ACO11_MOUSE
ID ACO11_MOUSE Reviewed; 594 AA.
AC Q8VHQ9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Acyl-coenzyme A thioesterase 11 {ECO:0000250|UniProtKB:Q8WXI4};
DE Short=Acyl-CoA thioesterase 11 {ECO:0000250|UniProtKB:Q8WXI4};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:Q8WXI4};
DE AltName: Full=Acyl-CoA thioester hydrolase 11;
DE AltName: Full=Adipose-associated thioesterase;
DE AltName: Full=Brown fat-inducible thioesterase;
DE Short=BFIT;
DE AltName: Full=Palmitoyl-coenzyme A thioesterase {ECO:0000250|UniProtKB:Q8WXI4};
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q8WXI4};
DE Flags: Precursor;
GN Name=Acot11; Synonyms=Bfit, Thea;
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].
RC STRAIN=FVB/N;
RX PubMed=11696000; DOI=10.1042/bj3600135;
RA Adams S.H., Chui C., Schilbach S.L., Yu X.X., Goddard A.D., Grimaldi J.C.,
RA Lee J., Dowd P., Colman S., Lewin D.A.;
RT "BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose
RT tissue: cloning, organization of the human gene and assessment of a
RT potential link to obesity.";
RL Biochem. J. 360:135-142(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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).
CC -!- FUNCTION: Has an acyl-CoA thioesterase activity with a preference for
CC the long chain fatty acyl-CoA thioesters hexadecanoyl-CoA/palmitoyl-CoA
CC and tetradecanoyl-CoA/myristoyl-CoA which are the main substrates in
CC the mitochondrial beta-oxidation pathway.
CC {ECO:0000250|UniProtKB:Q8WXI4}.
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:Q8WXI4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:Q8WXI4};
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:Q8WXI4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q8WXI4};
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:Q8WXI4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q8WXI4};
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:Q8WXI4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000250|UniProtKB:Q8WXI4};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q8WXI4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q8WXI4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8WXI4}.
CC -!- INDUCTION: By cold exposure and repressed by heat exposure.
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DR EMBL; AF416923; AAL40939.1; -; mRNA.
DR EMBL; BC042492; AAH42492.1; -; mRNA.
DR CCDS; CCDS18426.1; -.
DR RefSeq; NP_079866.2; NM_025590.4.
DR AlphaFoldDB; Q8VHQ9; -.
DR SMR; Q8VHQ9; -.
DR BioGRID; 236860; 3.
DR STRING; 10090.ENSMUSP00000099823; -.
DR iPTMnet; Q8VHQ9; -.
DR PhosphoSitePlus; Q8VHQ9; -.
DR SwissPalm; Q8VHQ9; -.
DR EPD; Q8VHQ9; -.
DR MaxQB; Q8VHQ9; -.
DR PaxDb; Q8VHQ9; -.
DR PRIDE; Q8VHQ9; -.
DR ProteomicsDB; 285842; -.
DR Antibodypedia; 33192; 257 antibodies from 30 providers.
DR DNASU; 329910; -.
DR Ensembl; ENSMUST00000102762; ENSMUSP00000099823; ENSMUSG00000034853.
DR GeneID; 329910; -.
DR KEGG; mmu:329910; -.
DR UCSC; uc008tyv.2; mouse.
DR CTD; 26027; -.
DR MGI; MGI:1913736; Acot11.
DR VEuPathDB; HostDB:ENSMUSG00000034853; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00940000156460; -.
DR HOGENOM; CLU_035725_0_0_1; -.
DR InParanoid; Q8VHQ9; -.
DR OMA; YEQCEVI; -.
DR PhylomeDB; Q8VHQ9; -.
DR TreeFam; TF328368; -.
DR BRENDA; 3.1.2.20; 3474.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 329910; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Acot11; mouse.
DR PRO; PR:Q8VHQ9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VHQ9; protein.
DR Bgee; ENSMUSG00000034853; Expressed in gastrula and 205 other tissues.
DR ExpressionAtlas; Q8VHQ9; baseline and differential.
DR Genevisible; Q8VHQ9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0009409; P:response to cold; IEP:BHF-UCL.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 1.
DR Pfam; PF03061; 4HBT; 2.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Mitochondrion; Phosphoprotein; Reference proteome; Repeat; Serine esterase;
KW Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..594
FT /note="Acyl-coenzyme A thioesterase 11"
FT /id="PRO_0000053814"
FT DOMAIN 45..157
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 217..330
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 370..582
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..95
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 122..124
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 272..274
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 594 AA; 67355 MW; 9A51D3BCF38870C9 CRC64;
MIQNVGNHLR RGFASMFSNR TSRKSISHPE SGDPPTMAEG EGYRNPTEVQ MSQLVLPCHT
NHRGELSIGQ LLKWIDTTAC LSAERHAGCP CVTASMDDIY FDHTISVGQV VNIKAKVNRA
FNSSMEVGIQ VVSEDLCSEK QWSVCKALAT FVAHRELSKV KLKQVIPLTE EEKTEHGVAA
ERRRMRLVYA DTIKDLLTHC VIQDDLDKDC SNMVPAEKTR VESVELVLPP HANHQGNTFG
GQIMAWMENV ATIAASRLCH AHPTLKAIEM FHFRGPSQVG DRLVLKAIVN NAFKHSMEVG
VCVEAYRQEA ETQRRHINSA FMTFVVLDKD DQPQKLPWIR PQPGEGERRY REASARKKIR
LDRKYLVSCK QAEVALSVPW DPSNQVYLSY YNVSSLKTLM AKDNWVLSVE ISEVRLYILE
EDFLSFHLEM VVNVDAAQVF QLLSDLRRRP EWDKHYRSVE LVQQVDEDDA IYHVISPALS
GNTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHHETP EYQRGETLCS GFCLWREGDQ
MTKVSYYNQA TPGFLNYVTT NVSGLSSEFY NTFKACESFL LDNRNDLAPS LQTL
