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Entry version 141 (17 Jun 2020)
Sequence version 1 (01 Jan 1990)
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Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

Acaa2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (Probable). Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies (Probable). Also displays hydrolase activity on various fatty acyl-CoAs (PubMed:16476568). Thereby, could be responsible for the production of acetate in a side reaction to beta-oxidation (Probable). Abolishes BNIP3-mediated apoptosis and mitochondrial damage (By similarity).By similarity1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The 3-oxoacetyl-CoA thiolase activity is inhibited by acetyl-CoA while the acetyl-CoA hydrolase activity is inhibited by acetoacetyl-CoA.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=11.4 µM for acetoacetyl-CoA1 Publication
  2. KM=0.71 mM for acetyl-CoA1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei92Acyl-thioester intermediateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei224Coenzyme ABy similarity1
    Binding sitei227Coenzyme ABy similarity1
    Binding sitei251Coenzyme A; via carbonyl oxygenBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei352Increases nucleophilicity of active site CysBy similarity1
    Active sitei382Proton donor/acceptorPROSITE-ProRule annotation1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Hydrolase, Transferase
    Biological processFatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-77289 Mitochondrial Fatty Acid Beta-Oxidation

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P13437

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00659

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001412

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    3-ketoacyl-CoA thiolase, mitochondrialCurated (EC:2.3.1.161 Publication)
    Alternative name(s):
    Acetyl-CoA acetyltransferaseCurated (EC:2.3.1.91 Publication)
    Acetyl-CoA acyltransferase
    Acyl-CoA hydrolase, mitochondrialCurated (EC:3.1.2.-1 Publication, EC:3.1.2.11 Publication, EC:3.1.2.21 Publication)
    Beta-ketothiolase
    Mitochondrial 3-oxoacyl-CoA thiolase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:Acaa2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    620482 Acaa2

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002233011 – 3973-ketoacyl-CoA thiolase, mitochondrialAdd BLAST397
    <p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 16Mitochondrion; not cleavedAdd BLAST16

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25N6-acetyllysine; alternateBy similarity1
    Modified residuei25N6-succinyllysine; alternateBy similarity1
    Modified residuei45N6-succinyllysineBy similarity1
    Modified residuei119PhosphothreonineBy similarity1
    Modified residuei121PhosphoserineBy similarity1
    Modified residuei127PhosphotyrosineBy similarity1
    Modified residuei136PhosphothreonineBy similarity1
    Modified residuei137N6-acetyllysine; alternateBy similarity1
    Modified residuei137N6-succinyllysine; alternateBy similarity1
    Modified residuei143N6-acetyllysine; alternateBy similarity1
    Modified residuei143N6-succinyllysine; alternateBy similarity1
    Modified residuei158N6-acetyllysine; alternateBy similarity1
    Modified residuei158N6-succinyllysine; alternateBy similarity1
    Modified residuei171N6-acetyllysine; alternateBy similarity1
    Modified residuei171N6-succinyllysine; alternateBy similarity1
    Modified residuei191N6-acetyllysine; alternateBy similarity1
    Modified residuei191N6-succinyllysine; alternateBy similarity1
    Modified residuei209N6-acetyllysine; alternateBy similarity1
    Modified residuei209N6-succinyllysine; alternateBy similarity1
    Modified residuei211N6-succinyllysineBy similarity1
    Modified residuei212N6-succinyllysineBy similarity1
    Modified residuei214N6-succinyllysineBy similarity1
    Modified residuei240N6-succinyllysineBy similarity1
    Modified residuei241N6-acetyllysineBy similarity1
    Modified residuei269N6-acetyllysineBy similarity1
    Modified residuei270N6-acetyllysineBy similarity1
    Modified residuei305N6-acetyllysine; alternateBy similarity1
    Modified residuei305N6-succinyllysine; alternateBy similarity1
    Modified residuei310PhosphoserineBy similarity1
    Modified residuei312N6-acetyllysine; alternateBy similarity1
    Modified residuei312N6-succinyllysine; alternateBy similarity1
    Modified residuei333PhosphoserineBy similarity1
    Modified residuei340N6-acetyllysineBy similarity1
    Modified residuei344PhosphoserineBy similarity1
    Modified residuei375N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P13437

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P13437

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P13437

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P13437

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P13437

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P13437

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in liver, brown adipose tissue and heart (at protein level).1 Publication

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated in liver, brown adipose tissue, heart, intestine and kidney by DEHP/bis(2-ethylhexyl)phthalate (at protein level).1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.

