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Q8BWT1

- THIM_MOUSE

UniProt

Q8BWT1 - THIM_MOUSE

Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

Acaa2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Abolishes BNIP3-mediated apoptosis and mitochondrial damage.By similarity

    Catalytic activityi

    Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei92 – 921Acyl-thioester intermediateBy similarity
    Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation
    Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA C-acyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid metabolic process Source: UniProtKB-UniPathway
    2. negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    UniPathwayiUPA00199.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-ketoacyl-CoA thiolase, mitochondrial (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
    Mitochondrial 3-oxoacyl-CoA thiolase
    Gene namesi
    Name:Acaa2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1098623. Acaa2.

    Subcellular locationi

    Mitochondrion By similarity
    Note: Colocalizes with BNIP3 in the mitochondria.By similarity

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrialPRO_0000223300Add
    BLAST
    Transit peptidei1 – 1616Mitochondrion; not cleavedBy similarityAdd
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251N6-acetyllysine; alternate1 Publication
    Modified residuei25 – 251N6-succinyllysine; alternate1 Publication
    Modified residuei28 – 281Phosphoserine1 Publication
    Modified residuei45 – 451N6-succinyllysine1 Publication
    Modified residuei119 – 1191PhosphothreonineBy similarity
    Modified residuei121 – 1211PhosphoserineBy similarity
    Modified residuei127 – 1271PhosphotyrosineBy similarity
    Modified residuei137 – 1371N6-acetyllysine; alternate1 Publication
    Modified residuei137 – 1371N6-succinyllysine; alternate1 Publication
    Modified residuei143 – 1431N6-acetyllysine; alternate1 Publication
    Modified residuei143 – 1431N6-succinyllysine; alternate1 Publication
    Modified residuei158 – 1581N6-acetyllysine; alternate1 Publication
    Modified residuei158 – 1581N6-succinyllysine; alternate1 Publication
    Modified residuei171 – 1711N6-acetyllysine; alternate1 Publication
    Modified residuei171 – 1711N6-succinyllysine; alternate1 Publication
    Modified residuei191 – 1911N6-acetyllysine; alternate2 Publications
    Modified residuei191 – 1911N6-succinyllysine; alternate1 Publication
    Modified residuei209 – 2091N6-acetyllysine; alternate1 Publication
    Modified residuei209 – 2091N6-succinyllysine; alternate1 Publication
    Modified residuei211 – 2111N6-succinyllysine1 Publication
    Modified residuei212 – 2121N6-succinyllysine1 Publication
    Modified residuei214 – 2141N6-succinyllysine1 Publication
    Modified residuei234 – 2341N6-acetyllysine; alternate1 Publication
    Modified residuei234 – 2341N6-succinyllysine; alternate1 Publication
    Modified residuei240 – 2401N6-succinyllysine1 Publication
    Modified residuei241 – 2411N6-acetyllysine1 Publication
    Modified residuei269 – 2691N6-acetyllysine1 Publication
    Modified residuei270 – 2701N6-acetyllysine1 Publication
    Modified residuei305 – 3051N6-acetyllysine; alternate1 Publication
    Modified residuei305 – 3051N6-succinyllysine; alternate1 Publication
    Modified residuei312 – 3121N6-acetyllysine; alternate1 Publication
    Modified residuei312 – 3121N6-succinyllysine; alternate1 Publication
    Modified residuei340 – 3401N6-acetyllysine1 Publication
    Modified residuei375 – 3751N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8BWT1.
    PaxDbiQ8BWT1.
    PRIDEiQ8BWT1.

    2D gel databases

    REPRODUCTION-2DPAGEQ8BWT1.

    PTM databases

    PhosphoSiteiQ8BWT1.

    Expressioni

    Gene expression databases

    BgeeiQ8BWT1.
    GenevestigatoriQ8BWT1.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with BNIP3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi206649. 3 interactions.
    IntActiQ8BWT1. 9 interactions.
    MINTiMINT-1839761.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BWT1.
    SMRiQ8BWT1. Positions 4-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiQ3TIT9.
    KOiK07508.
    OMAiQTLACAD.
    OrthoDBiEOG7JQBNG.
    TreeFamiTF105696.

    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.

