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O14734

- ACOT8_HUMAN

UniProt

O14734 - ACOT8_HUMAN

Protein

Acyl-coenzyme A thioesterase 8

Gene

ACOT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs By similarity. May be involved in the metabolic regulation of peroxisome proliferation.By similarity1 Publication

    Catalytic activityi

    Choloyl-CoA + H2O = cholate + CoA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321Charge relay systemBy similarity
    Active sitei254 – 2541Charge relay systemBy similarity
    Active sitei304 – 3041Charge relay systemBy similarity

    GO - Molecular functioni

    1. acyl-CoA hydrolase activity Source: UniProtKB
    2. choloyl-CoA hydrolase activity Source: UniProtKB-EC
    3. medium-chain acyl-CoA hydrolase activity Source: UniProtKB
    4. palmitoyl-CoA hydrolase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. receptor binding Source: UniProtKB

    GO - Biological processi

    1. acyl-CoA metabolic process Source: UniProtKB
    2. alpha-linolenic acid metabolic process Source: Reactome
    3. bile acid biosynthetic process Source: Reactome
    4. bile acid metabolic process Source: Reactome
    5. cellular lipid metabolic process Source: Reactome
    6. dicarboxylic acid catabolic process Source: UniProtKB
    7. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
    8. peroxisome fission Source: UniProtKB
    9. small molecule metabolic process Source: Reactome
    10. unsaturated fatty acid metabolic process Source: Reactome
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Host-virus interaction, Peroxisome biogenesis

    Enzyme and pathway databases

    BRENDAi3.1.2.2. 2681.
    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17017. Beta-oxidation of pristanoyl-CoA.
    REACT_17062. Beta-oxidation of very long chain fatty acids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 8 (EC:3.1.2.27)
    Short name:
    Acyl-CoA thioesterase 8
    Alternative name(s):
    Choloyl-coenzyme A thioesterase
    HIV-Nef-associated acyl-CoA thioesterase
    PTE-2
    Peroxisomal acyl-coenzyme A thioester hydrolase 1
    Short name:
    PTE-1
    Peroxisomal long-chain acyl-CoA thioesterase 1
    Thioesterase II
    Short name:
    hACTE-III
    Short name:
    hACTEIII
    Short name:
    hTE
    Gene namesi
    Name:ACOT8
    Synonyms:ACTEIII, PTE1, PTE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15919. ACOT8.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. peroxisomal matrix Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33941.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 319319Acyl-coenzyme A thioesterase 8PRO_0000202152Add
    BLAST

    Proteomic databases

    MaxQBiO14734.
    PaxDbiO14734.
    PRIDEiO14734.

    PTM databases

    PhosphoSiteiO14734.

    Expressioni

    Tissue specificityi

    Detected in a T-cell line (at protein level). Ubiquitous.1 Publication

    Inductioni

    Regulated by peroxisome proliferator (such as Clofibrate), via the peroxisome proliferator-activated receptors (PPARs).By similarity

    Gene expression databases

    ArrayExpressiO14734.
    BgeeiO14734.
    CleanExiHS_ACOT8.
    GenevestigatoriO14734.

    Organism-specific databases

    HPAiCAB010261.

    Interactioni

    Subunit structurei

    Interacts with HIV-1 Nef.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nefP046015EBI-1237371,EBI-6164028From a different organism.

    Protein-protein interaction databases

    BioGridi115323. 9 interactions.
    IntActiO14734. 5 interactions.
    MINTiMINT-2998229.
    STRINGi9606.ENSP00000217455.

    Structurei

    3D structure databases

    ProteinModelPortaliO14734.
    SMRiO14734. Positions 37-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi317 – 3193Microbody targeting signalSequence Analysis

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1946.
    HOGENOMiHOG000246495.
    HOVERGENiHBG019167.
    InParanoidiO14734.
    KOiK11992.
    OMAiHAYFLLI.
    OrthoDBiEOG7VTDNQ.
    PhylomeDBiO14734.
    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.

