THIKA_MOUSE
ID THIKA_MOUSE Reviewed; 424 AA.
AC Q921H8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=3-ketoacyl-CoA thiolase A, peroxisomal {ECO:0000305};
DE EC=2.3.1.16 {ECO:0000305|PubMed:15043762};
DE AltName: Full=Acetyl-CoA C-myristoyltransferase;
DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P21775};
DE AltName: Full=Acetyl-CoA acyltransferase A;
DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P21775};
DE AltName: Full=Beta-ketothiolase A;
DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase A;
DE Flags: Precursor;
GN Name=Acaa1a {ECO:0000312|MGI:MGI:2148491}; Synonyms=Acaa1;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, FUNCTION, AND PATHWAY.
RC STRAIN=129/Sv, and C57BL/6J; TISSUE=Liver;
RX PubMed=15043762; DOI=10.1186/1471-2091-5-3;
RA Chevillard G., Clemencet M.-C., Etienne P., Martin P., Pineau T.,
RA Latruffe N., Nicolas-Frances V.;
RT "Molecular cloning, gene structure and expression profile of two mouse
RT peroxisomal 3-ketoacyl-CoA thiolase genes.";
RL BMC Biochem. 5:3-3(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173 AND LYS-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Responsible for the thiolytic cleavage of straight chain 3-
CC keto fatty acyl-CoAs (3-oxoacyl-CoAs) (Probable). Plays an important
CC role in fatty acid peroxisomal beta-oxidation (Probable). Catalyzes the
CC cleavage of short, medium, long, and very long straight chain 3-
CC oxoacyl-CoAs (By similarity). {ECO:0000250|UniProtKB:P21775,
CC ECO:0000305|PubMed:15043762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000305|PubMed:15043762};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000305|PubMed:15043762};
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:0000250|UniProtKB:P21775};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000305|PubMed:15043762};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000305|PubMed:15043762};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA +
CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + CoA =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + acetyl-CoA;
CC Xref=Rhea:RHEA:39131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74298, ChEBI:CHEBI:74304;
CC Evidence={ECO:0000250|UniProtKB:P09110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39132;
CC Evidence={ECO:0000250|UniProtKB:P09110};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:15043762}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in liver and intestine.
CC {ECO:0000269|PubMed:15043762}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AY273811; AAP31668.1; -; mRNA.
DR EMBL; AY304542; AAP72964.1; -; Genomic_DNA.
DR EMBL; BC012400; AAH12400.1; -; mRNA.
DR CCDS; CCDS23613.1; -.
DR RefSeq; NP_570934.1; NM_130864.3.
DR RefSeq; XP_006511986.1; XM_006511923.1.
DR AlphaFoldDB; Q921H8; -.
DR SMR; Q921H8; -.
DR BioGRID; 227535; 5.
DR IntAct; Q921H8; 4.
DR MINT; Q921H8; -.
DR STRING; 10090.ENSMUSP00000042351; -.
DR iPTMnet; Q921H8; -.
DR PhosphoSitePlus; Q921H8; -.
DR SwissPalm; Q921H8; -.
DR EPD; Q921H8; -.
DR jPOST; Q921H8; -.
DR MaxQB; Q921H8; -.
DR PaxDb; Q921H8; -.
DR PeptideAtlas; Q921H8; -.
DR PRIDE; Q921H8; -.
DR ProteomicsDB; 262916; -.
DR Ensembl; ENSMUST00000039784; ENSMUSP00000042351; ENSMUSG00000036138.
DR GeneID; 113868; -.
DR KEGG; mmu:113868; -.
DR UCSC; uc009sas.1; mouse.
DR CTD; 113868; -.
DR MGI; MGI:2148491; Acaa1a.
DR VEuPathDB; HostDB:ENSMUSG00000036138; -.
DR eggNOG; KOG1389; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; Q921H8; -.
DR OMA; DYYWGMG; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; Q921H8; -.
DR TreeFam; TF332308; -.
DR BRENDA; 2.3.1.16; 3474.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 113868; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Acaa1a; mouse.
DR PRO; PR:Q921H8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q921H8; protein.
DR Bgee; ENSMUSG00000036138; Expressed in ileal epithelium and 284 other tissues.
DR ExpressionAtlas; Q921H8; baseline and differential.
DR Genevisible; Q921H8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0008775; F:acetate CoA-transferase activity; ISO:MGI.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; TAS:MGI.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:MGI.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:MGI.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Peroxisome; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Peroxisome"
FT /evidence="ECO:0000250"
FT CHAIN 27..424
FT /note="3-ketoacyl-CoA thiolase A, peroxisomal"
FT /id="PRO_0000034068"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 424 AA; 43953 MW; 56F30DF43198C9A8 CRC64;
MHRLQVVLGH LAGRPESSSA LQAAPCSARF PQASASDVVV VHGRRTPIGR ASRGGFKNTT
PDELLSAVLT AVLQDVRLKP EQLGDISVGN VLEPGAGAVM ARIAQFLSGI PETVPLSTVN
RQCSSGLQAV ANIAGGIRNG SYDIGMACGV ESMSLSGMGN PGNISSRLLE SEKARDCLTP
MGMTSENVAE RFGISRQKQD DFALASQQKA ASAQSRGCFR AEIVPVTTTV LDDKGDKKTI
TVSQDEGVRP STTMQGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI
LGVLRSYAVV GVPPDVMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS QAVYCVEKLG
IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR AYGVVSMCIG TGMGAAAVFE
YPGN
