ACO12_MOUSE
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 03-AUG-2022, entry version 161.
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: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels. 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 AlphaFoldDB; Q9DBK0; -.
DR SMR; 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; 177 antibodies from 24 providers.
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 VEuPathDB; HostDB:ENSMUSG00000021620; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00940000160328; -.
DR HOGENOM; CLU_035725_0_0_1; -.
DR InParanoid; Q9DBK0; -.
DR OMA; CTVSYLN; -.
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; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9DBK0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9DBK0; protein.
DR Bgee; ENSMUSG00000021620; Expressed in right kidney and 48 other tissues.
DR ExpressionAtlas; Q9DBK0; baseline and differential.
DR Genevisible; Q9DBK0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; 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 BINDING 54..56
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 83..85
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
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
