ACOT8_HUMAN
ID ACOT8_HUMAN Reviewed; 319 AA.
AC O14734; O15261; Q17RX4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Acyl-coenzyme A thioesterase 8;
DE Short=Acyl-CoA thioesterase 8;
DE EC=3.1.2.1 {ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9299485};
DE EC=3.1.2.11 {ECO:0000250|UniProtKB:P58137};
DE EC=3.1.2.2 {ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485};
DE EC=3.1.2.3 {ECO:0000250|UniProtKB:P58137};
DE EC=3.1.2.5 {ECO:0000250|UniProtKB:P58137};
DE AltName: Full=Choloyl-coenzyme A thioesterase;
DE EC=3.1.2.27 {ECO:0000269|PubMed:9299485};
DE AltName: Full=HIV-Nef-associated acyl-CoA thioesterase;
DE AltName: Full=Peroxisomal acyl-CoA thioesterase 2 {ECO:0000303|PubMed:11755680};
DE Short=PTE-2 {ECO:0000303|PubMed:11755680};
DE AltName: Full=Peroxisomal acyl-coenzyme A thioester hydrolase 1;
DE Short=PTE-1;
DE AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase 1;
DE AltName: Full=Thioesterase II;
DE Short=hACTE-III;
DE Short=hACTEIII;
DE Short=hTE;
GN Name=ACOT8; Synonyms=ACTEIII, PTE1 {ECO:0000303|PubMed:10092594};
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RX PubMed=9299485; DOI=10.1006/bbrc.1997.7217;
RA Watanabe H., Shiratori T., Shoji H., Miyatake S., Okazaki Y., Ikuta K.,
RA Sato T., Saito T.;
RT "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct
RT binding with HIV Nef.";
RL Biochem. Biophys. Res. Commun. 238:234-239(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH HIV-1
RP NEF (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RC TISSUE=Lymphoid tissue;
RX PubMed=9153233; DOI=10.1074/jbc.272.21.13779;
RA Liu L.X., Margottin F., Le Gall S., Schwartz O., Selig L., Benarous R.,
RA Benichou S.;
RT "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-
RT mediated CD4 down-regulation.";
RL J. Biol. Chem. 272:13779-13785(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Muscle;
RX PubMed=10092594; DOI=10.1074/jbc.274.14.9216;
RA Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.;
RT "Identification of peroxisomal acyl-CoA thioesterases in yeast and
RT humans.";
RL J. Biol. Chem. 274:9216-9223(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 CATALYTIC ACTIVITY, AND PATHWAY.
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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-78.
RX PubMed=15194431; DOI=10.1016/j.yexcr.2004.02.029;
RA Ishizuka M., Toyama Y., Watanabe H., Fujiki Y., Takeuchi A., Yamasaki S.,
RA Yuasa S., Miyazaki M., Nakajima N., Taki S., Saito T.;
RT "Overexpression of human acyl-CoA thioesterase upregulates peroxisome
RT biogenesis.";
RL Exp. Cell Res. 297:127-141(2004).
RN [8]
RP REVIEW.
RX PubMed=11755680; DOI=10.1016/s0163-7827(01)00017-0;
RA Hunt M.C., Alexson S.E.H.;
RT "The role Acyl-CoA thioesterases play in mediating intracellular lipid
RT metabolism.";
RL Prog. Lipid Res. 41:99-130(2002).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:9299485, PubMed:9153233, PubMed:15194431). Displays no
CC strong substrate specificity with respect to the carboxylic acid moiety
CC of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20)
CC straight-chain, saturated and unsaturated acyl-CoAS but is inactive
CC towards substrates with longer aliphatic chains (PubMed:9299485,
CC PubMed:9153233). Moreover, it catalyzes the hydrolysis of CoA esters of
CC bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes
CC with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity).
CC Is also able to hydrolyze CoA esters of dicarboxylic acids (By
CC similarity). It is involved in the metabolic regulation of peroxisome
CC proliferation (PubMed:15194431). {ECO:0000250|UniProtKB:P58137,
CC ECO:0000269|PubMed:15194431, ECO:0000269|PubMed:9153233,
CC ECO:0000269|PubMed:9299485}.
CC -!- FUNCTION: (Microbial infection) May mediate Nef-induced down-regulation
CC of CD4 cell-surface expression (PubMed:9153233).
