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Protein

Acyl-coenzyme A thioesterase 13

Gene

ACOT13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity).By similarity2 Publications

Kineticsi

  1. KM=4.9 µM for n-decanoyl-CoA1 Publication
  2. KM=26 µM for n-octanoyl-CoA1 Publication
  3. KM=5 µM for myristoyl-CoA1 Publication
  4. KM=9 µM for palmitoyl-CoA1 Publication
  5. KM=9 µM for oleoyl-CoA1 Publication
  6. KM=10 µM for 3,4-dihydroxyphenylacetyl-CoA1 Publication
  7. KM=40 µM for 3-hydroxyphenylacetyl-CoA1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei50Substrate1

    GO - Molecular functioni

    • acyl-CoA hydrolase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000112304-MONOMER.
    BRENDAi3.1.2.20. 2681.
    ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.
    SABIO-RKQ9NPJ3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 13 (EC:3.1.2.-)
    Short name:
    Acyl-CoA thioesterase 13
    Alternative name(s):
    Thioesterase superfamily member 2
    Cleaved into the following chain:
    Gene namesi
    Name:ACOT13
    Synonyms:THEM2
    ORF Names:HT012, PNAS-27
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20999. ACOT13.

    Subcellular locationi

    • Cytoplasmcytosol By similarity
    • Mitochondrion By similarity
    • Nucleus By similarity
    • Cytoplasmcytoskeletonspindle By similarity

    • Note: During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin.By similarity

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: UniProtKB-SubCell
    • nucleus Source: UniProtKB
    • spindle Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi50N → A: Reduced activity. 1 Publication1
    Mutagenesisi56H → A: Decreases affinity for substrate. 1 Publication1
    Mutagenesisi65D → A: Loss of activity. 2 Publications1
    Mutagenesisi65D → E or N: Reduced activity. 2 Publications1
    Mutagenesisi83S → A: Reduced activity. 1 Publication1

    Organism-specific databases

    DisGeNETi55856.
    OpenTargetsiENSG00000112304.
    PharmGKBiPA165617655.

    Polymorphism and mutation databases

    BioMutaiACOT13.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001566971 – 140Acyl-coenzyme A thioesterase 13Add BLAST140
    Initiator methionineiRemoved; alternateCombined sources
    ChainiPRO_00004245012 – 140Acyl-coenzyme A thioesterase 13, N-terminally processedAdd BLAST139

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylmethionineCombined sources1
    Modified residuei2N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processedCombined sources1
    Modified residuei27N6-acetyllysineBy similarity1
    Modified residuei37N6-acetyllysineBy similarity1
    Modified residuei43N6-acetyllysineBy similarity1
    Modified residuei108N6-acetyllysineBy similarity1
    Modified residuei127N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ9NPJ3.
    MaxQBiQ9NPJ3.
    PaxDbiQ9NPJ3.
    PeptideAtlasiQ9NPJ3.
    PRIDEiQ9NPJ3.
    TopDownProteomicsiQ9NPJ3-1. [Q9NPJ3-1]

    PTM databases

    iPTMnetiQ9NPJ3.
    PhosphoSitePlusiQ9NPJ3.

    Expressioni

    Gene expression databases

    BgeeiENSG00000112304.
    CleanExiHS_THEM2.
    GenevisibleiQ9NPJ3. HS.

    Organism-specific databases

    HPAiHPA019881.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi120958. 24 interactors.
    IntActiQ9NPJ3. 6 interactors.
    STRINGi9606.ENSP00000230048.

    Structurei

    Secondary structure

    1140
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 15Combined sources13
    Beta strandi18 – 20Combined sources3
    Helixi21 – 25Combined sources5
    Beta strandi29 – 34Combined sources6
    Beta strandi37 – 43Combined sources7
    Helixi46 – 48Combined sources3
    Beta strandi53 – 55Combined sources3
    Helixi57 – 73Combined sources17
    Beta strandi75 – 77Combined sources3
    Beta strandi82 – 90Combined sources9
    Beta strandi99 – 109Combined sources11
    Beta strandi111 – 122Combined sources12
    Turni123 – 125Combined sources3
    Beta strandi128 – 137Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2F0XX-ray2.30A/B/C/D/E/F/G/H1-140[»]
    2H4UX-ray2.20A/B/C/D19-140[»]
    3F5OX-ray1.70A/B/C/D/E/F/G/H1-140[»]
    ProteinModelPortaliQ9NPJ3.
    SMRiQ9NPJ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPJ3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.Curated

