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P17764

- THIL_RAT

UniProt

P17764 - THIL_RAT

Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

Acat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Plays a major role in ketone body metabolism.

    Catalytic activityi

    2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

    Enzyme regulationi

    Activated by potassium ions, but not sodium ions.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231Acyl-thioester intermediateBy similarity
    Metal bindingi216 – 2161PotassiumBy similarity
    Binding sitei216 – 2161Coenzyme ABy similarity
    Binding sitei260 – 2601Coenzyme ABy similarity
    Metal bindingi277 – 2771Potassium; via carbonyl oxygenBy similarity
    Metal bindingi278 – 2781Potassium; via carbonyl oxygenBy similarity
    Metal bindingi280 – 2801Potassium; via carbonyl oxygenBy similarity
    Binding sitei281 – 2811Coenzyme ABy similarity
    Metal bindingi378 – 3781Potassium; via carbonyl oxygenBy similarity
    Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation
    Active sitei410 – 4101Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA C-acetyltransferase activity Source: RGD
    2. coenzyme binding Source: RGD
    3. enzyme binding Source: RGD
    4. metal ion binding Source: UniProtKB-KW
    5. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. adipose tissue development Source: RGD
    2. brain development Source: RGD
    3. liver development Source: RGD
    4. metanephric proximal convoluted tubule development Source: RGD
    5. protein homooligomerization Source: RGD
    6. response to hormone Source: RGD
    7. response to organic cyclic compound Source: RGD
    8. response to starvation Source: RGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Potassium

    Enzyme and pathway databases

    ReactomeiREACT_203677. Synthesis of Ketone Bodies.
    REACT_215799. Utilization of Ketone Bodies.
    REACT_221218. Branched-chain amino acid catabolism.
    SABIO-RKP17764.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase, mitochondrial (EC:2.3.1.9)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    Gene namesi
    Name:Acat1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi2016. Acat1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: RGD
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
    BLAST
    Chaini31 – 424394Acetyl-CoA acetyltransferase, mitochondrialPRO_0000034088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631N6-acetyllysine; alternateBy similarity
    Modified residuei63 – 631N6-succinyllysine; alternateBy similarity
    Modified residuei75 – 751N6-succinyllysineBy similarity
    Modified residuei171 – 1711N6-acetyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-succinyllysine; alternateBy similarity
    Modified residuei178 – 1781N6-acetyllysine; alternateBy similarity
    Modified residuei178 – 1781N6-succinyllysine; alternateBy similarity
    Modified residuei187 – 1871N6-acetyllysine; alternateBy similarity
    Modified residuei187 – 1871N6-succinyllysine; alternateBy similarity
    Modified residuei199 – 1991N6-acetyllysine; alternateBy similarity
    Modified residuei199 – 1991N6-succinyllysine; alternateBy similarity
    Modified residuei220 – 2201N6-acetyllysine; alternateBy similarity
    Modified residuei220 – 2201N6-succinyllysine; alternateBy similarity
    Modified residuei227 – 2271N6-acetyllysine; alternateBy similarity
    Modified residuei227 – 2271N6-succinyllysine; alternateBy similarity
    Modified residuei240 – 2401N6-succinyllysineBy similarity
    Modified residuei242 – 2421N6-acetyllysine; alternateBy similarity
    Modified residuei242 – 2421N6-succinyllysine; alternateBy similarity
    Modified residuei248 – 2481N6-acetyllysineBy similarity
    Modified residuei254 – 2541N6-acetyllysineBy similarity
    Modified residuei260 – 2601N6-acetyllysine; alternateBy similarity
    Modified residuei260 – 2601N6-succinyllysine; alternateBy similarity
    Modified residuei263 – 2631N6-succinyllysineBy similarity
    Modified residuei265 – 2651N6-succinyllysineBy similarity
    Modified residuei270 – 2701N6-acetyllysineBy similarity
    Modified residuei335 – 3351N6-acetyllysineBy similarity

    Post-translational modificationi

    Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP17764.
    PRIDEiP17764.

    PTM databases

    PhosphoSiteiP17764.

