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Protein

Acyl-coenzyme A thioesterase 8

Gene

Acot8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-coenzyme A (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 (PubMed:11673457). Competes with bile acid CoA:amino acid N-acyltransferase (BAAT) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA) (PubMed:11673457). Shows a preference for medium-length fatty acyl-CoAs (C2 to C20) (PubMed:11673457). Catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA (PubMed:11673457). May be involved in the metabolic regulation of peroxisome proliferation (By similarity).By similarity1 Publication

Catalytic activityi

Choloyl-CoA + H2O = cholate + CoA.1 Publication

Enzyme regulationi

Inhibited by CoASH (IC50=10-15 µM). Also inhibited by cysteine-reactive agents.1 Publication

Kineticsi

In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 µM, and with short-chain acyl CoAs range from 8 to 30 µM. KM for bile acid-CoA esters is in the range 6-15 µM.1 Publication

Manual assertion based on experiment ini

  1. KM=29.4 µM for acetyl-CoA1 Publication
  2. KM=8.0 µM for propionyl-CoA1 Publication
  3. KM=22.6 µM for butyryl-CoA1 Publication
  4. KM=23.4 µM for hexanoyl-CoA1 Publication
  5. KM=6.9 µM for octanoyl-CoA1 Publication
  6. KM=2.9 µM for decanoyl-CoA1 Publication
  7. KM=2.5 µM for myristoyl-CoA1 Publication
  8. KM=1.7 µM for palmitoyl-CoA1 Publication
  9. KM=1.4 µM for palmitoleoyl-CoA1 Publication
  10. KM=1.6 µM for oleoyl-CoA1 Publication
  11. KM=4.2 µM for arachidoyl-CoA1 Publication
  12. KM=6.7 µM for arachidonoyl-CoA1 Publication
  13. KM=6.3 µM for trihydroxycoprostanoyl-CoA1 Publication
  14. KM=14.6 µM for choloyl-CoA1 Publication
  15. KM=8.8 µM for chenodeoxycholoyl-CoA1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei233Charge relay systemBy similarity1
    Active sitei255Charge relay systemBy similarity1
    Active sitei305Charge relay systemBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Peroxisome biogenesis

    Enzyme and pathway databases

    BRENDAi3.1.2.2. 3474.
    3.1.2.20. 3474.
    3.1.2.27. 3474.
    ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
    R-MMU-389887. Beta-oxidation of pristanoyl-CoA.
    R-MMU-390247. Beta-oxidation of very long chain fatty acids.
    R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

    Chemistry databases

    SwissLipidsiSLP:000000534.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 8 (EC:3.1.2.271 Publication)
    Short name:
    Acyl-CoA thioesterase 8
    Alternative name(s):
    Choloyl-coenzyme A thioesterase
    Peroxisomal acyl-CoA thioesterase 2
    Short name:
    PTE-2
    Peroxisomal acyl-coenzyme A thioester hydrolase 1
    Short name:
    PTE-1
    Peroxisomal long-chain acyl-CoA thioesterase 1
    Gene namesi
    Name:Acot8
    Synonyms:Pte1, Pte2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 2

    Organism-specific databases

    MGIiMGI:2158201. Acot8.

    Subcellular locationi

    • Cytoplasm By similarity
    • Peroxisome matrix 1 Publication

    • Note: Predominantly localized in the peroxisome (PubMed:11673457).1 Publication

    GO - Cellular componenti

    • mitochondrion Source: MGI
    • peroxisomal matrix Source: MGI
    • peroxisome Source: HGNC
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002021531 – 320Acyl-coenzyme A thioesterase 8Add BLAST320

    Proteomic databases

    EPDiP58137.
    PaxDbiP58137.
    PeptideAtlasiP58137.
    PRIDEiP58137.

    PTM databases

    iPTMnetiP58137.
    PhosphoSitePlusiP58137.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    Induced in the liver, by peroxisome proliferator or fasting via the peroxisome proliferator-activated receptors (PPARs). Diurnal regulation of its expression.1 Publication

    Gene expression databases

    BgeeiENSMUSG00000017307.
    CleanExiMM_ACOT8.
    ExpressionAtlasiP58137. baseline and differential.
    GenevisibleiP58137. MM.

    Interactioni

    Subunit structurei

    homodimer.1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    IntActiP58137. 1 interactor.
    MINTiMINT-1850038.
    STRINGi10090.ENSMUSP00000099383.

