ACO13_PONAB
ID ACO13_PONAB Reviewed; 140 AA.
AC Q5R833;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Acyl-coenzyme A thioesterase 13 {ECO:0000250|UniProtKB:Q9NPJ3};
DE Short=Acyl-CoA thioesterase 13 {ECO:0000250|UniProtKB:Q9NPJ3};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:Q9NPJ3};
DE AltName: Full=Hotdog-fold thioesterase superfamily member 2 {ECO:0000250|UniProtKB:Q9NPJ3};
DE AltName: Full=Palmitoyl-CoA hydrolase {ECO:0000250|UniProtKB:Q9NPJ3};
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q9NPJ3};
DE AltName: Full=Thioesterase superfamily member 2 {ECO:0000250|UniProtKB:Q9NPJ3};
DE Short=THEM2 {ECO:0000250|UniProtKB:Q9NPJ3};
DE Contains:
DE RecName: Full=Acyl-coenzyme A thioesterase 13, N-terminally processed;
GN Name=ACOT13; Synonyms=THEM2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (By similarity). Has acyl-CoA thioesterase activity towards
CC medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also
CC hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA
CC (in vitro) (By similarity). May play a role in controlling adaptive
CC thermogenesis (By similarity). {ECO:0000250|UniProtKB:Q9CQR4,
CC ECO:0000250|UniProtKB:Q9NPJ3}.
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:0000250|UniProtKB:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
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:Q9NPJ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000250|UniProtKB:Q9NPJ3};
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with PCTP (By
CC similarity). {ECO:0000250|UniProtKB:Q9CQR4,
CC ECO:0000250|UniProtKB:Q9NPJ3}.
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 -!- SIMILARITY: Belongs to the thioesterase PaaI family. {ECO:0000305}.
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DR EMBL; CR859922; CAH92077.1; -; mRNA.
DR RefSeq; NP_001126211.1; NM_001132739.1.
DR AlphaFoldDB; Q5R833; -.
DR SMR; Q5R833; -.
DR STRING; 9601.ENSPPYP00000018207; -.
DR GeneID; 100173179; -.
DR KEGG; pon:100173179; -.
DR CTD; 55856; -.
DR eggNOG; KOG3328; Eukaryota.
DR InParanoid; Q5R833; -.
DR OrthoDB; 1607235at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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 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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; Hydrolase; Lipid metabolism;
KW Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..140
FT /note="Acyl-coenzyme A thioesterase 13"
FT /id="PRO_0000424503"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
FT CHAIN 2..140
FT /note="Acyl-coenzyme A thioesterase 13, N-terminally
FT processed"
FT /id="PRO_0000290196"
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 2
FT /note="N-acetylthreonine; in Acyl-coenzyme A thioesterase
FT 13, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ3"
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"
SQ SEQUENCE 140 AA; 14960 MW; 084E36EFEE715A18 CRC64;
MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT
ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL
TNKATGKLIA QGRHTKHLGN
