ACO13_MOUSE
ID ACO13_MOUSE Reviewed; 140 AA.
AC Q9CQR4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Acyl-coenzyme A thioesterase 13 {ECO:0000303|PubMed:19405909};
DE Short=Acyl-CoA thioesterase 13 {ECO:0000303|PubMed:19405909};
DE EC=3.1.2.- {ECO:0000269|PubMed:19405909};
DE AltName: Full=Hotdog-fold thioesterase superfamily member 2 {ECO:0000303|PubMed:19405909};
DE AltName: Full=Palmitoyl-CoA hydrolase {ECO:0000303|PubMed:19405909};
DE EC=3.1.2.2 {ECO:0000269|PubMed:19405909};
DE AltName: Full=Thioesterase superfamily member 2 {ECO:0000250|UniProtKB:Q9NPJ3};
DE Short=THEM2 {ECO:0000250|UniProtKB:Q9NPJ3};
GN Name=Acot13 {ECO:0000312|MGI:MGI:1914084}; Synonyms=Them2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17045243; DOI=10.1016/j.bbrc.2006.09.105;
RA Cheng Z., Bao S., Shan X., Xu H., Gong W.;
RT "Human thioesterase superfamily member 2 (hTHEM2) is co-localized with
RT beta-tubulin onto the microtubule.";
RL Biochem. Biophys. Res. Commun. 350:850-853(2006).
RN [4]
RP INTERACTION WITH PCTP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17704541; DOI=10.1074/jbc.m703745200;
RA Kanno K., Wu M.K., Agate D.S., Fanelli B.J., Wagle N., Scapa E.F.,
RA Ukomadu C., Cohen D.E.;
RT "Interacting proteins dictate function of the minimal START domain
RT phosphatidylcholine transfer protein/StarD2.";
RL J. Biol. Chem. 282:30728-30736(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19405909; DOI=10.1042/bj20090039;
RA Wei J., Kang H.W., Cohen D.E.;
RT "Thioesterase superfamily member 2 (Them2)/acyl-CoA thioesterase 13
RT (Acot13): A homotetrameric hotdog fold thioesterase with selectivity for
RT long chain fatty acyl-CoAs.";
RL Biochem. J. 421:311-322(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22345407; DOI=10.1096/fj.11-202853;
RA Kang H.W., Niepel M.W., Han S., Kawano Y., Cohen D.E.;
RT "Thioesterase superfamily member 2/acyl-CoA thioesterase 13 (Them2/Acot13)
RT regulates hepatic lipid and glucose metabolism.";
RL FASEB J. 26:2209-2221(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24072708; DOI=10.1074/jbc.m113.481408;
RA Kang H.W., Ozdemir C., Kawano Y., LeClair K.B., Vernochet C., Kahn C.R.,
RA Hagen S.J., Cohen D.E.;
RT "Thioesterase superfamily member 2/Acyl-CoA thioesterase 13 (Them2/Acot13)
RT regulates adaptive thermogenesis in mice.";
RL J. Biol. Chem. 288:33376-33386(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-37; LYS-43; LYS-108 AND
RP LYS-127, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [10] {ECO:0007744|PDB:2CY9}
RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS), AND APOPROTEIN.
RA Hosaka T., Murayama K., Kishishita S., Shirouzu M., Yokoyama S.;
RT "Crystal structure of thioesterase superfamily member2 from Mus musculus.";
RL Submitted (JUL-2005) 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:19405909). Has acyl-CoA thioesterase activity towards
CC medium (C12) and long-chain (C18) fatty acyl-CoA substrates
CC (PubMed:19405909). Can also hydrolyze 3-hydroxyphenylacetyl-CoA and
CC 3,4-dihydroxyphenylacetyl-CoA (in vitro) (By similarity). May play a
CC role in controlling adaptive thermogenesis (PubMed:24072708).
CC {ECO:0000250|UniProtKB:Q9NPJ3, ECO:0000269|PubMed:19405909,
CC ECO:0000269|PubMed:24072708}.