    Q8BWT1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLRGVFIV AAKRTPFGAY GGLLKDFSAT DLTEFAARAA LSAGKVPPET    50
    IDSVIVGNVM QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV 100
    SGCQEICSKD AEVVLCGGTE SMSQSPYCVR NVRFGTKFGL DLKLEDTLWA 150
    GLTDQHVKLP MGMTAENLAA KYNISREDCD RYALQSQQRW KAANEAGYFN 200
    EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPSVFK KDGTVTAGNA 250
    SGVSDGAGAV IIASEDAVKK HNFTPLARVV GYFVSGCDPT IMGIGPVPAI 300
    NGALKKAGLS LKDMDLIDVN EAFAPQFLSV QKALDLDPSK TNVSGGAIAL 350
    GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIA LIIQNTA 397
    Length:397
    Mass (Da):41,830
    Last modified:July 27, 2011 - v3
    Checksum:i856840546F5CB8DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti397 – 3971A → V in AAH28901. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK050101 mRNA. Translation: BAC34067.1.
    AK167567 mRNA. Translation: BAE39630.1.
    AK167715 mRNA. Translation: BAE39757.1.
    AK169359 mRNA. Translation: BAE41108.1.
    CH466528 Genomic DNA. Translation: EDL09521.1.
    BC028901 mRNA. Translation: AAH28901.1.
    CCDSiCCDS29342.1.
    RefSeqiNP_803421.1. NM_177470.3.
    UniGeneiMm.245724.

    Genome annotation databases

    EnsembliENSMUST00000041053; ENSMUSP00000037348; ENSMUSG00000036880.
    GeneIDi52538.
    KEGGimmu:52538.
    UCSCiuc008fpt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK050101 mRNA. Translation: BAC34067.1 .
    AK167567 mRNA. Translation: BAE39630.1 .
    AK167715 mRNA. Translation: BAE39757.1 .
    AK169359 mRNA. Translation: BAE41108.1 .
    CH466528 Genomic DNA. Translation: EDL09521.1 .
    BC028901 mRNA. Translation: AAH28901.1 .
    CCDSi CCDS29342.1.
    RefSeqi NP_803421.1. NM_177470.3.
    UniGenei Mm.245724.

    3D structure databases

    ProteinModelPortali Q8BWT1.
    SMRi Q8BWT1. Positions 4-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206649. 3 interactions.
    IntActi Q8BWT1. 9 interactions.
    MINTi MINT-1839761.

    PTM databases

    PhosphoSitei Q8BWT1.

    2D gel databases

    REPRODUCTION-2DPAGE Q8BWT1.

    Proteomic databases

    MaxQBi Q8BWT1.
    PaxDbi Q8BWT1.
    PRIDEi Q8BWT1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000041053 ; ENSMUSP00000037348 ; ENSMUSG00000036880 .
    GeneIDi 52538.
    KEGGi mmu:52538.
    UCSCi uc008fpt.1. mouse.

    Organism-specific databases

    CTDi 10449.
    MGIi MGI:1098623. Acaa2.

    Phylogenomic databases

    eggNOGi COG0183.
    GeneTreei ENSGT00390000009412.
    HOGENOMi HOG000012238.
    HOVERGENi HBG003112.
    InParanoidi Q3TIT9.
    KOi K07508.
    OMAi QTLACAD.
    OrthoDBi EOG7JQBNG.
    TreeFami TF105696.

    Enzyme and pathway databases

    UniPathwayi UPA00199 .

    Miscellaneous databases

    NextBioi 309107.
    PROi Q8BWT1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BWT1.
    Genevestigatori Q8BWT1.

    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. "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.
      Tissue: Amnion, Heart and Liver.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Strain: FVB/N.
      Tissue: Liver.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-45; LYS-137; LYS-143; LYS-158; LYS-171; LYS-191; LYS-209; LYS-211; LYS-212; LYS-214; LYS-234; LYS-240; LYS-305 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: 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-25; LYS-137; LYS-143; LYS-158; LYS-171; LYS-191; LYS-209; LYS-234; LYS-241; LYS-269; LYS-270; LYS-305; LYS-312; LYS-340 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiTHIM_MOUSE
    AccessioniPrimary (citable) accession number: Q8BWT1
    Secondary accession number(s): Q3TIT9, Q8JZR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 94 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3