BACH_MOUSE
ID BACH_MOUSE Reviewed; 381 AA.
AC Q91V12; A2A8K9; A2A8L0; A2A8L2; Q3U8C6; Q59HQ2;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytosolic acyl coenzyme A thioester hydrolase;
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q64559};
DE AltName: Full=Acyl-CoA thioesterase 7;
DE AltName: Full=Brain acyl-CoA hydrolase;
DE Short=BACH;
DE AltName: Full=CTE-IIa;
DE Short=CTE-II;
DE AltName: Full=Long chain acyl-CoA thioester hydrolase;
GN Name=Acot7; Synonyms=Bach;
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] (ISOFORMS B AND C).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=12435388; DOI=10.1016/s0006-291x(02)02587-1;
RA Yamada J., Kuramochi Y., Takagi M., Watanabe T., Suga T.;
RT "Human brain acyl-CoA hydrolase isoforms encoded by a single gene.";
RL Biochem. Biophys. Res. Commun. 299:49-56(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11834298; DOI=10.1016/s0169-328x(01)00323-0;
RA Kuramochi Y., Takagi-Sakuma M., Kitahara M., Emori R., Asaba Y.,
RA Sakaguchi R., Watanabe T., Kuroda J., Hiratsuka K., Nagae Y., Suga T.,
RA Yamada J.;
RT "Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular
RT cloning and neuronal localization.";
RL Brain Res. Mol. Brain Res. 98:81-92(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=15288813; DOI=10.1016/j.abb.2004.06.005;
RA Takagi M., Kawabe K., Suga T., Yamada J.;
RT "A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and
RT molecular properties.";
RL Arch. Biochem. Biophys. 429:100-105(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Colon;
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 [7]
RP PROTEIN SEQUENCE OF 174-184 AND 269-284, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=14729242; DOI=10.1016/j.neulet.2003.10.049;
RA Yamada J., Kuramochi Y., Takagi M., Suga T.;
RT "Expression of acyl-CoA hydrolase in the developing mouse brain.";
RL Neurosci. Lett. 355:89-92(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 203-381, X-RAY CRYSTALLOGRAPHY
RP (1.78 ANGSTROMS) OF 59-206 (ISOFORM A), SUBUNIT, INDUCTION, MUTAGENESIS OF
RP ASN-67 AND ASP-256, AND ACTIVE SITE.
RX PubMed=17563367; DOI=10.1073/pnas.0700974104;
RA Forwood J.K., Thakur A.S., Guncar G., Marfori M., Mouradov D., Meng W.,
RA Robinson J., Huber T., Kellie S., Martin J.L., Hume D.A., Kobe B.;
RT "Structural basis for recruitment of tandem hotdog domains in acyl-CoA
RT thioesterase 7 and its role in inflammation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10382-10387(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (Probable). Preferentially hydrolyzes palmitoyl-CoA, but has a
CC broad specificity acting on other fatty acyl-CoAs with chain-lengths of
CC C8-C18 (Probable). May play an important physiological function in
CC brain (Probable). {ECO:0000305|PubMed:15288813}.
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:15288813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:15288813};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
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:0000250|UniProtKB:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for palmitoyl-CoA (isoform A at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15288813};
CC KM=12 uM for palmitoyl-CoA (isoform D at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15288813};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:15288813}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17563367}.
CC -!- INTERACTION:
CC Q91V12-2; Q91V12-2: Acot7; NbExp=5; IntAct=EBI-15642238, EBI-15642238;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm, cytosol
CC {ECO:0000305|PubMed:15288813}.
CC -!- SUBCELLULAR LOCATION: [Isoform D]: Cytoplasm, cytosol
CC {ECO:0000305|PubMed:15288813}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B; Synonyms=mBACHb;
CC IsoId=Q91V12-1; Sequence=Displayed;
CC Name=A; Synonyms=mBach, mBACHa, 43-kDa BACH;
CC IsoId=Q91V12-2; Sequence=VSP_000158;
CC Name=C; Synonyms=mBACHc;
CC IsoId=Q91V12-3; Sequence=VSP_000157;
CC Name=D; Synonyms=50-kDa BACH;
CC IsoId=Q91V12-4; Sequence=VSP_016955;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain. High
CC levels also found in thymus, large intestine and testis. Negligible in
CC muscle and adipose tissue. In the central and peripheral nervous
CC systems, displays a predominantly neuronal localization with highest
CC expression in cell bodies and neurites. {ECO:0000269|PubMed:11834298}.