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:19405909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782;
CC Evidence={ECO:0000303|PubMed:19405909};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:19405909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000303|PubMed:19405909};
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:19405909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000303|PubMed:19405909};
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:19405909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000303|PubMed:19405909};
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:19405909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000303|PubMed:19405909};
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:19405909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000303|PubMed:19405909};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=138 uM for hexanoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=47 uM for decanoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=27 uM for lauroyl-CoA/dodecanoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=15 uM for myristoyl-CoA/tetradecanoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=7 uM for myristoyl-CoA/tetradecanoyl-CoA (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=21 uM for myristoyl-CoA/tetradecanoyl-CoA (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=10 uM for palmitoyl-CoA/hexadecanoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=27 uM for oleoyl-CoA/(9Z)-octadecenoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=162 uM for beta-hydroxybutyryl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=305 uM for (3S)-hydroxy-3-methylglutaryl-CoA (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:19405909};
CC KM=142 uM for malonyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC KM=191 uM for phenylacetyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19405909};
CC Vmax=29 nmol/min/mg enzyme with hexanoyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=54 nmol/min/mg enzyme with decanoyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=37 nmol/min/mg enzyme with dodecanoyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=46 nmol/min/mg enzyme with tetradecanoyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=30 nmol/min/mg enzyme with tetradecanoyl-CoA as substrate (at 25
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=61 nmol/min/mg enzyme with tetradecanoyl-CoA as substrate (at 50
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=38 nmol/min/mg enzyme with hexadecanoyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=60 nmol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate
CC (at 37 degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=45 nmol/min/mg enzyme with beta-hydroxybutyryl-CoA as substrate
CC (at 37 degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=6 nmol/min/mg enzyme with (3S)-hydroxy-3-methylglutaryl-CoA as
CC substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=14 nmol/min/mg enzyme with malonyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Vmax=119 nmol/min/mg enzyme with phenylacetyl-CoA as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:19405909};
CC Note=kcat is 3 sec(-1) for hexanoyl-CoA hydrolase activity (at 37
CC degrees Celsius) (PubMed:19405909). kcat is 5 sec(-1) for decanoyl-
CC CoA hydrolase activity (at 37 degrees Celsius) (PubMed:19405909).
CC kcat is 3 sec(-1) for dodecanoyl-CoA hydrolase activity (at 37
CC degrees Celsius) (PubMed:19405909). kcat is 4 sec(-1) for
CC tetradecanoyl-CoA hydrolase activity (at 37 degrees Celsius)
CC (PubMed:19405909). kcat is 3 sec(-1) for tetradecanoyl-CoA hydrolase
CC activity (at 25 degrees Celsius) (PubMed:19405909). kcat is 6 sec(-1)
CC for tetradecanoyl-CoA hydrolase activity (at 50 degrees Celsius)
CC (PubMed:19405909). kcat is 3 sec(-1) for hexadecanoyl-CoA hydrolase
CC activity (at 37 degrees Celsius) (PubMed:19405909). kcat is 6 sec(-1)
CC for (9Z)-octadecenoyl-CoA hydrolase activity (at 37 degrees Celsius)
CC (PubMed:19405909). kcat is 4 sec(-1) for beta-hydroxybutyryl-CoA
CC hydrolase activity (at 37 degrees Celsius) (PubMed:19405909). kcat is
CC 7 sec(-1) for (3S)-hydroxy-3-methylglutaryl-CoA hydrolase activity
CC (at 37 degrees Celsius) (PubMed:19405909). kcat is 1 sec(-1) for
CC malonyl-CoA hydrolase activity (at 37 degrees Celsius)
CC (PubMed:19405909). kcat is 1 sec(-1) for phenylacetyl-CoA hydrolase
CC activity (at 37 degrees Celsius) (PubMed:19405909).
CC {ECO:0000269|PubMed:19405909};
CC -!- SUBUNIT: Homotetramer. Interacts with PCTP.
CC {ECO:0000269|PubMed:17704541, ECO:0000269|PubMed:19405909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17045243,
CC ECO:0000269|PubMed:17704541, ECO:0000269|PubMed:19405909}.
CC Mitochondrion {ECO:0000269|PubMed:19405909}. Nucleus
CC {ECO:0000269|PubMed:17045243, ECO:0000269|PubMed:17704541}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:17045243}. Note=During
CC interphase, found both in the nucleus and in the cytoplasm. At mitosis,
CC localizes to the spindle. Colocalizes with tubulin.
CC {ECO:0000269|PubMed:17045243}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidney and moderately in
CC the heart, liver, brain, small and large intestine. Also expressed in
CC brown adipose tissue. {ECO:0000269|PubMed:17045243,
CC ECO:0000269|PubMed:17704541, ECO:0000269|PubMed:19405909,
CC ECO:0000269|PubMed:22345407}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype until 7 weeks of age.