    Expressioni

    Gene expression databases

    GenevestigatoriP17764.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP17764. 3 interactions.
    MINTiMINT-4588676.
    STRINGi10116.ENSRNOP00000010573.

    Structurei

    3D structure databases

    ProteinModelPortaliP17764.
    SMRiP17764. Positions 32-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni255 – 2573Coenzyme A bindingBy similarity

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiP17764.
    KOiK00626.
    OMAiSNVPYTM.
    OrthoDBiEOG7JQBNG.
    PhylomeDBiP17764.
    TreeFamiTF300650.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17764-1 [UniParc]FASTAAdd to Basket

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    MAALAVLHGV VRRPLLRGLL QEVRCLGRSY ASKPTLNDVV IVSATRTPIG    50
    SFLGSLASQP ATKLGTIAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP 100
    TRQATLGAGL PIATPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM 150
    ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK 200
    LSISREEQDK YAIGSYTRSK EAWDAGKFAN EITPITISVK GKPDVVVKED 250
    EEYKRVDFSK VPKLKTVFQK ENGTVTAANA STLNDGAAAV VLMTAEAAQR 300
    LKVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN 350
    EAFSVVVLAN IKMLEIDPQK VNVHGGAVSL GHPIGMSGAR IVVHLAHALK 400
    QGEFGLASIC NGGGGASAVL IEKL 424
    Length:424
    Mass (Da):44,695
    Last modified:August 1, 1990 - v1
    Checksum:i79E8881DB242EFEE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00512 mRNA. Translation: BAA00401.1. Sequence problems.
    D13921 mRNA. Translation: BAA03016.1.
    PIRiJU0072. XXRTAC.
    RefSeqiNP_058771.2. NM_017075.2.
    UniGeneiRn.4054.

    Genome annotation databases

    EnsembliENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862.
    GeneIDi25014.
    KEGGirno:25014.
    UCSCiRGD:2016. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00512 mRNA. Translation: BAA00401.1 . Sequence problems.
    D13921 mRNA. Translation: BAA03016.1 .
    PIRi JU0072. XXRTAC.
    RefSeqi NP_058771.2. NM_017075.2.
    UniGenei Rn.4054.

    3D structure databases

    ProteinModelPortali P17764.
    SMRi P17764. Positions 32-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P17764. 3 interactions.
    MINTi MINT-4588676.
    STRINGi 10116.ENSRNOP00000010573.

    Chemistry

    BindingDBi P17764.
    GuidetoPHARMACOLOGYi 2435.

    PTM databases

    PhosphoSitei P17764.

    Proteomic databases

    PaxDbi P17764.
    PRIDEi P17764.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010573 ; ENSRNOP00000010573 ; ENSRNOG00000007862 .
    GeneIDi 25014.
    KEGGi rno:25014.
    UCSCi RGD:2016. rat.

    Organism-specific databases

    CTDi 38.
    RGDi 2016. Acat1.

    Phylogenomic databases

    eggNOGi COG0183.
    GeneTreei ENSGT00390000009412.
    HOGENOMi HOG000012238.
    HOVERGENi HBG003112.
    InParanoidi P17764.
    KOi K00626.
    OMAi SNVPYTM.
    OrthoDBi EOG7JQBNG.
    PhylomeDBi P17764.
    TreeFami TF300650.

    Enzyme and pathway databases

    Reactomei REACT_203677. Synthesis of Ketone Bodies.
    REACT_215799. Utilization of Ketone Bodies.
    REACT_221218. Branched-chain amino acid catabolism.
    SABIO-RK P17764.

    Miscellaneous databases

    NextBioi 605101.
    PROi P17764.

    Gene expression databases

    Genevestigatori P17764.

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat mitochondrial acetoacetyl-CoA thiolase."
      Fukao T., Kamijo K., Osumi T., Fujiki Y., Yamaguchi S., Orii T., Hashimoto T.
      J. Biochem. 106:197-204(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-50.

    Entry informationi

    Entry nameiTHIL_RAT
    AccessioniPrimary (citable) accession number: P17764
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3