    Structurei

    3D structure databases

    ProteinModelPortaliP58137.
    SMRiP58137.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi318 – 320Microbody targeting signalSequence analysis3

    Sequence similaritiesi

    Belongs to the C/M/P thioester hydrolase family.Curated

    Phylogenomic databases

    eggNOGiKOG3016. Eukaryota.
    COG1946. LUCA.
    GeneTreeiENSGT00390000004207.
    HOGENOMiHOG000246495.
    HOVERGENiHBG019167.
    InParanoidiP58137.
    KOiK11992.
    OMAiPIFTCSA.
    OrthoDBiEOG091G0BLB.
    PhylomeDBiP58137.
    TreeFamiTF315124.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    InterProiIPR003703. Acyl_CoA_thio.
    IPR029069. HotDog_dom.
    [Graphical view]
    PANTHERiPTHR11066. PTHR11066. 1 hit.
    SUPFAMiSSF54637. SSF54637. 2 hits.
    TIGRFAMsiTIGR00189. tesB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P58137-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAPEGLGDA HGDADRGDLS GDLRSVLVTS VLNLEPLDED LYRGRHYWVP
    60 70 80 90 100
    TSQRLFGGQI MGQALVAAAK SVSEDVHVHS LHCYFVRAGD PKVPVLYHVE
    110 120 130 140 150
    RIRTGASFSV RAVKAVQHGK AIFICQASFQ QMQPSPLQHQ FSMPSVPPPE
    160 170 180 190 200
    DLLDHEALID QYLRDPNLHK KYRVGLNRVA AQEVPIEIKV VNPPTLTQLQ
    210 220 230 240 250
    ALEPKQMFWV RARGYIGEGD IKMHCCVAAY ISDYAFLGTA LLPHQSKYKV
    260 270 280 290 300
    NFMASLDHSM WFHAPFRADH WMLYECESPW AGGSRGLVHG RLWRRDGVLA
    310 320
    VTCAQEGVIR LKPQVSESKL
    Length:320
    Mass (Da):35,827
    Last modified:June 1, 2001 - v1
    Checksum:i94F6AFCFEEE2FA23
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti284S → F in AAL35333 (PubMed:11673457).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF441166 mRNA. Translation: AAL35333.1.
    BC005792 mRNA. Translation: AAH05792.1.
    CCDSiCCDS17057.1.
    RefSeqiNP_573503.2. NM_133240.2.
    UniGeneiMm.277878.

    Genome annotation databases

    EnsembliENSMUST00000103094; ENSMUSP00000099383; ENSMUSG00000017307.
    GeneIDi170789.
    KEGGimmu:170789.
    UCSCiuc008nwf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF441166 mRNA. Translation: AAL35333.1.
    BC005792 mRNA. Translation: AAH05792.1.
    CCDSiCCDS17057.1.
    RefSeqiNP_573503.2. NM_133240.2.
    UniGeneiMm.277878.

    3D structure databases

    ProteinModelPortaliP58137.
    SMRiP58137.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP58137. 1 interactor.
    MINTiMINT-1850038.
    STRINGi10090.ENSMUSP00000099383.

    Chemistry databases

    SwissLipidsiSLP:000000534.

    PTM databases

    iPTMnetiP58137.
    PhosphoSitePlusiP58137.

    Proteomic databases

    EPDiP58137.
    PaxDbiP58137.
    PeptideAtlasiP58137.
    PRIDEiP58137.

    Protocols and materials databases

    DNASUi170789.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000103094; ENSMUSP00000099383; ENSMUSG00000017307.
    GeneIDi170789.
    KEGGimmu:170789.
    UCSCiuc008nwf.2. mouse.

    Organism-specific databases

    CTDi10005.
    MGIiMGI:2158201. Acot8.

    Phylogenomic databases

    eggNOGiKOG3016. Eukaryota.
    COG1946. LUCA.
    GeneTreeiENSGT00390000004207.
    HOGENOMiHOG000246495.
    HOVERGENiHBG019167.
    InParanoidiP58137.
    KOiK11992.
    OMAiPIFTCSA.
    OrthoDBiEOG091G0BLB.
    PhylomeDBiP58137.
    TreeFamiTF315124.

    Enzyme and pathway databases

    BRENDAi3.1.2.2. 3474.
    3.1.2.20. 3474.
    3.1.2.27. 3474.
    ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
    R-MMU-389887. Beta-oxidation of pristanoyl-CoA.
    R-MMU-390247. Beta-oxidation of very long chain fatty acids.
    R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

    Miscellaneous databases

    PROiP58137.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000017307.
    CleanExiMM_ACOT8.
    ExpressionAtlasiP58137. baseline and differential.
    GenevisibleiP58137. MM.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    InterProiIPR003703. Acyl_CoA_thio.
    IPR029069. HotDog_dom.
    [Graphical view]
    PANTHERiPTHR11066. PTHR11066. 1 hit.
    SUPFAMiSSF54637. SSF54637. 2 hits.
    TIGRFAMsiTIGR00189. tesB. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACOT8_MOUSE
    AccessioniPrimary (citable) accession number: P58137
    Secondary accession number(s): Q8VHM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: June 1, 2001
    Last modified: November 2, 2016
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Constitutes about 1% of total peroxisomal protein.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. 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.