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3-ketoacyl-CoA thiolase, peroxisomal (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase) (Peroxisomal 3-oxoacyl-CoA thiolase)

 THIK_HUMAN              Reviewed;         424 AA.
P09110; G5E935; Q96CA6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
10-OCT-2018, entry version 200.
RecName: Full=3-ketoacyl-CoA thiolase, peroxisomal;
EC=2.3.1.16;
AltName: Full=Acetyl-CoA acyltransferase;
AltName: Full=Beta-ketothiolase;
AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase;
Flags: Precursor;
Name=ACAA1; Synonyms=ACAA, PTHIO;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3194209; DOI=10.1093/nar/16.21.10369;
Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.;
"Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase.";
Nucleic Acids Res. 16:10369-10369(1988).
[2]
SEQUENCE REVISION TO 285-287.
Bout A.;
Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2726492; DOI=10.1093/nar/17.9.3588;
Fairbairn L.J., Tanner M.J.A.;
"Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-
CoA thiolase.";
Nucleic Acids Res. 17:3588-3588(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1679347; DOI=10.1016/0167-4781(91)90035-K;
Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.;
"Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA
thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient
patient.";
Biochim. Biophys. Acta 1090:43-51(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ALA-387.
TISSUE=Lymph, Ovary, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND THR-60, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-26, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, AND SUBUNIT.
Structural genomics consortium (SGC);
"Crystal structure of human peroxisomal acetyl-COA acyl transferase 1
(ACAA1).";
Submitted (OCT-2006) to the PDB data bank.
-!- CATALYTIC ACTIVITY: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
-!- PATHWAY: Lipid metabolism; fatty acid metabolism.
-!- SUBUNIT: Homodimer. {ECO:0000269|Ref.12}.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P09110-1; Sequence=Displayed;
Name=2;
IsoId=P09110-2; Sequence=VSP_046195, VSP_046196;
Note=No experimental confirmation available.;
-!- INDUCTION: Peroxisomal thiolase is markedly induced (at the level
of transcription) by various hypolipidemic compounds in parallel
with the other two enzymes of the peroxisomal beta-oxidation
system.
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X12966; CAA31412.1; -; mRNA.
EMBL; X14813; CAA32918.1; -; mRNA.
EMBL; X65140; CAA46270.1; -; Genomic_DNA.
EMBL; X65148; CAA46271.1; -; Genomic_DNA.
EMBL; AP006309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64516.1; -; Genomic_DNA.
EMBL; BC000635; AAH00635.1; -; mRNA.
EMBL; BC011977; AAH11977.1; -; mRNA.
EMBL; BC014474; AAH14474.1; -; mRNA.
CCDS; CCDS2673.1; -. [P09110-1]
CCDS; CCDS46794.1; -. [P09110-2]
PIR; S17515; XUHUAB.
RefSeq; NP_001123882.1; NM_001130410.1. [P09110-2]
RefSeq; NP_001598.1; NM_001607.3. [P09110-1]
UniGene; Hs.643487; -.
PDB; 2IIK; X-ray; 2.55 A; A/B=30-423.
PDBsum; 2IIK; -.
ProteinModelPortal; P09110; -.
SMR; P09110; -.
BioGrid; 106548; 32.
IntAct; P09110; 7.
STRING; 9606.ENSP00000333664; -.
DrugBank; DB09069; Trimetazidine.
CarbonylDB; P09110; -.
iPTMnet; P09110; -.
PhosphoSitePlus; P09110; -.
SwissPalm; P09110; -.
BioMuta; ACAA1; -.
DMDM; 135751; -.
REPRODUCTION-2DPAGE; IPI00012828; -.
UCD-2DPAGE; P09110; -.
EPD; P09110; -.
MaxQB; P09110; -.
PaxDb; P09110; -.
PeptideAtlas; P09110; -.
PRIDE; P09110; -.
ProteomicsDB; 52200; -.
DNASU; 30; -.
Ensembl; ENST00000301810; ENSP00000301810; ENSG00000060971. [P09110-2]
Ensembl; ENST00000333167; ENSP00000333664; ENSG00000060971. [P09110-1]
GeneID; 30; -.
KEGG; hsa:30; -.
UCSC; uc003cht.4; human. [P09110-1]
CTD; 30; -.
DisGeNET; 30; -.
EuPathDB; HostDB:ENSG00000060971.17; -.
GeneCards; ACAA1; -.
HGNC; HGNC:82; ACAA1.
HPA; HPA006764; -.
HPA; HPA007244; -.
MIM; 604054; gene.
neXtProt; NX_P09110; -.
OpenTargets; ENSG00000060971; -.
PharmGKB; PA24419; -.
eggNOG; KOG1389; Eukaryota.
eggNOG; COG0183; LUCA.
GeneTree; ENSGT00910000144143; -.
HOGENOM; HOG000012239; -.
HOVERGEN; HBG003112; -.
InParanoid; P09110; -.
KO; K07513; -.
OMA; GVQLNRM; -.
OrthoDB; EOG091G09C6; -.
PhylomeDB; P09110; -.
TreeFam; TF332308; -.
BioCyc; MetaCyc:HS00752-MONOMER; -.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-9033241; Peroxisomal protein import.
Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins.
UniPathway; UPA00199; -.