CC -!- DEVELOPMENTAL STAGE: Detected in the brain as early as embryonic day
CC (E) 11.5. The level was low until 12.5 dpc, but promptly elevated to a
CC peak 7 days after birth. Thereafter, it declined somewhat and reached a
CC steady-state level in adulthood. These changes in BACH expression were
CC approximately reflected in the palmitoyl-CoA hydrolyzing activity in
CC the developing mouse brain, and the time course was quite similar to
CC that of microtubule-associated protein 2 (MAP2) expression. Induced
CC during embryogenesis in association with neuronal differentiation, and
CC persists after terminal differentiation into neurons in postnatal
CC stages, resulting in the constitutive high expression of BACH in the
CC adult brain in a neuron-specific manner. {ECO:0000269|PubMed:14729242}.
CC -!- INDUCTION: Up-Regulated in activated macrophages.
CC {ECO:0000269|PubMed:17563367}.
CC -!- DOMAIN: Both HotDog ACOT-type hydrolase domains are required for
CC efficient activity.
CC -!- MISCELLANEOUS: [Isoform A]: Major isoform. {ECO:0000305}.
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DR EMBL; AB088411; BAC20217.1; -; mRNA.
DR EMBL; AB088412; BAC20218.1; -; mRNA.
DR EMBL; AB049821; BAB61731.1; -; mRNA.
DR EMBL; AB207243; BAD91166.1; -; mRNA.
DR EMBL; AK152277; BAE31092.1; -; mRNA.
DR EMBL; AL611985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013507; AAH13507.1; -; mRNA.
DR CCDS; CCDS51390.1; -. [Q91V12-4]
DR CCDS; CCDS51391.2; -. [Q91V12-1]
DR CCDS; CCDS51392.1; -. [Q91V12-3]
DR RefSeq; NP_001139529.1; NM_001146057.1. [Q91V12-1]
DR RefSeq; NP_001139530.1; NM_001146058.1. [Q91V12-3]
DR RefSeq; NP_579926.2; NM_133348.2. [Q91V12-4]
DR PDB; 2Q2B; X-ray; 2.50 A; A/B=203-381.
DR PDB; 2V1O; X-ray; 1.78 A; A/B/C/D/E/F=59-206.
DR PDB; 4ZV3; X-ray; 3.10 A; A/B/C=55-369.
DR PDB; 6VFY; X-ray; 2.60 A; D/E/F=55-369.
DR PDBsum; 2Q2B; -.
DR PDBsum; 2V1O; -.
DR PDBsum; 4ZV3; -.
DR PDBsum; 6VFY; -.
DR AlphaFoldDB; Q91V12; -.
DR SMR; Q91V12; -.
DR BioGRID; 213825; 9.
DR DIP; DIP-54691N; -.
DR IntAct; Q91V12; 3.
DR MINT; Q91V12; -.
DR STRING; 10090.ENSMUSP00000074827; -.
DR iPTMnet; Q91V12; -.
DR PhosphoSitePlus; Q91V12; -.
DR SwissPalm; Q91V12; -.
DR REPRODUCTION-2DPAGE; Q91V12; -.
DR EPD; Q91V12; -.
DR MaxQB; Q91V12; -.
DR PaxDb; Q91V12; -.
DR PeptideAtlas; Q91V12; -.
DR PRIDE; Q91V12; -.
DR ProteomicsDB; 265194; -. [Q91V12-1]
DR ProteomicsDB; 265195; -. [Q91V12-2]
DR ProteomicsDB; 265196; -. [Q91V12-3]
DR ProteomicsDB; 265197; -. [Q91V12-4]
DR Antibodypedia; 12967; 159 antibodies from 22 providers.
DR DNASU; 70025; -.
DR Ensembl; ENSMUST00000030779; ENSMUSP00000030779; ENSMUSG00000028937. [Q91V12-1]
DR Ensembl; ENSMUST00000075363; ENSMUSP00000074827; ENSMUSG00000028937. [Q91V12-4]
DR Ensembl; ENSMUST00000105652; ENSMUSP00000101277; ENSMUSG00000028937. [Q91V12-3]
DR GeneID; 70025; -.
DR KEGG; mmu:70025; -.
DR UCSC; uc008vzx.2; mouse. [Q91V12-4]
DR UCSC; uc008vzz.2; mouse. [Q91V12-3]
DR UCSC; uc008waa.2; mouse. [Q91V12-2]
DR CTD; 11332; -.
DR MGI; MGI:1917275; Acot7.
DR VEuPathDB; HostDB:ENSMUSG00000028937; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00940000155229; -.
DR HOGENOM; CLU_050164_0_1_1; -.
DR InParanoid; Q91V12; -.
