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Q86TX2

- ACOT1_HUMAN

UniProt

Q86TX2 - ACOT1_HUMAN

Protein

Acyl-coenzyme A thioesterase 1

Gene

ACOT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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. Active towards fatty acyl-CoA with chain-lengths of C12-C16 By similarity.By similarity

    Catalytic activityi

    Palmitoyl-CoA + H2O = CoA + palmitate.

    Kineticsi

    1. KM=35.8 µM for C10-acyl-CoA1 Publication
    2. KM=3.6 µM for C12-acyl-CoA1 Publication
    3. KM=2.8 µM for C14-acyl-CoA1 Publication
    4. KM=3.6 µM for C16-acyl-CoA1 Publication
    5. KM=2.4 µM for C18-acyl-CoA1 Publication
    6. KM=2 µM for C20-acyl-CoA1 Publication
    7. KM=2.4 µM for C16:1-acyl-CoA1 Publication
    8. KM=4.1 µM for C18:1-acyl-CoA1 Publication
    9. KM=2.1 µM for C18:1-trans-acyl-CoA1 Publication

    Vmax=224 nmol/min/mg enzyme toward C10-acyl-CoA1 Publication

    Vmax=700 nmol/min/mg enzyme toward C12-acyl-CoA1 Publication

    Vmax=912 nmol/min/mg enzyme toward C14-acyl-CoA1 Publication

    Vmax=691 nmol/min/mg enzyme toward C16-acyl-CoA1 Publication

    Vmax=597 nmol/min/mg enzyme toward C18-acyl-CoA1 Publication

    Vmax=520 nmol/min/mg enzyme toward C20-acyl-CoA1 Publication

    Vmax=577 nmol/min/mg enzyme toward C16:1-acyl-CoA1 Publication

    Vmax=258 nmol/min/mg enzyme toward C18:1-acyl-CoA1 Publication

    Vmax=309 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321Charge relay systemBy similarity
    Active sitei326 – 3261Charge relay systemBy similarity
    Active sitei360 – 3601Charge relay systemBy similarity

    GO - Molecular functioni

    1. acyl-CoA hydrolase activity Source: HGNC
    2. palmitoyl-CoA hydrolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. acyl-CoA metabolic process Source: HGNC
    2. long-chain fatty acid metabolic process Source: HGNC
    3. very long-chain fatty acid metabolic process Source: HGNC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14105.
    BRENDAi3.1.2.2. 2681.
    SABIO-RKQ86TX2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 1 (EC:3.1.2.2)
    Short name:
    Acyl-CoA thioesterase 1
    Alternative name(s):
    CTE-I
    CTE-Ib
    Inducible cytosolic acyl-coenzyme A thioester hydrolase
    Long chain acyl-CoA thioester hydrolase
    Short name:
    Long chain acyl-CoA hydrolase
    Gene namesi
    Name:ACOT1
    Synonyms:CTE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:33128. ACOT1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162375318.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 421420Acyl-coenzyme A thioesterase 1PRO_0000202155Add
    BLAST

    Proteomic databases

    MaxQBiQ86TX2.
    PaxDbiQ86TX2.
    PRIDEiQ86TX2.

    2D gel databases

    UCD-2DPAGEQ86TX2.

    PTM databases

    PhosphoSiteiQ86TX2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ86TX2.
    BgeeiQ86TX2.
    CleanExiHS_ACOT1.
    GenevestigatoriQ86TX2.

    Organism-specific databases

    HPAiHPA043705.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi534965. 5 interactions.
    STRINGi9606.ENSP00000311224.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86TX2.
    SMRiQ86TX2. Positions 1-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1073.
    HOGENOMiHOG000116219.
    HOVERGENiHBG000331.
    InParanoidiQ86TX2.
    KOiK01068.
    OMAiIPWHWIP.
    OrthoDBiEOG75TMC9.
    PhylomeDBiQ86TX2.
    TreeFamiTF314911.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR016662. Acyl-CoA_thioEstase_long-chain.
    IPR014940. BAAT_C.
    IPR006862. Thio_Ohase/aa_AcTrfase.
    [Graphical view]
    PfamiPF08840. BAAT_C. 1 hit.
    PF04775. Bile_Hydr_Trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
    SUPFAMiSSF53474. SSF53474. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    Q86TX2-1 [UniParc]FASTAAdd to Basket