ChiTaRS; ACAA1; human.
EvolutionaryTrace; P09110; -.
GeneWiki; ACAA1; -.
GenomeRNAi; 30; -.
PRO; PR:P09110; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000060971; Expressed in 236 organ(s), highest expression level in nephron tubule.
CleanEx; HS_ACAA1; -.
ExpressionAtlas; P09110; baseline and differential.
Genevisible; P09110; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0008775; F:acetate CoA-transferase activity; EXP:Reactome.
GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; TAS:Reactome.
GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IMP:UniProtKB.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0008206; P:bile acid metabolic process; IMP:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 1.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
InterPro; IPR020610; Thiolase_AS.
InterPro; IPR020617; Thiolase_C.
InterPro; IPR020613; Thiolase_CS.
InterPro; IPR020616; Thiolase_N.
Pfam; PF02803; Thiolase_C; 1.
Pfam; PF00108; Thiolase_N; 1.
PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
SUPFAM; SSF53901; SSF53901; 2.
TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
PROSITE; PS00098; THIOLASE_1; 1.
PROSITE; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing;
Complete proteome; Fatty acid metabolism; Lipid metabolism;
Peroxisome; Phosphoprotein; Polymorphism; Reference proteome;
Transferase; Transit peptide.
TRANSIT 1 26 Peroxisome.
{ECO:0000244|PubMed:25944712}.
CHAIN 27 424 3-ketoacyl-CoA thiolase, peroxisomal.
/FTId=PRO_0000034067.
ACT_SITE 123 123 Acyl-thioester intermediate.
{ECO:0000250}.
ACT_SITE 377 377 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020}.
ACT_SITE 408 408 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020}.
MOD_RES 59 59 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 60 60 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 149 181 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046195.
VAR_SEQ 272 331 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046196.
VARIANT 172 172 E -> D (in dbSNP:rs156265).
/FTId=VAR_011904.
VARIANT 387 387 V -> A (in dbSNP:rs2229528).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_069148.
STRAND 38 45 {ECO:0000244|PDB:2IIK}.
TURN 51 53 {ECO:0000244|PDB:2IIK}.
TURN 55 58 {ECO:0000244|PDB:2IIK}.
HELIX 61 76 {ECO:0000244|PDB:2IIK}.
HELIX 80 82 {ECO:0000244|PDB:2IIK}.
STRAND 86 89 {ECO:0000244|PDB:2IIK}.
STRAND 91 94 {ECO:0000244|PDB:2IIK}.
HELIX 95 97 {ECO:0000244|PDB:2IIK}.
HELIX 98 107 {ECO:0000244|PDB:2IIK}.
STRAND 116 120 {ECO:0000244|PDB:2IIK}.
HELIX 122 124 {ECO:0000244|PDB:2IIK}.
HELIX 125 138 {ECO:0000244|PDB:2IIK}.
STRAND 143 152 {ECO:0000244|PDB:2IIK}.
TURN 153 155 {ECO:0000244|PDB:2IIK}.
HELIX 168 170 {ECO:0000244|PDB:2IIK}.
HELIX 172 175 {ECO:0000244|PDB:2IIK}.
HELIX 176 178 {ECO:0000244|PDB:2IIK}.
HELIX 181 191 {ECO:0000244|PDB:2IIK}.
HELIX 196 216 {ECO:0000244|PDB:2IIK}.
TURN 217 222 {ECO:0000244|PDB:2IIK}.
STRAND 226 231 {ECO:0000244|PDB:2IIK}.
STRAND 237 242 {ECO:0000244|PDB:2IIK}.
HELIX 254 259 {ECO:0000244|PDB:2IIK}.
STRAND 263 265 {ECO:0000244|PDB:2IIK}.
STRAND 279 289 {ECO:0000244|PDB:2IIK}.
HELIX 290 296 {ECO:0000244|PDB:2IIK}.
STRAND 302 311 {ECO:0000244|PDB:2IIK}.
HELIX 314 319 {ECO:0000244|PDB:2IIK}.
HELIX 320 332 {ECO:0000244|PDB:2IIK}.
HELIX 336 338 {ECO:0000244|PDB:2IIK}.
STRAND 339 344 {ECO:0000244|PDB:2IIK}.
HELIX 349 359 {ECO:0000244|PDB:2IIK}.
HELIX 363 365 {ECO:0000244|PDB:2IIK}.
HELIX 372 375 {ECO:0000244|PDB:2IIK}.
TURN 379 381 {ECO:0000244|PDB:2IIK}.
HELIX 382 397 {ECO:0000244|PDB:2IIK}.
STRAND 401 409 {ECO:0000244|PDB:2IIK}.
TURN 410 412 {ECO:0000244|PDB:2IIK}.
STRAND 413 421 {ECO:0000244|PDB:2IIK}.
SEQUENCE 424 AA; 44292 MW; 71B2BBAFA06AE412 CRC64;
MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT
PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLSDI PETVPLSTVN
RQCSSGLQAV ASIAGGIRNG SYDIGMACGV ESMSLADRGN PGNITSRLME KEKARDCLIP
MGITSENVAE RFGISREKQD TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI
TVTQDEGIRP STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI
LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS QAAYCVEKLR
LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR AYGVVSMCIG TGMGAAAVFE
YPGN


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