DR OMA; PTDVNWG; -.
DR OrthoDB; 1069806at2759; -.
DR PhylomeDB; Q91V12; -.
DR TreeFam; TF329579; -.
DR BRENDA; 3.1.2.2; 3474.
DR BRENDA; 3.1.2.20; 3474.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SABIO-RK; Q91V12; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 70025; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Acot7; mouse.
DR EvolutionaryTrace; Q91V12; -.
DR PRO; PR:Q91V12; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91V12; protein.
DR Bgee; ENSMUSG00000028937; Expressed in seminiferous tubule of testis and 286 other tissues.
DR ExpressionAtlas; Q91V12; baseline and differential.
DR Genevisible; Q91V12; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISO:MGI.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; ISO:MGI.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; ISO:MGI.
DR GO; GO:0009062; P:fatty acid catabolic process; IDA:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0036116; P:long-chain fatty-acyl-CoA catabolic process; ISO:MGI.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; ISO:MGI.
DR GO; GO:1900535; P:palmitic acid biosynthetic process; ISO:MGI.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 2.
DR Pfam; PF03061; 4HBT; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Reference proteome; Repeat; Serine esterase.
FT CHAIN 1..381
FT /note="Cytosolic acyl coenzyme A thioester hydrolase"
FT /id="PRO_0000053807"
FT DOMAIN 51..169
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 225..339
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT REGION 342..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /evidence="ECO:0000269|PubMed:17563367"
FT ACT_SITE 256
FT /evidence="ECO:0000269|PubMed:17563367"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00154"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00154"
FT MOD_RES 284
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00154"
FT VAR_SEQ 1..59
FT /note="MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLG
FT HCVTMGR -> MLTLHRALALRVLRKEVTEAYLREKVKQ (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12435388"
FT /id="VSP_000157"
FT VAR_SEQ 1..58
FT /note="MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLG
FT HCVTMG -> MSGPTTDTPAAIQIC (in isoform A)"
FT /evidence="ECO:0000303|PubMed:11834298,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_000158"
FT VAR_SEQ 1..58
FT /note="MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLG
FT HCVTMG -> MAPPLPSSSMAPPRLIHSGTGLLDTCSQIPPPPPSSAVAAKMSGPTTDT
FT PAAIQIC (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15288813"
FT /id="VSP_016955"
FT MUTAGEN 67
FT /note="N->A: Dramatic reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:17563367"
FT MUTAGEN 256
FT /note="D->A: Dramatic reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:17563367"
FT CONFLICT 186
FT /note="E -> D (in Ref. 4; BAE31092)"
FT /evidence="ECO:0000305"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6VFY"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2V1O"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2V1O"
FT HELIX 74..93
FT /evidence="ECO:0007829|PDB:2V1O"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2V1O"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:2V1O"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2V1O"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:2V1O"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2V1O"
FT STRAND 153..170
FT /evidence="ECO:0007829|PDB:2V1O"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:2V1O"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:2Q2B"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2Q2B"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6VFY"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6VFY"
FT HELIX 248..267
FT /evidence="ECO:0007829|PDB:2Q2B"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:2Q2B"
FT STRAND 289..301
FT /evidence="ECO:0007829|PDB:2Q2B"
FT STRAND 304..316
FT /evidence="ECO:0007829|PDB:2Q2B"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6VFY"
FT STRAND 324..334
FT /evidence="ECO:0007829|PDB:2Q2B"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6VFY"
FT HELIX 353..367
FT /evidence="ECO:0007829|PDB:2Q2B"
SQ SEQUENCE 381 AA; 42537 MW; 813852DBEB6834C4 CRC64;
MKLLVGTLRL WEVGRQVAFS SLTPGQECSG LRKTFWAAMR AVRTRADHQK LGHCVTMGRI
MRPDDANVAG NVHGGTILKM IEEAGAIIST RHCNSQNGER CVAALARVER TDFLSPMCIG
EVAHVSAEIT YTSKHSVEVQ VHVMSENILT GTKKLTNKAT LWYVPLSLKN VDKVLEVPPI
VYLRQEQEEE GRKRYEAQKL ERMETKWRNG DIVQPVLNPE PNTVSYSQSS LIHLVGPSDC
TLHGFVHGGV TMKLMDEVAG IVAARHCKTN IVTASVDAIN FHDKIRKGCV ITISGRMTFT
SNKSMEIEVL VDADPVVDNS QKRYRAASAF FTYVSLNQEG KPMPVPQLVP ETEDEKKRFE
EGKGRYLQMK AKRQGHTEPQ P
