE; Q9NPJ3; -.
DR ProteomicsDB; 26006; -.
DR ProteomicsDB; 82025; -. [Q9NPJ3-1]
DR TopDownProteomics; Q9NPJ3-1; -. [Q9NPJ3-1]
DR Antibodypedia; 10661; 215 antibodies from 34 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 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; EHLNQRG; -.
DR OrthoDB; 1607235at2759; -.
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 1081 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 199 other tissues.
DR Genevisible; Q9NPJ3; HS.
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 InterPro; IPR039298; ACOT13.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR21660; PTHR21660; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR00369; unchar_dom_1; 1.
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