CC {ECO:0000269|PubMed:9153233}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
CC Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+);
CC Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC Evidence={ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC Evidence={ECO:0000305|PubMed:9299485};
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:10944470, ECO:0000269|PubMed:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000305|PubMed:9299485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA + H(+);
CC Xref=Rhea:RHEA:40799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:48944, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338;
CC Evidence={ECO:0000269|PubMed:10944470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40800;
CC Evidence={ECO:0000305|PubMed:10944470};
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:9153233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000305|PubMed:9153233};
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:10944470, ECO:0000269|PubMed:9153233,
CC ECO:0000269|PubMed:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000305|PubMed:9299485};
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:9153233,
CC ECO:0000269|PubMed:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:9299485};
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:9153233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:9153233};
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:9153233,
CC ECO:0000269|PubMed:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:9299485};
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:9153233, ECO:0000269|PubMed:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:9299485};
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:9299485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:9299485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonyl-CoA = CoA + H(+) + malonate;
CC Xref=Rhea:RHEA:40219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15792, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40220;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetyl-CoA + H2O = acetoacetate + CoA + H(+);
CC Xref=Rhea:RHEA:15673, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287; EC=3.1.2.11;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15674;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate;
CC Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + succinyl-CoA = CoA + H(+) + succinate;
CC Xref=Rhea:RHEA:11516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=3.1.2.3;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutaryl-CoA + H2O = CoA + glutarate + H(+);
CC Xref=Rhea:RHEA:40575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30921, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanedioyl-CoA = CoA + H(+) + hexanedioate;
CC Xref=Rhea:RHEA:40583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17128, ChEBI:CHEBI:57287, ChEBI:CHEBI:76327;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40584;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanedioyl-CoA = CoA + H(+) + octanedioate;
CC Xref=Rhea:RHEA:40587, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76282, ChEBI:CHEBI:76317;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40588;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanedioyl-CoA + H2O = CoA + decanedioate + H(+);
CC Xref=Rhea:RHEA:40591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76283, ChEBI:CHEBI:76316;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40592;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanedioyl-CoA + H2O = CoA + dodecanedioate + H(+);
CC Xref=Rhea:RHEA:40595, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76273, ChEBI:CHEBI:76315;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40596;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + H2O = (9Z)-tetradecenoate + CoA +
CC H(+); Xref=Rhea:RHEA:40135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32370, ChEBI:CHEBI:57287, ChEBI:CHEBI:65060;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40136;
CC Evidence={ECO:0000250|UniProtKB:P58137};
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:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000250|UniProtKB:P58137};
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:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000250|UniProtKB:P58137};
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:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC Evidence={ECO:0000250|UniProtKB:P58137};
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:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000250|UniProtKB:P58137};
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:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,8-dimethylnonanoyl-CoA + H2O = 4,8-dimethylnonanoate + CoA +
CC H(+); Xref=Rhea:RHEA:40223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77061, ChEBI:CHEBI:77063;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40224;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6-dimethylheptanoyl-CoA + H2O = 2,6-dimethylheptanoate + CoA
CC + H(+); Xref=Rhea:RHEA:59952, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:84847, ChEBI:CHEBI:143533;
CC Evidence={ECO:0000250|UniProtKB:Q8VHK0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59953;
CC Evidence={ECO:0000250|UniProtKB:Q8VHK0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA + H2O = 3-hydroxy-3-
CC methylglutarate + CoA + H(+); Xref=Rhea:RHEA:16305,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17325,
CC ChEBI:CHEBI:43074, ChEBI:CHEBI:57287; EC=3.1.2.5;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16306;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA +
CC H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA
CC + H(+); Xref=Rhea:RHEA:59936, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:63001, ChEBI:CHEBI:85674;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59937;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyloctadecanoyl-CoA + H2O = 2-methyloctadecanoate + CoA +
CC H(+); Xref=Rhea:RHEA:59940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:143530, ChEBI:CHEBI:143531;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59941;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin F2alpha-CoA = CoA + H(+) + prostaglandin
CC F2alpha; Xref=Rhea:RHEA:59948, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57404, ChEBI:CHEBI:143532;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59949;
CC Evidence={ECO:0000250|UniProtKB:P58137};
CC -!- ACTIVITY REGULATION: Inhibited by CoASH (IC(50)=10-15 uM). Also
CC inhibited by cysteine-reactive agents. {ECO:0000250|UniProtKB:P58137}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.1 uM for decanoyl-CoA {ECO:0000269|PubMed:9153233};
CC Vmax=7.1 umol/min/mg enzyme {ECO:0000269|PubMed:9153233};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:9299485}.
CC -!- SUBUNIT: Homodimer (By similarity). {ECO:0000250|UniProtKB:P58137}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human immunodeficiency
CC virus (HIV-1) Nef (via middle region); this interaction enhances ACOT8
CC Acyl-CoA thioesterase activity and occurs in a Nef myristoylation-
CC independent manner (PubMed:9299485). According to a second report, the
CC interaction with HIV-1 Nef occurs in a Nef myristoylation-independent
CC manner but does not enhance ACOT8 Acyl-CoA thioesterase activity
CC (PubMed:9153233). {ECO:0000269|PubMed:9153233,
CC ECO:0000269|PubMed:9299485}.
CC -!- INTERACTION:
CC O14734; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-1237371, EBI-10181968;
CC O14734; P50542: PEX5; NbExp=3; IntAct=EBI-1237371, EBI-597835;
CC O14734; Q04864: REL; NbExp=3; IntAct=EBI-1237371, EBI-307352;
CC O14734; Q04864-2: REL; NbExp=3; IntAct=EBI-1237371, EBI-10829018;
CC O14734; P04601: nef; Xeno; NbExp=7; IntAct=EBI-1237371, EBI-6164028;
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:10092594,
CC ECO:0000269|PubMed:15194431}. Note=Predominantly localized in the
CC peroxisome but a localization to the cytosol cannot be excluded.
CC {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}.
