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Protein

Acyl-coenzyme A thioesterase THEM5

Gene

THEM5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has acyl-CoA thioesterase activity towards long-chain (C16 and C18) fatty acyl-CoA substrates, with a preference for linoleyl-CoA and other unsaturated long-chain fatty acid-CoA esters. Plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin. Required for normal mitochondrial function.1 Publication

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.1 Publication

Kineticsi

  1. KM=2.4 µM for palmitoyl-CoA (C16:0)1 Publication
  2. KM=4.2 µM for stearoyl-CoA (C18:0)1 Publication
  3. KM=2.9 µM for oleoyl-CoA (C18:1)1 Publication
  4. KM=4.2 µM for linoleyl-CoA (C18:2)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei167 – 1671Proton donor/acceptorBy similarity

    GO - Molecular functioni

    • palmitoyl-CoA hydrolase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.
    SABIO-RKQ8N1Q8.

    Chemistry

    SwissLipidsiSLP:000000659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase THEM5 (EC:3.1.2.2)
    Short name:
    Acyl-CoA thioesterase THEM5
    Alternative name(s):
    Acyl-coenzyme A thioesterase 15
    Thioesterase superfamily member 5
    Gene namesi
    Name:THEM5
    Synonyms:ACOT15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:26755. THEM5.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrial matrix Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi160 – 1601G → A: Strongly reduces enzyme activity. Abolishes enzyme activity; when associated with A-183. 1 Publication
    Mutagenesisi167 – 1671D → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi183 – 1831T → A: Reduces enzyme activity. Abolishes enzyme activity; when associated with A-160. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670814.

    Polymorphism and mutation databases

    BioMutaiTHEM5.
    DMDMi145566964.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 247247Acyl-coenzyme A thioesterase THEM5PRO_0000284519Add
    BLAST

    Proteomic databases

    PaxDbiQ8N1Q8.
    PRIDEiQ8N1Q8.

    PTM databases

    PhosphoSiteiQ8N1Q8.

    Expressioni

    Gene expression databases

    BgeeiQ8N1Q8.
    CleanExiHS_THEM5.
    ExpressionAtlasiQ8N1Q8. baseline and differential.

    Organism-specific databases

    HPAiHPA027646.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAGEA11P43364-23EBI-10264970,EBI-10178634

    Protein-protein interaction databases

    BioGridi129888. 1 interaction.
    IntActiQ8N1Q8. 2 interactions.
    STRINGi9606.ENSP00000357807.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi55 – 573Combined sources
    Helixi64 – 7916Combined sources
    Helixi116 – 1183Combined sources
    Turni123 – 1253Combined sources
    Beta strandi126 – 1349Combined sources
    Turni135 – 1384Combined sources
    Beta strandi139 – 1468Combined sources
    Helixi148 – 1503Combined sources
    Beta strandi151 – 1533Combined sources
    Helixi159 – 17820Combined sources
    Beta strandi180 – 19011Combined sources
    Beta strandi200 – 21011Combined sources
    Beta strandi213 – 2219Combined sources
    Beta strandi228 – 23811Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AE7X-ray1.45A35-247[»]
    ProteinModelPortaliQ8N1Q8.
    SMRiQ8N1Q8. Positions 52-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the THEM4/THEM5 thioesterase family.Curated

    Phylogenomic databases

    eggNOGiKOG4781. Eukaryota.
    ENOG4111ZF6. LUCA.
    GeneTreeiENSGT00390000018826.
    HOGENOMiHOG000220857.
    HOVERGENiHBG054340.
    InParanoidiQ8N1Q8.
    OMAiDQQTVYA.
    OrthoDBiEOG7Q5HFM.
    PhylomeDBiQ8N1Q8.
    TreeFamiTF332518.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q8N1Q8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIRRCFQVAA RLGHHRGLLE APRILPRLNP ASAFGSSTDS MFSRFLPEKT
    60 70 80 90 100
    DLKDYALPNA SWCSDMLSLY QEFLEKTKSS GWIKLPSFKS NRDHIRGLKL
    110 120 130 140 150
    PSGLAVSSDK GDCRIFTRCI QVEGQGFEYV IFFQPTQKKS VCLFQPGSYL
    160 170 180 190 200
    EGPPGFAHGG SLAAMMDETF SKTAFLAGEG LFTLSLNIRF KNLIPVDSLV
    210 220 230 240
    VMDVELDKIE DQKLYMSCIA HSRDQQTVYA KSSGVFLQLQ LEEESPQ
    Length:247
    Mass (Da):27,677
    Last modified:April 17, 2007 - v2
    Checksum:i55117AE70FFC183F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551Y → S.
    Corresponds to variant rs16833597 [ dbSNP | Ensembl ].
    VAR_031764
    Natural varianti197 – 1971D → G.
    Corresponds to variant rs6587625 [ dbSNP | Ensembl ].
    VAR_031765
    Natural varianti206 – 2061L → V.2 Publications
    Corresponds to variant rs6587624 [ dbSNP | Ensembl ].
    VAR_031766

