THIC_MOUSE
ID THIC_MOUSE Reviewed; 397 AA.
AC Q8CAY6; Q3TJY7; Q62292; Q96EB7; Q99K88; Q9CYV2;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Acetyl-CoA acetyltransferase, cytosolic;
DE EC=2.3.1.9 {ECO:0000255|PROSITE-ProRule:PRU10020};
DE AltName: Full=Cytosolic acetoacetyl-CoA thiolase;
GN Name=Acat2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Embryo, and Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Retina;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 115-397.
RC STRAIN=C57BL/6J;
RX PubMed=2055458; DOI=10.1017/s0016672300029220;
RA Dudley K., Shanahan F., Burtenshaw M., Evans E.P., Ruddy S., Lyon M.F.;
RT "Isolation and characterization of a cDNA clone corresponding to the mouse
RT T-complex gene Tcp-1x.";
RL Genet. Res. 57:147-152(1991).
RN [4]
RP PROTEIN SEQUENCE OF 342-372, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Involved in the biosynthetic pathway of cholesterol.
CC {ECO:0000250|UniProtKB:Q9BWD1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC Evidence={ECO:0000250|UniProtKB:Q9BWD1};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q9BWD1}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BWD1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BWD1}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK013275; BAB28763.1; ALT_INIT; mRNA.
DR EMBL; AK037249; BAC29776.1; -; mRNA.
DR EMBL; AK166813; BAE39040.1; -; mRNA.
DR EMBL; AK167234; BAE39358.1; -; mRNA.
DR EMBL; BC004823; AAH04823.2; -; mRNA.
DR EMBL; BC012496; AAH12496.2; -; mRNA.
DR EMBL; M35797; AAA76575.1; -; mRNA.
DR CCDS; CCDS37437.1; -.
DR PIR; A53174; A53174.
DR RefSeq; NP_033364.2; NM_009338.3.
DR AlphaFoldDB; Q8CAY6; -.
DR SMR; Q8CAY6; -.
DR BioGRID; 225610; 3.
DR STRING; 10090.ENSMUSP00000007005; -.
DR iPTMnet; Q8CAY6; -.
DR PhosphoSitePlus; Q8CAY6; -.
DR SwissPalm; Q8CAY6; -.
DR REPRODUCTION-2DPAGE; Q8CAY6; -.
DR EPD; Q8CAY6; -.
DR jPOST; Q8CAY6; -.
DR MaxQB; Q8CAY6; -.
DR PaxDb; Q8CAY6; -.
DR PeptideAtlas; Q8CAY6; -.
DR PRIDE; Q8CAY6; -.
DR ProteomicsDB; 262810; -.
DR Ensembl; ENSMUST00000007005; ENSMUSP00000007005; ENSMUSG00000023832.
DR GeneID; 110460; -.
DR KEGG; mmu:110460; -.
DR UCSC; uc008alp.1; mouse.
DR CTD; 39; -.
DR MGI; MGI:87871; Acat2.
DR VEuPathDB; HostDB:ENSMUSG00000023832; -.
DR eggNOG; KOG1390; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR InParanoid; Q8CAY6; -.
DR OMA; ICPSIAI; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; Q8CAY6; -.
DR TreeFam; TF300650; -.
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 110460; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Acat2; mouse.
DR PRO; PR:Q8CAY6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CAY6; protein.
DR Bgee; ENSMUSG00000023832; Expressed in condyle and 292 other tissues.
DR ExpressionAtlas; Q8CAY6; baseline and differential.
DR Genevisible; Q8CAY6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; IDA:CACAO.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT CHAIN 1..397
FT /note="Acetyl-CoA acetyltransferase, cytosolic"
FT /id="PRO_0000206410"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT ACT_SITE 383
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT BINDING 223
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT BINDING 226
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT BINDING 252
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT SITE 353
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P42765"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWD1"
FT CONFLICT 106
FT /note="I -> L (in Ref. 2; AAH12496)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..119
FT /note="VAGGM -> CLTGK (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> P (in Ref. 3; AAA76575)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="H -> T (in Ref. 3; AAA76575)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> D (in Ref. 1; BAB28763)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="K -> T (in Ref. 3; AAA76575)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="V -> L (in Ref. 1; BAB28763)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="K -> E (in Ref. 1; BAC29776)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="E -> G (in Ref. 3; AAA76575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 41298 MW; AABC2DF22F4EE930 CRC64;
MNAGSDPVVI VSAARTAIGS FNGALSTVPV HEMGTTVIKE VLQRAKVAPE EVSEVIFGHV
LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAAQSIAMGD STIVVAGGME
NMSKAPHLTH LRTGVRMGEV PLADSILCDG LTDAFHNYHM GITAENVAKK WQVSREAQDK
VAVLSQNRAE HAQKAGHFDK EIVPVLVSSR KGLTEVKIDE FPRHGSNLEA MGKLKPYFLT
DGTGTVTPAN ASGMNDGAAA VVLMKKTEAE RRMLKPLARI VSWSQAGVEP SVMGVGPIPA
IKQAVAKAGW SLEDVDLFEI NEAFAAVSAA IAKELGLNPE KVNIDGGAIA LGHPLGASGC
RILVTLLHTL ERVGGTRGVA ALCIGGGMGV AMCVQRG