CC Animals are viable and fertile. After 7 weeks, mutant mice exhibit a
CC modest decrease in body weight and decreased adiposity, compared to
CC wild-type animals, despite increased food consumption. They tend to
CC show a reduced hepatic fatty acyl-CoA thioesterase activity, leading to
CC alterations in fatty acid metabolism and improved glucose homeostasis.
CC When fed a high-fat diet, mutant livers are protected against steatosis
CC and increased hepatic glucose production (PubMed:22345407). Mutant mice
CC adapt more rapidly than wild-type to short-term cold exposure by
CC increasing physical activity, food consumption and energy expenditure.
CC After 96-hour equilibration at cold temperature, genotype-dependent
CC differences are abolished. Mutant brown adipose tissue show reduced
CC lipid droplets, alterations in the ultrastructure of mitochondria and a
CC small increase in the expression of thermogenic genes
CC (PubMed:24072708). {ECO:0000269|PubMed:22345407,
CC ECO:0000269|PubMed:24072708}.
CC -!- SIMILARITY: Belongs to the thioesterase PaaI family. {ECO:0000305}.
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DR EMBL; AK002261; BAB21973.1; -; mRNA.
DR EMBL; AK008624; BAB25786.1; -; mRNA.
DR EMBL; BC018165; AAH18165.1; -; mRNA.
DR CCDS; CCDS26380.1; -.
DR RefSeq; NP_080066.1; NM_025790.2.
DR PDB; 2CY9; X-ray; 2.72 A; A/B=1-140.
DR PDBsum; 2CY9; -.
DR AlphaFoldDB; Q9CQR4; -.
DR SMR; Q9CQR4; -.
DR BioGRID; 211751; 4.
DR IntAct; Q9CQR4; 2.
DR MINT; Q9CQR4; -.
DR STRING; 10090.ENSMUSP00000006900; -.
DR iPTMnet; Q9CQR4; -.
DR PhosphoSitePlus; Q9CQR4; -.
DR REPRODUCTION-2DPAGE; Q9CQR4; -.
DR EPD; Q9CQR4; -.
DR jPOST; Q9CQR4; -.
DR MaxQB; Q9CQR4; -.
DR PaxDb; Q9CQR4; -.
DR PRIDE; Q9CQR4; -.
DR ProteomicsDB; 285707; -.
DR Antibodypedia; 10661; 215 antibodies from 34 providers.
DR DNASU; 66834; -.
DR Ensembl; ENSMUST00000006900; ENSMUSP00000006900; ENSMUSG00000006717.
DR GeneID; 66834; -.
DR KEGG; mmu:66834; -.
DR UCSC; uc007pwj.1; mouse.
DR CTD; 55856; -.
DR MGI; MGI:1914084; Acot13.
DR VEuPathDB; HostDB:ENSMUSG00000006717; -.
DR eggNOG; KOG3328; Eukaryota.
DR GeneTree; ENSGT00390000013934; -.
DR HOGENOM; CLU_089876_12_2_1; -.
DR InParanoid; Q9CQR4; -.
DR OMA; QIMRAMV; -.
DR OrthoDB; 1607235at2759; -.
DR PhylomeDB; Q9CQR4; -.
DR TreeFam; TF315062; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SABIO-RK; Q9CQR4; -.
DR BioGRID-ORCS; 66834; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Acot13; mouse.
DR EvolutionaryTrace; Q9CQR4; -.
DR PRO; PR:Q9CQR4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CQR4; protein.
DR Bgee; ENSMUSG00000006717; Expressed in interventricular septum and 257 other tissues.
DR ExpressionAtlas; Q9CQR4; baseline and differential.
DR Genevisible; Q9CQR4; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS: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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
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; Cytoplasm; Cytoskeleton; Hydrolase;
KW Lipid metabolism; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..140
FT /note="Acyl-coenzyme A thioesterase 13"
FT /id="PRO_0000156698"
FT BINDING 46
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT BINDING 83
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT BINDING 90..95
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT BINDING 108..113
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT BINDING 137
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2CY9"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2CY9"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:2CY9"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2CY9"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 111..122
FT /evidence="ECO:0007829|PDB:2CY9"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2CY9"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:2CY9"
SQ SEQUENCE 140 AA; 15183 MW; 66E47830E8643051 CRC64;
MSSMTQNLRE VMKVMFKVPG FDRVLEKVTL VSAAPEKLIC EMKVEEQHTN KLGTLHGGLT
ATLVDSISTM ALMCTERGAP GVSVDMNITY MSPAKIGEEI VITAHILKQG KTLAFASVDL
TNKTTGKLIA QGRHTKHLGN