    Interacts with BNIP3 (By similarity).

    By similarity

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    250910, 1 interactor

    Protein interaction database and analysis system

    More...
    IntActi
    P13437, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000060140

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P13437

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1391 Eukaryota
    COG0183 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P13437

    KEGG Orthology (KO)

    More...
    KOi
    K07508

    Database of Orthologous Groups

    More...
    OrthoDBi
    1129049at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P13437

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00751 thiolase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.47.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000429 Ac-CoA_Ac_transf, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53901 SSF53901, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01930 AcCoA-C-Actrans, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P13437-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MALLRGVFIV AAKRTPFGAY GGLLKDFTAT DLTEFAARAA LSAGKVPPET
    60 70 80 90 100
    IDSVIVGNVM QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV
    110 120 130 140 150
    SGCQEICSKD AEVVLCGGTE SMSQSPYSVR NVRFGTKFGL DLKLEDTLWA
    160 170 180 190 200
    GLTDQHVKLP MGMTAENLAA KYNISREDCD RYALQSQQRW KAANEAGYFN
    210 220 230 240 250
    EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQNLPPVFK KEGTVTAGNA
    260 270 280 290 300
    SGMSDGAGVV IIASEDAVKK HNFTPLARVV GYFVSGCDPA IMGIGPVPAI
    310 320 330 340 350
    TGALKKAGLS LKDMDLIDVN EAFAPQFLAV QKSLDLDPSK TNVSGGAIAL
    360 370 380 390
    GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIS LIIQNTA
    Length:397
    Mass (Da):41,871
    Last modified:January 1, 1990 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8344FB7271C3E2E1
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    G3V9U2G3V9U2_RAT
    3-ketoacyl-CoA thiolase, mitochondr...
    Acaa2 rCG_41706
    397Annotation score:

    Annotation score:2 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A0G2K642A0A0G2K642_RAT
    3-ketoacyl-CoA thiolase, mitochondr...
    Acaa2
    396Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X05341 mRNA Translation: CAA28952.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A29452 XURT

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_569117.1, NM_130433.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    170465

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:170465

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05341 mRNA Translation: CAA28952.1
    PIRiA29452 XURT
    RefSeqiNP_569117.1, NM_130433.1

    3D structure databases

    SMRiP13437
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi250910, 1 interactor
    IntActiP13437, 2 interactors
    STRINGi10116.ENSRNOP00000060140

    Chemistry databases

    SwissLipidsiSLP:000001412

    PTM databases

    CarbonylDBiP13437
    iPTMnetiP13437
    PhosphoSitePlusiP13437

    Proteomic databases

    jPOSTiP13437
    PaxDbiP13437
    PRIDEiP13437

    Genome annotation databases

    GeneIDi170465
    KEGGirno:170465

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    10449
    RGDi620482 Acaa2

    Phylogenomic databases

    eggNOGiKOG1391 Eukaryota
    COG0183 LUCA
    InParanoidiP13437
    KOiK07508
    OrthoDBi1129049at2759
    PhylomeDBiP13437

    Enzyme and pathway databases

    UniPathwayiUPA00659
    ReactomeiR-RNO-77289 Mitochondrial Fatty Acid Beta-Oxidation
    SABIO-RKiP13437

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P13437

    Family and domain databases

    CDDicd00751 thiolase, 1 hit
    Gene3Di3.40.47.10, 2 hits
    InterProiView protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N
    PfamiView protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit
    PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
    SUPFAMiSSF53901 SSF53901, 2 hits
    TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
    PROSITEiView protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTHIM_RAT
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13437
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: June 17, 2020
    This is version 141 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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