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Protein

Acyl-coenzyme A thioesterase 13

Gene

Acot13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis.2 Publications

Kineticsi

  1. KM=47 µM for decanoyl-CoA1 Publication
  2. KM=27 µM for oleoyl-CoA1 Publication
  3. KM=10 µM for palmitoyl-CoA1 Publication
  4. KM=15 µM for myristoyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.
    SABIO-RKQ9CQR4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 13 (EC:3.1.2.-)
    Short name:
    Acyl-CoA thioesterase 13
    Alternative name(s):
    Thioesterase superfamily member 2
    Cleaved into the following chain:
    Gene namesi
    Name:Acot13
    Synonyms:Them2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 13

    Organism-specific databases

    MGIiMGI:1914084. Acot13.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB-SubCell
    • extracellular exosome Source: MGI
    • mitochondrion Source: UniProtKB
    • nucleus Source: MGI
    • spindle Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype until 7 weeks of age. Animals are viable and fertile. After 7 weeks, mutant mice exhibit a modest decrease in body weight and decreased adiposity, compared to wild-type animals, despite increased food consumption. They tend to show a reduced hepatic fatty acyl-CoA thioesterase activity, leading to alterations in fatty acid metabolism and improved glucose homeostasis. When fed a high-fat diet, mutant livers are protected against steatosis and increased hepatic glucose production (PubMed:22345407). Mutant mice adapt more rapidly than wild-type to short-term cold exposure by increasing physical activity, food consumption and energy expenditure. After 96-hour equilibration at cold temperature, genotype-dependent differences are abolished. Mutant brown adipose tissue show reduced lipid droplets, alterations in the ultrastructure of mitochondria and a small increase in the expression of thermogenic genes (PubMed:24072708).2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 140140Acyl-coenzyme A thioesterase 13PRO_0000156698Add
    BLAST
    Initiator methionineiRemoved; alternateBy similarity
    Chaini2 – 140139Acyl-coenzyme A thioesterase 13, N-terminally processedPRO_0000434364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei27 – 271N6-acetyllysineCombined sources
    Modified residuei37 – 371N6-acetyllysineCombined sources
    Modified residuei43 – 431N6-acetyllysineCombined sources
    Modified residuei108 – 1081N6-acetyllysineCombined sources
    Modified residuei127 – 1271N6-acetyllysineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ9CQR4.
    MaxQBiQ9CQR4.
    PaxDbiQ9CQR4.
    PRIDEiQ9CQR4.

    2D gel databases

    REPRODUCTION-2DPAGEQ9CQR4.

    PTM databases

    iPTMnetiQ9CQR4.
    PhosphoSiteiQ9CQR4.

    Expressioni

    Tissue specificityi

    Highly expressed in the kidney and moderately in the heart, liver, brain, small and large intestine. Also expressed in brown adipose tissue.4 Publications

    Gene expression databases

    BgeeiQ9CQR4.
    CleanExiMM_THEM2.
    ExpressionAtlasiQ9CQR4. baseline and differential.
    GenevisibleiQ9CQR4. MM.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with PCTP.2 Publications

    Protein-protein interaction databases

    BioGridi211751. 1 interaction.
    IntActiQ9CQR4. 2 interactions.
    MINTiMINT-1851718.
    STRINGi10090.ENSMUSP00000006900.

    Structurei

    Secondary structure

    1
    140
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 129Combined sources
    Beta strandi38 – 436Combined sources
    Turni46 – 483Combined sources
    Beta strandi53 – 553Combined sources
    Helixi57 – 659Combined sources
    Turni66 – 683Combined sources
    Helixi70 – 723Combined sources
    Beta strandi82 – 909Combined sources
    Beta strandi99 – 1035Combined sources
    Beta strandi106 – 1083Combined sources
    Beta strandi111 – 12212Combined sources
    Turni123 – 1253Combined sources
    Beta strandi128 – 13710Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CY9X-ray2.72A/B1-140[»]
    ProteinModelPortaliQ9CQR4.
    SMRiQ9CQR4. Positions 1-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CQR4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.Curated

    Phylogenomic databases

    eggNOGiKOG3328. Eukaryota.
    COG2050. LUCA.
    GeneTreeiENSGT00390000013934.
    HOGENOMiHOG000170540.
    InParanoidiQ9CQR4.
    KOiK17362.
    OMAiICEMKVE.
    OrthoDBiEOG7Q8CQ4.
    PhylomeDBiQ9CQR4.
    TreeFamiTF315062.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9CQR4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSMTQNLRE VMKVMFKVPG FDRVLEKVTL VSAAPEKLIC EMKVEEQHTN
    60 70 80 90 100
    KLGTLHGGLT ATLVDSISTM ALMCTERGAP GVSVDMNITY MSPAKIGEEI
    110 120 130 140
    VITAHILKQG KTLAFASVDL TNKTTGKLIA QGRHTKHLGN
    Length:140
    Mass (Da):15,183
    Last modified:June 1, 2001 - v1
    Checksum:i66E47830E8643051
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK002261 mRNA. Translation: BAB21973.1.
    AK008624 mRNA. Translation: BAB25786.1.
    BC018165 mRNA. Translation: AAH18165.1.
    CCDSiCCDS26380.1.
    RefSeqiNP_080066.1. NM_025790.2.
    UniGeneiMm.2125.