    O14734-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP    50
    AKRLFGGQIV GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER 100
    TRTGSSFSVR SVKAVQHGKP IFICQASFQQ AQPSPMQHQF SMPTVPPPEE 150
    LLDCETLIDQ YLRDPNLQKR YPLALNRIAA QEVPIEIKPV NPSPLSQLQR 200
    MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL LPHQWQHKVH 250
    FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV 300
    TCAQEGVIRV KPQVSESKL 319
    Length:319
    Mass (Da):35,914
    Last modified:January 1, 1998 - v1
    Checksum:i8345C6E5EABF3326
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2933LWR → VWS in CAA60024. (PubMed:9153233)Curated
    Sequence conflicti319 – 3191L → R in CAA60024. (PubMed:9153233)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF014404 mRNA. Translation: AAB71665.1.
    X86032 mRNA. Translation: CAA60024.1.
    AF124264 mRNA. Translation: AAD27616.1.
    AL008726 Genomic DNA. Translation: CAA15502.1.
    BC117155 mRNA. Translation: AAI17156.1.
    BC117157 mRNA. Translation: AAI17158.1.
    CCDSiCCDS13378.1.
    PIRiJC5644.
    RefSeqiNP_005460.2. NM_005469.3.
    UniGeneiHs.444776.

    Genome annotation databases

    EnsembliENST00000217455; ENSP00000217455; ENSG00000101473.
    GeneIDi10005.
    KEGGihsa:10005.
    UCSCiuc002xqa.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF014404 mRNA. Translation: AAB71665.1 .
    X86032 mRNA. Translation: CAA60024.1 .
    AF124264 mRNA. Translation: AAD27616.1 .
    AL008726 Genomic DNA. Translation: CAA15502.1 .
    BC117155 mRNA. Translation: AAI17156.1 .
    BC117157 mRNA. Translation: AAI17158.1 .
    CCDSi CCDS13378.1.
    PIRi JC5644.
    RefSeqi NP_005460.2. NM_005469.3.
    UniGenei Hs.444776.

    3D structure databases

    ProteinModelPortali O14734.
    SMRi O14734. Positions 37-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115323. 9 interactions.
    IntActi O14734. 5 interactions.
    MINTi MINT-2998229.
    STRINGi 9606.ENSP00000217455.

    PTM databases

    PhosphoSitei O14734.

    Proteomic databases

    MaxQBi O14734.
    PaxDbi O14734.
    PRIDEi O14734.

    Protocols and materials databases

    DNASUi 10005.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217455 ; ENSP00000217455 ; ENSG00000101473 .
    GeneIDi 10005.
    KEGGi hsa:10005.
    UCSCi uc002xqa.2. human.

    Organism-specific databases

    CTDi 10005.
    GeneCardsi GC20M044470.
    HGNCi HGNC:15919. ACOT8.
    HPAi CAB010261.
    MIMi 608123. gene.
    neXtProti NX_O14734.
    PharmGKBi PA33941.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1946.
    HOGENOMi HOG000246495.
    HOVERGENi HBG019167.
    InParanoidi O14734.
    KOi K11992.
    OMAi HAYFLLI.
    OrthoDBi EOG7VTDNQ.
    PhylomeDBi O14734.
    TreeFami TF315124.

    Enzyme and pathway databases

    BRENDAi 3.1.2.2. 2681.
    Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17017. Beta-oxidation of pristanoyl-CoA.
    REACT_17062. Beta-oxidation of very long chain fatty acids.

    Miscellaneous databases

    GeneWikii ACOT8.
    GenomeRNAii 10005.
    NextBioi 37789.
    PROi O14734.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14734.
    Bgeei O14734.
    CleanExi HS_ACOT8.
    Genevestigatori O14734.

    Family and domain databases

    Gene3Di 3.10.129.10. 2 hits.
    InterProi IPR003703. Acyl_CoA_thio.
    IPR029069. HotDog_dom.
    [Graphical view ]
    PANTHERi PTHR11066. PTHR11066. 1 hit.
    SUPFAMi SSF54637. SSF54637. 2 hits.
    TIGRFAMsi TIGR00189. tesB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef."
      Watanabe H., Shiratori T., Shoji H., Miyatake S., Okazaki Y., Ikuta K., Sato T., Saito T.
      Biochem. Biophys. Res. Commun. 238:234-239(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HIV-1 NEF, TISSUE SPECIFICITY.
    2. "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation."
      Liu L.X., Margottin F., Le Gall S., Schwartz O., Selig L., Benarous R., Benichou S.
      J. Biol. Chem. 272:13779-13785(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphoid tissue.
    3. "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans."
      Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.
      J. Biol. Chem. 274:9216-9223(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Muscle.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis."
      Ishizuka M., Toyama Y., Watanabe H., Fujiki Y., Takeuchi A., Yamasaki S., Yuasa S., Miyazaki M., Nakajima N., Taki S., Saito T.
      Exp. Cell Res. 297:127-141(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism."
      Hunt M.C., Alexson S.E.H.
      Prog. Lipid Res. 41:99-130(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACOT8_HUMAN
    AccessioniPrimary (citable) accession number: O14734
    Secondary accession number(s): O15261, Q17RX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 136 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3