ID   THIC_HUMAN              Reviewed;         397 AA.
AC   Q9BWD1; B7Z233; E1P5B1; Q16146; Q5TCL7; Q8TDM4;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Acetyl-CoA acetyltransferase, cytosolic;
DE            EC=2.3.1.9 {ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000269|PubMed:7911016};
DE   AltName: Full=Acetyl-CoA transferase-like protein;
DE   AltName: Full=Cytosolic acetoacetyl-CoA thiolase;
GN   Name=ACAT2; Synonyms=ACTL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP   ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX   PubMed=7911016; DOI=10.1006/bbrc.1994.1726;
RA   Song X.-Q., Fukao T., Yamaguchi S., Miyazawa S., Hashimoto T., Orii T.;
RT   "Molecular cloning and nucleotide sequence of complementary DNA for human
RT   hepatic cytosolic acetoacetyl-coenzyme A thiolase.";
RL   Biochem. Biophys. Res. Commun. 201:478-485(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Chen H., Peng J., Huang C.-H.;
RT   "Identification of the human acetyl CoA transferase like (ACTL) protein by
RT   yeast two-hybrid screen.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-211.
RC   TISSUE=Lung;
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 16-39; 195-210; 280-302 AND 342-361, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-233 AND LYS-235, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH COENZYME A,
RP   FUNCTION, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=15733928; DOI=10.1016/j.jmb.2005.01.018;
RA   Kursula P., Sikkila H., Fukao T., Kondo N., Wierenga R.K.;
RT   "High resolution crystal structures of human cytosolic thiolase (CT): a
RT   comparison of the active sites of human CT, bacterial thiolase, and
RT   bacterial KAS I.";
RL   J. Mol. Biol. 347:189-201(2005).
CC   -!- FUNCTION: Involved in the biosynthetic pathway of cholesterol.
CC       {ECO:0000303|PubMed:15733928}.
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         ECO:0000269|PubMed:7911016};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC         Evidence={ECO:0000305|PubMed:7911016};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000269|PubMed:7911016}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15733928}.
CC   -!- INTERACTION:
CC       Q9BWD1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1047273, EBI-739832;
CC       Q9BWD1; P54274: TERF1; NbExp=2; IntAct=EBI-1047273, EBI-710997;
CC       Q9BWD1; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-1047273, EBI-12040603;
CC       Q9BWD1; P36508: ZNF76; NbExp=3; IntAct=EBI-1047273, EBI-7254550;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:7911016}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BWD1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BWD1-2; Sequence=VSP_056217;
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; S70154; AAB30856.1; -; mRNA.
DR   EMBL; AF356877; AAM00223.1; -; mRNA.
DR   EMBL; AK294273; BAH11719.1; -; mRNA.
DR   EMBL; AL135914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47619.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW47620.1; -; Genomic_DNA.
DR   EMBL; BC000408; AAH00408.1; -; mRNA.
DR   CCDS; CCDS5268.1; -. [Q9BWD1-1]
DR   PIR; JC2378; JC2378.
DR   RefSeq; NP_001290182.1; NM_001303253.1. [Q9BWD1-2]
DR   RefSeq; NP_005882.2; NM_005891.2. [Q9BWD1-1]
DR   PDB; 1WL4; X-ray; 1.55 A; A=1-397.
DR   PDB; 1WL5; X-ray; 2.26 A; A=1-397.
DR   PDBsum; 1WL4; -.
DR   PDBsum; 1WL5; -.
DR   AlphaFoldDB; Q9BWD1; -.
DR   SMR; Q9BWD1; -.
DR   BioGRID; 106557; 66.
DR   IntAct; Q9BWD1; 11.
DR   MINT; Q9BWD1; -.
DR   STRING; 9606.ENSP00000356015; -.
DR   DrugBank; DB01992; Coenzyme A.
DR   DrugBank; DB01915; S-Hydroxycysteine.
DR   GuidetoPHARMACOLOGY; 2436; -.
DR   SwissLipids; SLP:000001266; -.
DR   GlyCosmos; Q9BWD1; 1 site, 1 glycan.
DR   GlyGen; Q9BWD1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BWD1; -.
DR   PhosphoSitePlus; Q9BWD1; -.
DR   SwissPalm; Q9BWD1; -.
DR   BioMuta; ACAT2; -.
DR   DMDM; 52000838; -.
DR   OGP; Q9BWD1; -.
DR   REPRODUCTION-2DPAGE; IPI00291419; -.
DR   EPD; Q9BWD1; -.
DR   jPOST; Q9BWD1; -.
DR   MassIVE; Q9BWD1; -.
DR   MaxQB; Q9BWD1; -.
DR   PaxDb; 9606-ENSP00000356015; -.
DR   PeptideAtlas; Q9BWD1; -.
DR   ProteomicsDB; 6403; -.