    Genome annotation databases

    EnsembliENSMUST00000006900; ENSMUSP00000006900; ENSMUSG00000006717.
    GeneIDi66834.
    KEGGimmu:66834.
    UCSCiuc007pwj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK002261 mRNA. Translation: BAB21973.1.
    AK008624 mRNA. Translation: BAB25786.1.
    BC018165 mRNA. Translation: AAH18165.1.
    CCDSiCCDS26380.1.
    RefSeqiNP_080066.1. NM_025790.2.
    UniGeneiMm.2125.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CY9X-ray2.72A/B1-140[»]
    ProteinModelPortaliQ9CQR4.
    SMRiQ9CQR4. Positions 1-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi211751. 1 interaction.
    IntActiQ9CQR4. 2 interactions.
    MINTiMINT-1851718.
    STRINGi10090.ENSMUSP00000006900.

    PTM databases

    iPTMnetiQ9CQR4.
    PhosphoSiteiQ9CQR4.

    2D gel databases

    REPRODUCTION-2DPAGEQ9CQR4.

    Proteomic databases

    EPDiQ9CQR4.
    MaxQBiQ9CQR4.
    PaxDbiQ9CQR4.
    PRIDEiQ9CQR4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000006900; ENSMUSP00000006900; ENSMUSG00000006717.
    GeneIDi66834.
    KEGGimmu:66834.
    UCSCiuc007pwj.1. mouse.

    Organism-specific databases

    CTDi55856.
    MGIiMGI:1914084. Acot13.

    Phylogenomic databases

    eggNOGiKOG3328. Eukaryota.
    COG2050. LUCA.
    GeneTreeiENSGT00390000013934.
    HOGENOMiHOG000170540.
    InParanoidiQ9CQR4.
    KOiK17362.
    OMAiICEMKVE.
    OrthoDBiEOG7Q8CQ4.
    PhylomeDBiQ9CQR4.
    TreeFamiTF315062.

    Enzyme and pathway databases

    ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.
    SABIO-RKQ9CQR4.

    Miscellaneous databases

    EvolutionaryTraceiQ9CQR4.
    NextBioi322771.
    PROiQ9CQR4.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9CQR4.
    CleanExiMM_THEM2.
    ExpressionAtlasiQ9CQR4. baseline and differential.
    GenevisibleiQ9CQR4. MM.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: Kidney and Stomach.
    2. "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].
    3. "Human thioesterase superfamily member 2 (hTHEM2) is co-localized with beta-tubulin onto the microtubule."
      Cheng Z., Bao S., Shan X., Xu H., Gong W.
      Biochem. Biophys. Res. Commun. 350:850-853(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Interacting proteins dictate function of the minimal START domain phosphatidylcholine transfer protein/StarD2."
      Kanno K., Wu M.K., Agate D.S., Fanelli B.J., Wagle N., Scapa E.F., Ukomadu C., Cohen D.E.
      J. Biol. Chem. 282:30728-30736(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCTP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "Thioesterase superfamily member 2 (Them2)/acyl-CoA thioesterase 13 (Acot13): A homotetrameric hotdog fold thioesterase with selectivity for long chain fatty acyl-CoAs."
      Wei J., Kang H.W., Cohen D.E.
      Biochem. J. 421:311-322(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
    7. "Thioesterase superfamily member 2/acyl-CoA thioesterase 13 (Them2/Acot13) regulates hepatic lipid and glucose metabolism."
      Kang H.W., Niepel M.W., Han S., Kawano Y., Cohen D.E.
      FASEB J. 26:2209-2221(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    8. "Thioesterase superfamily member 2/Acyl-CoA thioesterase 13 (Them2/Acot13) regulates adaptive thermogenesis in mice."
      Kang H.W., Ozdemir C., Kawano Y., LeClair K.B., Vernochet C., Kahn C.R., Hagen S.J., Cohen D.E.
      J. Biol. Chem. 288:33376-33386(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "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-27; LYS-37; LYS-43; LYS-108 AND LYS-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Crystal structure of thioesterase superfamily member 2 from Mus musculus."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS).

    Entry informationi

    Entry nameiACO13_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: June 1, 2001
    Last modified: March 16, 2016
    This is version 115 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.