CC -!- TISSUE SPECIFICITY: Detected in a T-cell line (at protein level).
CC Ubiquitous (PubMed:9153233, PubMed:9299485).
CC {ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.
CC -!- INDUCTION: Regulated by peroxisome proliferator (such as Clofibrate),
CC via the peroxisome proliferator-activated receptors (PPARs).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AF014404; AAB71665.1; -; mRNA.
DR EMBL; X86032; CAA60024.1; -; mRNA.
DR EMBL; AF124264; AAD27616.1; -; mRNA.
DR EMBL; AL008726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117155; AAI17156.1; -; mRNA.
DR EMBL; BC117157; AAI17158.1; -; mRNA.
DR CCDS; CCDS13378.1; -.
DR PIR; JC5644; JC5644.
DR RefSeq; NP_005460.2; NM_005469.3.
DR AlphaFoldDB; O14734; -.
DR SMR; O14734; -.
DR BioGRID; 115323; 56.
DR DIP; DIP-38179N; -.
DR IntAct; O14734; 23.
DR MINT; O14734; -.
DR STRING; 9606.ENSP00000217455; -.
DR SwissLipids; SLP:000000591; -.
DR GlyGen; O14734; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14734; -.
DR PhosphoSitePlus; O14734; -.
DR SwissPalm; O14734; -.
DR BioMuta; ACOT8; -.
DR EPD; O14734; -.
DR jPOST; O14734; -.
DR MassIVE; O14734; -.
DR MaxQB; O14734; -.
DR PaxDb; O14734; -.
DR PeptideAtlas; O14734; -.
DR PRIDE; O14734; -.
DR ProteomicsDB; 48196; -.
DR Antibodypedia; 4138; 250 antibodies from 28 providers.
DR DNASU; 10005; -.
DR Ensembl; ENST00000217455.9; ENSP00000217455.4; ENSG00000101473.17.
DR GeneID; 10005; -.
DR KEGG; hsa:10005; -.
DR MANE-Select; ENST00000217455.9; ENSP00000217455.4; NM_005469.4; NP_005460.2.
DR UCSC; uc002xqa.3; human.
DR CTD; 10005; -.
DR DisGeNET; 10005; -.
DR GeneCards; ACOT8; -.
DR HGNC; HGNC:15919; ACOT8.
DR HPA; ENSG00000101473; Low tissue specificity.
DR MIM; 608123; gene.
DR neXtProt; NX_O14734; -.
DR OpenTargets; ENSG00000101473; -.
DR PharmGKB; PA33941; -.
DR VEuPathDB; HostDB:ENSG00000101473; -.
DR eggNOG; KOG3016; Eukaryota.
DR GeneTree; ENSGT00390000004207; -.
DR InParanoid; O14734; -.
DR OMA; SQVWFRT; -.
DR OrthoDB; 826588at2759; -.
DR PhylomeDB; O14734; -.
DR TreeFam; TF315124; -.
DR BioCyc; MetaCyc:HS02282-MON; -.
DR BRENDA; 3.1.2.2; 2681.
DR BRENDA; 3.1.2.20; 2681.
DR PathwayCommons; O14734; -.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; O14734; -.
DR SignaLink; O14734; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 10005; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; ACOT8; human.
DR GeneWiki; ACOT8; -.
DR GenomeRNAi; 10005; -.
DR Pharos; O14734; Tbio.
DR PRO; PR:O14734; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O14734; protein.
DR Bgee; ENSG00000101473; Expressed in mucosa of transverse colon and 166 other tissues.
DR ExpressionAtlas; O14734; baseline and differential.
DR Genevisible; O14734; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
DR GO; GO:0047603; F:acetoacetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; TAS:Reactome.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016289; F:CoA hydrolase activity; TAS:Reactome.
DR GO; GO:0044466; F:glutaryl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047994; F:hydroxymethylglutaryl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0004778; F:succinyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
DR GO; GO:0043649; P:dicarboxylic acid catabolic process; IDA:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0045225; P:negative regulation of CD4 production; IDA:UniProtKB.
DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
DR Gene3D; 2.40.160.210; -; 1.
DR InterPro; IPR042171; Acyl-CoA_hotdog.
DR InterPro; IPR003703; Acyl_CoA_thio.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR11066; PTHR11066; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR TIGRFAMs; TIGR00189; tesB; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Host-virus interaction; Hydrolase; Lipid metabolism;
KW Peroxisome; Peroxisome biogenesis; Reference proteome; Serine esterase.
FT CHAIN 1..319
FT /note="Acyl-coenzyme A thioesterase 8"
FT /id="PRO_0000202152"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 317..319
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MUTAGEN 78
FT /note="H->A: Reduces Acyl-CoA thioesterase activity and
FT peroxisome proliferation."
FT /evidence="ECO:0000269|PubMed:15194431"
FT CONFLICT 291..293
FT /note="LWR -> VWS (in Ref. 2; CAA60024)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="L -> R (in Ref. 2; CAA60024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35914 MW; 8345C6E5EABF3326 CRC64;
MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV
GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP
IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA
QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL
LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV
TCAQEGVIRV KPQVSESKL