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK095283 mRNA. Translation: BAC04521.1.
    AL450992 Genomic DNA. Translation: CAI12161.1.
    BC101610 mRNA. Translation: AAI01611.1.
    BC112239 mRNA. Translation: AAI12240.1.
    CCDSiCCDS1005.1.
    RefSeqiNP_872384.1. NM_182578.3.
    UniGeneiHs.132648.

    Genome annotation databases

    EnsembliENST00000368817; ENSP00000357807; ENSG00000196407.
    GeneIDi284486.
    KEGGihsa:284486.
    UCSCiuc021oyw.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK095283 mRNA. Translation: BAC04521.1.
    AL450992 Genomic DNA. Translation: CAI12161.1.
    BC101610 mRNA. Translation: AAI01611.1.
    BC112239 mRNA. Translation: AAI12240.1.
    CCDSiCCDS1005.1.
    RefSeqiNP_872384.1. NM_182578.3.
    UniGeneiHs.132648.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AE7X-ray1.45A35-247[»]
    ProteinModelPortaliQ8N1Q8.
    SMRiQ8N1Q8. Positions 52-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi129888. 1 interaction.
    IntActiQ8N1Q8. 2 interactions.
    STRINGi9606.ENSP00000357807.

    Chemistry

    SwissLipidsiSLP:000000659.

    PTM databases

    PhosphoSiteiQ8N1Q8.

    Polymorphism and mutation databases

    BioMutaiTHEM5.
    DMDMi145566964.

    Proteomic databases

    PaxDbiQ8N1Q8.
    PRIDEiQ8N1Q8.

    Protocols and materials databases

    DNASUi284486.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000368817; ENSP00000357807; ENSG00000196407.
    GeneIDi284486.
    KEGGihsa:284486.
    UCSCiuc021oyw.2. human.

    Organism-specific databases

    CTDi284486.
    GeneCardsiTHEM5.
    HGNCiHGNC:26755. THEM5.
    HPAiHPA027646.
    MIMi615653. gene.
    neXtProtiNX_Q8N1Q8.
    PharmGKBiPA142670814.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG4781. Eukaryota.
    ENOG4111ZF6. LUCA.
    GeneTreeiENSGT00390000018826.
    HOGENOMiHOG000220857.
    HOVERGENiHBG054340.
    InParanoidiQ8N1Q8.
    OMAiDQQTVYA.
    OrthoDBiEOG7Q5HFM.
    PhylomeDBiQ8N1Q8.
    TreeFamiTF332518.

    Enzyme and pathway databases

    ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.
    SABIO-RKQ8N1Q8.

    Miscellaneous databases

    GenomeRNAii284486.
    NextBioi94926.
    PROiQ8N1Q8.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8N1Q8.
    CleanExiHS_THEM5.
    ExpressionAtlasiQ8N1Q8. baseline and differential.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-206.
      Tissue: Tongue.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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], VARIANT VAL-206.
      Tissue: Heart and Lung.
    4. "Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development."
      Zhuravleva E., Gut H., Hynx D., Marcellin D., Bleck C.K., Genoud C., Cron P., Keusch J.J., Dummler B., Esposti M.D., Hemmings B.A.
      Mol. Cell. Biol. 32:2685-2697(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 35-247, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-160; ASP-167 AND THR-183.

    Entry informationi

    Entry nameiACO15_HUMAN
    AccessioniPrimary (citable) accession number: Q8N1Q8
    Secondary accession number(s): Q5T1C3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: March 16, 2016
    This is version 101 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. 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.