    Phylogenomic databases

    eggNOGiKOG3328. Eukaryota.
    COG2050. LUCA.
    GeneTreeiENSGT00390000013934.
    HOGENOMiHOG000170540.
    InParanoidiQ9NPJ3.
    KOiK17362.
    OMAiKVICEMK.
    OrthoDBiEOG091G125K.
    PhylomeDBiQ9NPJ3.
    TreeFamiTF315062.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NPJ3-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN
    60 70 80 90 100
    AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI
    110 120 130 140
    VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN
    Length:140
    Mass (Da):14,960
    Last modified:October 1, 2000 - v1
    Checksum:i084E36EFEE715A18
    GO
    Isoform 2 (identifier: Q9NPJ3-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MTSMTQSLREVIKAMTKARNFERVLG → MVR

    Note: No experimental confirmation available.
    Show »
    Length:117
    Mass (Da):12,366
    Checksum:iA6F50AA63A00583A
    GO

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0461011 – 26MTSMT…ERVLG → MVR in isoform 2. 1 PublicationAdd BLAST26

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF155649 mRNA. Translation: AAF67006.1.
    AF220186 mRNA. Translation: AAF67651.1.
    AF274952 mRNA. Translation: AAK07529.1.
    AK000508 mRNA. Translation: BAA91215.1.
    AK309738 mRNA. No translation available.
    AL031775 Genomic DNA. Translation: CAD92509.1.
    BC000894 mRNA. Translation: AAH00894.1.
    CCDSiCCDS4558.1. [Q9NPJ3-1]
    CCDS54972.1. [Q9NPJ3-2]
    RefSeqiNP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
    NP_060943.1. NM_018473.3. [Q9NPJ3-1]
    UniGeneiHs.731605.

    Genome annotation databases

    EnsembliENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1]
    ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
    GeneIDi55856.
    KEGGihsa:55856.
    UCSCiuc003nek.4. human. [Q9NPJ3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF155649 mRNA. Translation: AAF67006.1.
    AF220186 mRNA. Translation: AAF67651.1.
    AF274952 mRNA. Translation: AAK07529.1.
    AK000508 mRNA. Translation: BAA91215.1.
    AK309738 mRNA. No translation available.
    AL031775 Genomic DNA. Translation: CAD92509.1.
    BC000894 mRNA. Translation: AAH00894.1.
    CCDSiCCDS4558.1. [Q9NPJ3-1]
    CCDS54972.1. [Q9NPJ3-2]
    RefSeqiNP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
    NP_060943.1. NM_018473.3. [Q9NPJ3-1]
    UniGeneiHs.731605.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2F0XX-ray2.30A/B/C/D/E/F/G/H1-140[»]
    2H4UX-ray2.20A/B/C/D19-140[»]
    3F5OX-ray1.70A/B/C/D/E/F/G/H1-140[»]
    ProteinModelPortaliQ9NPJ3.
    SMRiQ9NPJ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi120958. 24 interactors.
    IntActiQ9NPJ3. 6 interactors.
    STRINGi9606.ENSP00000230048.

    PTM databases

    iPTMnetiQ9NPJ3.
    PhosphoSitePlusiQ9NPJ3.

    Polymorphism and mutation databases

    BioMutaiACOT13.

    Proteomic databases

    EPDiQ9NPJ3.
    MaxQBiQ9NPJ3.
    PaxDbiQ9NPJ3.
    PeptideAtlasiQ9NPJ3.
    PRIDEiQ9NPJ3.
    TopDownProteomicsiQ9NPJ3-1. [Q9NPJ3-1]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1]
    ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
    GeneIDi55856.
    KEGGihsa:55856.
    UCSCiuc003nek.4. human. [Q9NPJ3-1]

    Organism-specific databases

    CTDi55856.
    DisGeNETi55856.
    GeneCardsiACOT13.
    H-InvDBHIX0005627.
    HGNCiHGNC:20999. ACOT13.
    HPAiHPA019881.
    MIMi615652. gene.
    neXtProtiNX_Q9NPJ3.
    OpenTargetsiENSG00000112304.
    PharmGKBiPA165617655.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3328. Eukaryota.
    COG2050. LUCA.
    GeneTreeiENSGT00390000013934.
    HOGENOMiHOG000170540.
    InParanoidiQ9NPJ3.
    KOiK17362.
    OMAiKVICEMK.
    OrthoDBiEOG091G125K.
    PhylomeDBiQ9NPJ3.
    TreeFamiTF315062.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000112304-MONOMER.
    BRENDAi3.1.2.20. 2681.
    ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.
    SABIO-RKQ9NPJ3.

    Miscellaneous databases

    ChiTaRSiACOT13. human.
    EvolutionaryTraceiQ9NPJ3.
    GenomeRNAii55856.
    PROiQ9NPJ3.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000112304.
    CleanExiHS_THEM2.
    GenevisibleiQ9NPJ3. HS.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACO13_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPJ3
    Secondary accession number(s): F5H2L4, O95549
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: October 1, 2000
    Last modified: November 30, 2016
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.