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    MAATLILEPA GRCCWDEPVR IAVRGLAPEQ PVTLRASLRD EKGALFQAHA    50
    RYRADTLGEL DLERAPALGG SFAGLEPMGL LWALEPEKPL VRLVKRDVRT 100
    PLAVELEVLD GHDPDPGRLL CRVRHERYFL PPGVRREPVR AGRVRGTLFL 150
    PPEPGPFPGI VDMFGTGGGL LEYRASLLAG KGFAVMALAY YNYEDLPKTM 200
    ETLHLEYFEE AVNYLLSHPE VKGPGVGLLG ISKGGELCLS MASFLKGITA 250
    AVVINGSVAN VGGTLRYKGE TLPPVGVNRN RIKVTKDGYA DIVDVLNSPL 300
    EGPDQKSFIP VERAESTFLF LVGQDDHNWK SEFYANEACK RLQAHGRRKP 350
    QIICYPETGH YIEPPYFPLC RASLHALVGS PIIWGGEPRA HAMAQVDAWK 400
    QLQTFFHKHL GGHEGTIPSK V 421
    Length:421
    Mass (Da):46,277
    Last modified:June 1, 2003 - v1
    Checksum:i04675F28D9D53B97
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti266 – 2661R → H.
    Corresponds to variant rs1049568 [ dbSNP | Ensembl ].
    VAR_059830

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ082754 mRNA. Translation: AAZ31236.1.
    BX161396 mRNA. Translation: CAD61883.1.
    BC127748 mRNA. Translation: AAI27749.1.
    BC132889 mRNA. Translation: AAI32890.1.
    BC132891 mRNA. Translation: AAI32892.1.
    BC143042 mRNA. Translation: AAI43043.1.
    CCDSiCCDS32117.1.
    RefSeqiNP_001032238.1. NM_001037161.1.
    UniGeneiHs.446685.
    Hs.568046.

    Genome annotation databases

    EnsembliENST00000311148; ENSP00000311224; ENSG00000184227.
    GeneIDi641371.
    KEGGihsa:641371.
    UCSCiuc001xol.1. human.

    Polymorphism databases

    DMDMi50428913.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ082754 mRNA. Translation: AAZ31236.1 .
    BX161396 mRNA. Translation: CAD61883.1 .
    BC127748 mRNA. Translation: AAI27749.1 .
    BC132889 mRNA. Translation: AAI32890.1 .
    BC132891 mRNA. Translation: AAI32892.1 .
    BC143042 mRNA. Translation: AAI43043.1 .
    CCDSi CCDS32117.1.
    RefSeqi NP_001032238.1. NM_001037161.1.
    UniGenei Hs.446685.
    Hs.568046.

    3D structure databases

    ProteinModelPortali Q86TX2.
    SMRi Q86TX2. Positions 1-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 534965. 5 interactions.
    STRINGi 9606.ENSP00000311224.

    Chemistry

    ChEMBLi CHEMBL2189136.

    PTM databases

    PhosphoSitei Q86TX2.

    Polymorphism databases

    DMDMi 50428913.

    2D gel databases

    UCD-2DPAGE Q86TX2.

    Proteomic databases

    MaxQBi Q86TX2.
    PaxDbi Q86TX2.
    PRIDEi Q86TX2.

    Protocols and materials databases

    DNASUi 641371.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311148 ; ENSP00000311224 ; ENSG00000184227 .
    GeneIDi 641371.
    KEGGi hsa:641371.
    UCSCi uc001xol.1. human.

    Organism-specific databases

    CTDi 641371.
    GeneCardsi GC14P074003.
    HGNCi HGNC:33128. ACOT1.
    HPAi HPA043705.
    MIMi 614313. gene.
    neXtProti NX_Q86TX2.
    PharmGKBi PA162375318.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1073.
    HOGENOMi HOG000116219.
    HOVERGENi HBG000331.
    InParanoidi Q86TX2.
    KOi K01068.
    OMAi IPWHWIP.
    OrthoDBi EOG75TMC9.
    PhylomeDBi Q86TX2.
    TreeFami TF314911.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14105.
    BRENDAi 3.1.2.2. 2681.
    SABIO-RK Q86TX2.

    Miscellaneous databases

    ChiTaRSi ACOT1. human.
    GenomeRNAii 641371.
    NextBioi 113125.
    PROi Q86TX2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86TX2.
    Bgeei Q86TX2.
    CleanExi HS_ACOT1.
    Genevestigatori Q86TX2.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR016662. Acyl-CoA_thioEstase_long-chain.
    IPR014940. BAAT_C.
    IPR006862. Thio_Ohase/aa_AcTrfase.
    [Graphical view ]
    Pfami PF08840. BAAT_C. 1 hit.
    PF04775. Bile_Hydr_Trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016521. Acyl-CoA_hydro. 1 hit.
    SUPFAMi SSF53474. SSF53474. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs."
      Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.
      FASEB J. 20:1855-1864(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    2. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Neuroblastoma.
    3. "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].
    4. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 25-35 AND 223-233, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.

    Entry informationi

    Entry nameiACOT1_HUMAN
    AccessioniPrimary (citable) accession number: Q86TX2
    Secondary accession number(s): A1L173, Q3I5F9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 100 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3