THIC_RAT
ID THIC_RAT Reviewed; 397 AA.
AC Q5XI22;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PROTEIN SEQUENCE OF 16-39; 195-210; 218-223 AND 342-372, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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}.
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DR EMBL; BC083872; AAH83872.1; -; mRNA.
DR RefSeq; NP_001006996.1; NM_001006995.1.
DR AlphaFoldDB; Q5XI22; -.
DR SMR; Q5XI22; -.
DR STRING; 10116.ENSRNOP00000068312; -.
DR iPTMnet; Q5XI22; -.
DR PhosphoSitePlus; Q5XI22; -.
DR jPOST; Q5XI22; -.
DR PaxDb; Q5XI22; -.
DR PRIDE; Q5XI22; -.
DR Ensembl; ENSRNOT00000114086; ENSRNOP00000083545; ENSRNOG00000019189.
DR GeneID; 308100; -.
DR KEGG; rno:308100; -.
DR CTD; 39; -.
DR RGD; 1359366; Acat2.
DR eggNOG; KOG1390; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR InParanoid; Q5XI22; -.
DR OrthoDB; 1129049at2759; -.
DR Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR SABIO-RK; Q5XI22; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q5XI22; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; TAS:UniProtKB.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:RGD.
DR GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0031670; P:cellular response to nutrient; IEP:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:UniProtKB.
DR GO; GO:0019408; P:dolichol biosynthetic process; TAS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0046952; P:ketone body catabolic process; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; ISO:RGD.
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_0000271366"
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"
SQ SEQUENCE 397 AA; 41108 MW; 850589DD5AF4D84F CRC64;
MNAGSDPVVI ISAARTAIGS FNGALSTVPV HNLGTTVIKE VLQRAKVAPE EVSEVIFGHV
LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAAQSIAMGD STIVVAGGME
NMSKAPHLAH LRSGVKMGEV PLADSILCDG LTDAFHNYHM GITAENVAKK WQVSREAQDK
VAVVSQNRAE HAQKAGHFDK EIVPVHVSSR KGLTEVKIDE FPRHGSNLEA MSKLKPYFLT
DGTGTVTPAN ASGMNDGAAA VVLMKKTEAE SRMLKPLAQV VSWSQAGVEP SVMGVGPIPA
IKQAVAKAGW SLEDVDVFEI NEAFAAVSAA IAKELGLSPE KVNIDGGAIA LGHPLGASGC
RILVTLLHTL ERVGGTRGVA ALCIGGGMGI AMCVQRG
