ID   ACO12_MOUSE             Reviewed;         556 AA.
AC   Q9DBK0; Q544M5; Q8R108;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   02-JUN-2021, entry version 157.
DE   RecName: Full=Acetyl-coenzyme A thioesterase {ECO:0000305};
DE            EC=3.1.2.1 {ECO:0000250|UniProtKB:Q8WYK0};
DE   AltName: Full=Acyl-CoA thioester hydrolase 12;
DE   AltName: Full=Acyl-coenzyme A thioesterase 12;
DE            Short=Acyl-CoA thioesterase 12;
DE   AltName: Full=Cytoplasmic acetyl-CoA hydrolase 1;
DE            Short=CACH-1;
DE            Short=mCACH-1;
GN   Name=Acot12; Synonyms=Cach, Cach1;
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=C57BL/6J; TISSUE=Liver;
RX   PubMed=12545200;
RA   Suematsu N., Okamoto K., Isohashi F.;
RT   "Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme
RT   involved in fat metabolism: cDNA cloning, sequencing and functional
RT   expression.";
RL   Acta Biochim. Pol. 49:937-945(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-556.
RC   TISSUE=Liver;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
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   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-97; LYS-160 AND
RP   LYS-229, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC       the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC       (CoASH), providing the potential to regulate intracellular levels of
CC       acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase
CC       12/ACOT12 preferentially hydrolyzes acetyl-CoA.
CC       {ECO:0000250|UniProtKB:Q8WYK0}.
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:0000250|UniProtKB:Q8WYK0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC         Evidence={ECO:0000250|UniProtKB:Q8WYK0};
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:Q99NB7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC         Evidence={ECO:0000250|UniProtKB:Q99NB7};
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:Q99NB7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC         Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC   -!- ACTIVITY REGULATION: Allosterically regulated by ATP (activator) and
CC       ADP (inhibitor) (By similarity). Cold labile, it dissociates into
CC       inactive monomers at low temperature (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WYK0, ECO:0000250|UniProtKB:Q99NB7}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000250|UniProtKB:Q8WYK0}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250|UniProtKB:Q99NB7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q8WYK0}.
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DR   EMBL; AB078618; BAB84021.1; -; mRNA.
DR   EMBL; AK004905; BAB23658.1; -; mRNA.
DR   EMBL; AK034622; BAC28775.1; -; mRNA.
DR   EMBL; BC025852; AAH25852.1; -; mRNA.
DR   CCDS; CCDS26678.1; -.
DR   RefSeq; NP_083066.1; NM_028790.3.
DR   SMR; Q9DBK0; -.
DR   IntAct; Q9DBK0; 3.
DR   MINT; Q9DBK0; -.
DR   STRING; 10090.ENSMUSP00000022120; -.
DR   iPTMnet; Q9DBK0; -.
DR   PhosphoSitePlus; Q9DBK0; -.
DR   SwissPalm; Q9DBK0; -.
DR   jPOST; Q9DBK0; -.
DR   MaxQB; Q9DBK0; -.
DR   PaxDb; Q9DBK0; -.
DR   PRIDE; Q9DBK0; -.
DR   ProteomicsDB; 285706; -.
DR   Antibodypedia; 24697; 165 antibodies.
DR   Ensembl; ENSMUST00000022120; ENSMUSP00000022120; ENSMUSG00000021620.
DR   GeneID; 74156; -.
DR   KEGG; mmu:74156; -.
DR   UCSC; uc007rka.1; mouse.
DR   CTD; 134526; -.
DR   MGI; MGI:1921406; Acot12.
DR   eggNOG; KOG2763; Eukaryota.
DR   GeneTree; ENSGT00940000160328; -.
DR   HOGENOM; CLU_035725_0_0_1; -.
DR   InParanoid; Q9DBK0; -.
DR   OMA; PLWDPHY; -.
DR   OrthoDB; 776852at2759; -.
DR   PhylomeDB; Q9DBK0; -.
DR   TreeFam; TF328368; -.
DR   BRENDA; 3.1.2.1; 3474.
DR   Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 74156; 0 hits in 52 CRISPR screens.
DR   PRO; PR:Q9DBK0; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9DBK0; protein.
DR   Bgee; ENSMUSG00000021620; Expressed in proximal tubule and 83 other tissues.
DR   Genevisible; Q9DBK0; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IDA:MGI.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:MGI.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; ISO:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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   Reference proteome; Repeat; Serine esterase.
FT   CHAIN           1..556
FT                   /note="Acetyl-coenzyme A thioesterase"
FT                   /id="PRO_0000053810"
FT   DOMAIN          6..118
FT                   /note="HotDog ACOT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          180..295
FT                   /note="HotDog ACOT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          327..536
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   REGION          54..56
FT                   /note="Coenzyme A binding"
FT                   /evidence="ECO:0000250"
FT   REGION          83..85
FT                   /note="Coenzyme A binding"
FT                   /evidence="ECO:0000250"
FT   REGION          235..237
FT                   /note="Coenzyme A binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /note="Coenzyme A"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         34
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         97
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         160
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         229
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   556 AA;  61762 MW;  9FE9C487BBCBB812 CRC64;
     MESMVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI SCVTASMDDI
     LFEDTARIGQ IITIRAKVTR AFSTSMEISI KVIVQDKFTG IQKLLCVAFS TFVAKPVGKE
     KVHLKPVLLQ TEQEQVEHNL ASERRKVRLQ HENTFNNIMK ESSRFSDSIC NEEEGTATTM
     GTSVQSIELV LPPHANHHGN TFGGQIMAWM ETVATISASR LCHGHPFLKS VDMFKFRGPS
     TVGDRLVFSA IVNNTFQNSV EVGVRVEAFD CQEWAEGQGR HINSAFLIYN AVDDQEKLIT
     FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL SAQWDISKKG SLSNTNVEAL
     KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKLVGSP AHIAYHLLSD LTKRPLWDPH
     YISCEVIDQV SEDDQIYYIT CSVVNGDKPK DFVVLVSRRK PLKDNNTYTV ALRSVVLPSV
     PSSPQYIRSE VICAGFLIQA VDSNSCTVTY LNQMSDSILP YFAGNIGGWS KSIEEAAASC
     IKFIENATPD GLKSVL
//