THIC_HUMAN
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 03-AUG-2022, entry version 189.
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; 55.
DR IntAct; Q9BWD1; 9.
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 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; Q9BWD1; -.
DR PeptideAtlas; Q9BWD1; -.
DR PRIDE; Q9BWD1; -.
DR ProteomicsDB; 6403; -.
DR ProteomicsDB; 79268; -. [Q9BWD1-1]
DR Antibodypedia; 20022; 463 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 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; 1129049at2759; -.
DR PhylomeDB; Q9BWD1; -.
DR TreeFam; TF300650; -.
DR BioCyc; MetaCyc:ENSG00000120437-MON; -.
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; 18 hits in 1087 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 203 other tissues.
DR Genevisible; Q9BWD1; HS.
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 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 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
