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Q8QZT1

- THIL_MOUSE

UniProt

Q8QZT1 - THIL_MOUSE

Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

Acat1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Plays a major role in ketone body metabolism.By similarity

    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: MGI
    2. coenzyme binding Source: Ensembl
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Potassium

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:87870. Acat1.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030MitochondrionBy similarityAdd
    BLAST
    Chaini31 – 424394Acetyl-CoA acetyltransferase, mitochondrialPRO_0000034087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631N6-acetyllysine; alternate1 Publication
    Modified residuei63 – 631N6-succinyllysine; alternate1 Publication
    Modified residuei75 – 751N6-succinyllysine1 Publication
    Modified residuei171 – 1711N6-acetyllysine; alternate2 Publications
    Modified residuei171 – 1711N6-succinyllysine; alternate1 Publication
    Modified residuei178 – 1781N6-acetyllysine; alternate1 Publication
    Modified residuei178 – 1781N6-succinyllysine; alternate1 Publication
    Modified residuei187 – 1871N6-acetyllysine; alternate1 Publication
    Modified residuei187 – 1871N6-succinyllysine; alternate1 Publication
    Modified residuei199 – 1991N6-acetyllysine; alternate1 Publication
    Modified residuei199 – 1991N6-succinyllysine; alternate1 Publication
    Modified residuei220 – 2201N6-acetyllysine; alternate1 Publication
    Modified residuei220 – 2201N6-succinyllysine; alternate1 Publication
    Modified residuei227 – 2271N6-acetyllysine; alternate1 Publication
    Modified residuei227 – 2271N6-succinyllysine; alternate1 Publication
    Modified residuei240 – 2401N6-succinyllysine1 Publication
    Modified residuei242 – 2421N6-acetyllysine; alternate1 Publication
    Modified residuei242 – 2421N6-succinyllysine; alternate1 Publication
    Modified residuei248 – 2481N6-acetyllysine1 Publication
    Modified residuei254 – 2541N6-acetyllysine1 Publication
    Modified residuei260 – 2601N6-acetyllysine; alternate1 Publication
    Modified residuei260 – 2601N6-succinyllysine; alternate1 Publication
    Modified residuei263 – 2631N6-succinyllysine1 Publication
    Modified residuei265 – 2651N6-succinyllysine1 Publication
    Modified residuei270 – 2701N6-acetyllysine1 Publication
    Modified residuei335 – 3351N6-acetyllysine1 Publication

    Post-translational modificationi

    Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8QZT1.
    PaxDbiQ8QZT1.
    PRIDEiQ8QZT1.

    2D gel databases

    REPRODUCTION-2DPAGEQ8QZT1.

    PTM databases

    PhosphoSiteiQ8QZT1.

    Expressioni

    Gene expression databases

    BgeeiQ8QZT1.
    CleanExiMM_ACAT1.
    GenevestigatoriQ8QZT1.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi225601. 1 interaction.
    IntActiQ8QZT1. 6 interactions.
    MINTiMINT-1840908.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8QZT1.
    SMRiQ8QZT1. 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.
    InParanoidiQ8QZT1.
    KOiK00626.
    OMAiDQVAIWE.
    OrthoDBiEOG7JQBNG.
    PhylomeDBiQ8QZT1.
    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.

    Q8QZT1-1 [UniParc]FASTAAdd to Basket

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    MAALVALHGV VRRPLLRGLL QEVRCLERSY ASKPTLNEVV IVSAIRTPIG    50
    SFLGSLASQP ATKLGTAAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP 100
    TRQATLGAGL PISTPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM 150
    ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK 200
    MNISRQEQDT YALSSYTRSK EAWDAGKFAS EITPITISVK GKPDVVVKED 250
    EEYKRVDFSK VPKLKTVFQK ENGTITAANA STLNDGAAAL VLMTAEAAQR 300
    LNVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN 350
    EAFSVVVLAN IKMLEIDPQK VNIHGGAVSL GHPIGMSGAR IVVHMAHALK 400
    PGEFGLASIC NGGGGASALL IEKL 424
    Length:424
    Mass (Da):44,816
    Last modified:June 1, 2002 - v1
    Checksum:i0F75A820E992BFD9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ510150 mRNA. Translation: CAD52869.1.
    AK032097 mRNA. Translation: BAC27697.1.
    AK081715 mRNA. Translation: BAC38304.1.
    AK169771 mRNA. Translation: BAE41356.1.
    BC024763 mRNA. Translation: AAH24763.1.
    CCDSiCCDS23184.1.
    RefSeqiNP_659033.1. NM_144784.3.
    UniGeneiMm.293233.

    Genome annotation databases

    EnsembliENSMUST00000034547; ENSMUSP00000034547; ENSMUSG00000032047.
    GeneIDi110446.
    KEGGimmu:110446.
    UCSCiuc009pmg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ510150 mRNA. Translation: CAD52869.1 .
    AK032097 mRNA. Translation: BAC27697.1 .
    AK081715 mRNA. Translation: BAC38304.1 .
    AK169771 mRNA. Translation: BAE41356.1 .
    BC024763 mRNA. Translation: AAH24763.1 .
    CCDSi CCDS23184.1.
    RefSeqi NP_659033.1. NM_144784.3.
    UniGenei Mm.293233.

    3D structure databases

    ProteinModelPortali Q8QZT1.
    SMRi Q8QZT1. Positions 32-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 225601. 1 interaction.
    IntActi Q8QZT1. 6 interactions.
    MINTi MINT-1840908.

    Chemistry

    BindingDBi Q8QZT1.

    PTM databases

    PhosphoSitei Q8QZT1.

    2D gel databases

    REPRODUCTION-2DPAGE Q8QZT1.

    Proteomic databases

    MaxQBi Q8QZT1.
    PaxDbi Q8QZT1.
    PRIDEi Q8QZT1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034547 ; ENSMUSP00000034547 ; ENSMUSG00000032047 .
    GeneIDi 110446.
    KEGGi mmu:110446.
    UCSCi uc009pmg.1. mouse.

    Organism-specific databases

    CTDi 38.
    MGIi MGI:87870. Acat1.

    Phylogenomic databases

    eggNOGi COG0183.
    GeneTreei ENSGT00390000009412.
    HOGENOMi HOG000012238.
    HOVERGENi HBG003112.
    InParanoidi Q8QZT1.
    KOi K00626.
    OMAi DQVAIWE.
    OrthoDBi EOG7JQBNG.
    PhylomeDBi Q8QZT1.
    TreeFami TF300650.

    Miscellaneous databases

    ChiTaRSi ACAT1. mouse.
    NextBioi 363999.
    PROi Q8QZT1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8QZT1.
    CleanExi MM_ACAT1.
    Genevestigatori Q8QZT1.

    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. "Species-specific differences in peroxisomal association of acetoacetyl-CoA synthase."
      Ghys K., Amery L., Van Veldhoven P.P.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Head, Medulla oblongata and Thymus.
    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].
      Tissue: Eye.
    4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 47-75; 85-121; 163-171; 179-187; 206-218; 228-254; 271-332 AND 363-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-265, DESUCCINYLATION BY SIRT5, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-75; LYS-171; LYS-178; LYS-187; LYS-199; LYS-220; LYS-227; LYS-240; LYS-242; LYS-260; LYS-263 AND LYS-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-171; LYS-178; LYS-187; LYS-199; LYS-220; LYS-227; LYS-242; LYS-248; LYS-254; LYS-260; LYS-270 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiTHIL_MOUSE
    AccessioniPrimary (citable) accession number: Q8QZT1
    Secondary accession number(s): Q3TE92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 101 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3