ACOT5_MOUSE
ID ACOT5_MOUSE Reviewed; 421 AA.
AC Q6Q2Z6; E9QKJ5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Acyl-coenzyme A thioesterase 5;
DE Short=Acyl-CoA thioesterase 5;
DE EC=3.1.2.2 {ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
DE AltName: Full=Peroxisomal acyl-coenzyme A thioester hydrolase Ic;
DE Short=PTE-Ic {ECO:0000303|PubMed:15007068};
DE Short=Peroxisomal acyl-CoA thioesterase Ic;
GN Name=Acot5;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=129/Sv;
RX PubMed=15007068; DOI=10.1074/jbc.m313863200;
RA Westin M.A.K., Alexson S.E.H., Hunt M.C.;
RT "Molecular cloning and characterization of two mouse peroxisome
RT proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal
RT acyl-CoA thioesterases.";
RL J. Biol. Chem. 279:21841-21848(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=16940157; DOI=10.1096/fj.06-6042com;
RA Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.;
RT "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters
RT shows that convergent, functional evolution results in a reduced number of
RT human peroxisomal ACOTs.";
RL FASEB J. 20:1855-1864(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:16940157). Mainly active on medium-chain acyl-CoAs
CC (PubMed:15007068). Seems to be involved in intraperoxisomal regulation
CC of acyl-CoA levels, but not CoASH levels (PubMed:15007068). May have a
CC function in termination of beta-oxidation of fatty acids
CC (PubMed:15007068). {ECO:0000269|PubMed:15007068,
CC ECO:0000303|PubMed:16940157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:15007068};
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:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:15007068};
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:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000305|PubMed:15007068};
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:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:15007068};
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:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:15007068};
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:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000305|PubMed:15007068};
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:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC Evidence={ECO:0000305|PubMed:15007068};
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:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540;
CC Evidence={ECO:0000269|PubMed:15007068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28.4 uM for hexanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=7.7 uM for octanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=18 uM for decanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=7.6 uM for dodecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=5.6 uM for tetradecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=15.9 uM for hexadecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=7.0 uM for (9Z)-hexadecenoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=34.8 uM for octadecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=8.9 uM for (9Z)-octadecenoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=32.5 uM for (9Z,12Z)-octadecadienoyl-coA
CC {ECO:0000269|PubMed:15007068};
CC KM=32.7 uM for eicosanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=1.6 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoyl-coA
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.23 umol/min/mg enzyme with hexanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.74 umol/min/mg enzyme with octanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=1.20 umol/min/mg enzyme with decanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=1.10 umol/min/mg enzyme with dodecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.83 umol/min/mg enzyme with tetradecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.49 umol/min/mg enzyme with hexadecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.32 umol/min/mg enzyme with (9Z)-hexadecenoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.38 umol/min/mg enzyme with octadecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.14 umol/min/mg enzyme with (9Z)-octadecenoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.17 umol/min/mg enzyme with (9Z,12Z)-octadecadienoyl-coA as
CC substrate {ECO:0000269|PubMed:15007068};
CC Vmax=0.18 umol/min/mg enzyme with eicosanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.23 umol/min/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoyl-
CC coA as substrate {ECO:0000269|PubMed:15007068};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:15007068, ECO:0000305|PubMed:16940157}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15007068}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, brain, testis and
CC proximal and distal intestine; expressed at low level in the liver.
CC {ECO:0000269|PubMed:15007068}.
CC -!- INDUCTION: In the liver and kidney, by peroxisome proliferator, via the
CC peroxisome proliferator-activated receptors (PPARs) and by fasting.
CC {ECO:0000269|PubMed:15007068}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AY563099; AAS75457.1; -; mRNA.
DR EMBL; AC125071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26037.1; -.
DR RefSeq; NP_663419.3; NM_145444.3.
DR RefSeq; XP_006515756.2; XM_006515693.3.
DR AlphaFoldDB; Q6Q2Z6; -.
DR SMR; Q6Q2Z6; -.
DR BioGRID; 229947; 2.
DR STRING; 10090.ENSMUSP00000042019; -.
DR SwissLipids; SLP:000000531; -.
DR ESTHER; mouse-acot5; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A51; -.
DR TCDB; 4.C.3.1.1; the acyl-coa thioesterase (acoa-t) family.
DR iPTMnet; Q6Q2Z6; -.
DR PhosphoSitePlus; Q6Q2Z6; -.
DR jPOST; Q6Q2Z6; -.
DR MaxQB; Q6Q2Z6; -.
DR PaxDb; Q6Q2Z6; -.
DR PeptideAtlas; Q6Q2Z6; -.
DR PRIDE; Q6Q2Z6; -.
DR ProteomicsDB; 285651; -.
DR DNASU; 217698; -.
DR Ensembl; ENSMUST00000046422; ENSMUSP00000042019; ENSMUSG00000042540.
DR GeneID; 217698; -.
DR KEGG; mmu:217698; -.
DR UCSC; uc007oeh.1; mouse.
DR CTD; 217698; -.
DR MGI; MGI:2384969; Acot5.
DR VEuPathDB; HostDB:ENSMUSG00000042540; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q6Q2Z6; -.
DR OMA; TICHKNE; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q6Q2Z6; -.
DR TreeFam; TF314911; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR SABIO-RK; Q6Q2Z6; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 217698; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q6Q2Z6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6Q2Z6; protein.
DR Bgee; ENSMUSG00000042540; Expressed in lip and 11 other tissues.
DR ExpressionAtlas; Q6Q2Z6; baseline and differential.
DR Genevisible; Q6Q2Z6; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:HGNC-UCL.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0032788; P:saturated monocarboxylic acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0032789; P:unsaturated monocarboxylic acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Peroxisome;
KW Reference proteome; Serine esterase.
FT CHAIN 1..421
FT /note="Acyl-coenzyme A thioesterase 5"
FT /id="PRO_0000202151"
FT MOTIF 419..421
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 326
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="R -> C (in Ref. 1; AAS75457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 46573 MW; 3156BA777FFBEE94 CRC64;
MVPTVSLEPT GHSCWDEPLS IAVRGLAPEQ PVTLRTALRD EKGALFRAHA RYRADSHGEL
DLARTPALGG SFSGLEPMGL LWAMEPDRPF WRLIKRDVQT PFVVELEVLD GHEPDGGRLL
ARAVHERHFM APGVRRVPVR EGRVRATLFL PPGTGPFPGI IDLFGVGGGL LEYRASLLAG
KGFAVMALAY YKYDDLPKVI DILHLEYFEE AVTYLLSHPQ VKGPGVGLLG ISKGAELSLS
MASFLKGITA AVVINGATVN VISTLYYKEE SLPGLGMHLE RIKVTKDGFK DIIDILNVPL
EAPDQKSLIP LERSDTAFLF LVGQDDHNWK SEFYAREASK RLQAHGKEKP QIVCYPKTGH
HIEPPYIPWS IAAPHSYFDK PILLGGEPRA HAMAQVDAWQ RLQTFFHKHL SGDKRPSPAK
L