DR   ProteomicsDB; 79268; -. [Q9BWD1-1]
DR   Pumba; Q9BWD1; -.
DR   Antibodypedia; 20022; 523 antibodies from 29 providers.
DR   DNASU; 39; -.
DR   Ensembl; ENST00000367048.5; ENSP00000356015.4; ENSG00000120437.9. [Q9BWD1-1]
DR   GeneID; 39; -.
DR   KEGG; hsa:39; -.
DR   MANE-Select; ENST00000367048.5; ENSP00000356015.4; NM_005891.3; NP_005882.2.
DR   UCSC; uc010kjy.4; human. [Q9BWD1-1]
DR   AGR; HGNC:94; -.
DR   CTD; 39; -.
DR   DisGeNET; 39; -.
DR   GeneCards; ACAT2; -.
DR   HGNC; HGNC:94; ACAT2.
DR   HPA; ENSG00000120437; Tissue enriched (liver).
DR   MalaCards; ACAT2; -.
DR   MIM; 100678; gene+phenotype.
DR   neXtProt; NX_Q9BWD1; -.
DR   OpenTargets; ENSG00000120437; -.
DR   PharmGKB; PA19; -.
DR   VEuPathDB; HostDB:ENSG00000120437; -.
DR   eggNOG; KOG1390; Eukaryota.
DR   GeneTree; ENSGT01030000234626; -.
DR   HOGENOM; CLU_031026_0_0_1; -.
DR   InParanoid; Q9BWD1; -.
DR   OMA; ICPSIAI; -.
DR   OrthoDB; 5481312at2759; -.
DR   PhylomeDB; Q9BWD1; -.
DR   TreeFam; TF300650; -.
DR   BioCyc; MetaCyc:ENSG00000120437-MONOMER; -.
DR   BRENDA; 2.3.1.9; 2681.
DR   PathwayCommons; Q9BWD1; -.
DR   Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR   SignaLink; Q9BWD1; -.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 39; 19 hits in 1165 CRISPR screens.
DR   ChiTaRS; ACAT2; human.
DR   EvolutionaryTrace; Q9BWD1; -.
DR   GeneWiki; ACAT2; -.
DR   GenomeRNAi; 39; -.
DR   Pharos; Q9BWD1; Tchem.
DR   PRO; PR:Q9BWD1; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9BWD1; Protein.
DR   Bgee; ENSG00000120437; Expressed in ventricular zone and 205 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
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   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
DR   Genevisible; Q9BWD1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW   Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT   CHAIN           1..397
FT                   /note="Acetyl-CoA acetyltransferase, cytosolic"
FT                   /id="PRO_0000206409"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000305|PubMed:15733928"
FT   ACT_SITE        383
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:15733928"
FT   BINDING         223
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:15733928,
FT                   ECO:0007744|PDB:1WL4"
FT   BINDING         226
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:15733928,
FT                   ECO:0007744|PDB:1WL4"
FT   BINDING         252
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:15733928,
FT                   ECO:0007744|PDB:1WL4"
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:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   MOD_RES         200
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         233
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         235
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..19
FT                   /note="MNAGSDPVVIVSAARTIIG -> MGSHPVLRIWGNRRATAASLGRSGGRLSS
FT                   PRLLRVVAPTLTFAQTSRC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056217"
FT   VARIANT         211
FT                   /note="K -> R (in dbSNP:rs25683)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_019686"
FT   CONFLICT        169
FT                   /note="K -> T (in Ref. 1; AAB30856)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="V -> A (in Ref. 1; AAB30856)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        375
FT                   /note="R -> G (in Ref. 2; AAM00223)"
FT                   /evidence="ECO:0000305"
FT   STRAND          8..15
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   TURN            24..27
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           30..45
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           69..76
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           94..107
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          112..122
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           145..149
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           160..171
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           175..194
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   TURN            195..201
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          212..216
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           228..232
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   TURN            240..243
FT                   /evidence="ECO:0007829|PDB:1WL5"
FT   HELIX           248..250
FT                   /evidence="ECO:0007829|PDB:1WL5"
FT   STRAND          255..265
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           266..271
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          277..287
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           290..295
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           297..308
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           325..335
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           348..351
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   HELIX           358..373
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          377..384
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   TURN            385..387
FT                   /evidence="ECO:0007829|PDB:1WL4"
FT   STRAND          388..396
FT                   /evidence="ECO:0007829|PDB:1WL4"
SQ   SEQUENCE   397 AA;  41351 MW;  E3A8DAFB6F341B18 CRC64;
     MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE DVSEVIFGHV
     LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAVQSIGIGD SSIVVAGGME
     NMSKAPHLAY LRTGVKIGEM PLTDSILCDG LTDAFHNCHM GITAENVAKK WQVSREDQDK
     VAVLSQNRTE NAQKAGHFDK EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT
     DGTGTVTPAN ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA
     IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA LGHPLGASGC
     RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE
//