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P49753

- ACOT2_HUMAN

UniProt

P49753 - ACOT2_HUMAN

Protein

Acyl-coenzyme A thioesterase 2, mitochondrial

Gene

ACOT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 6 (24 Nov 2009)
      Previous versions | rss
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    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. Displays high levels of activity on medium- and long chain acyl CoAs.1 Publication

    Catalytic activityi

    Palmitoyl-CoA + H2O = CoA + palmitate.

    Kineticsi

    1. KM=40.3 µM for C10-acyl-CoA1 Publication
    2. KM=8.9 µM for C12-acyl-CoA1 Publication
    3. KM=1.6 µM for C14-acyl-CoA1 Publication
    4. KM=2.0 µM for C16-acyl-CoA1 Publication
    5. KM=2.8 µM for C18-acyl-CoA1 Publication
    6. KM=4.8 µM for C20-acyl-CoA1 Publication
    7. KM=4.5 µM for C16:1-acyl-CoA1 Publication
    8. KM=6.1 µM for C18:1-acyl-CoA1 Publication
    9. KM=4.3 µM for C18:1-trans-acyl-CoA1 Publication

    Vmax=212 nmol/min/mg enzyme toward C10-acyl-CoA1 Publication

    Vmax=681 nmol/min/mg enzyme toward C12-acyl-CoA1 Publication

    Vmax=766 nmol/min/mg enzyme toward C14-acyl-CoA1 Publication

    Vmax=656 nmol/min/mg enzyme toward C16-acyl-CoA1 Publication

    Vmax=488 nmol/min/mg enzyme toward C18-acyl-CoA1 Publication

    Vmax=408 nmol/min/mg enzyme toward C20-acyl-CoA1 Publication

    Vmax=661 nmol/min/mg enzyme toward C16:1-acyl-CoA1 Publication

    Vmax=304 nmol/min/mg enzyme toward C18:1-acyl-CoA1 Publication

    Vmax=418 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei294 – 2941Charge relay systemBy similarity
    Active sitei388 – 3881Charge relay systemBy similarity
    Active sitei422 – 4221Charge relay systemBy similarity

    GO - Molecular functioni

    1. acyl-CoA hydrolase activity Source: HGNC
    2. palmitoyl-CoA hydrolase activity Source: UniProtKB-EC
    3. receptor binding Source: UniProtKB

    GO - Biological processi

    1. acyl-CoA metabolic process Source: HGNC
    2. long-chain fatty acid metabolic process Source: HGNC
    3. very long-chain fatty acid metabolic process Source: HGNC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04318-MONOMER.
    BRENDAi3.1.2.2. 2681.
    SABIO-RKP49753.

    Protein family/group databases

    MEROPSiS09.028.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 2, mitochondrial (EC:3.1.2.2)
    Short name:
    Acyl-CoA thioesterase 2
    Alternative name(s):
    Acyl-coenzyme A thioester hydrolase 2a
    CTE-Ia
    Long-chain acyl-CoA thioesterase 2
    ZAP128
    Gene namesi
    Name:ACOT2
    Synonyms:PTE2, PTE2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:18431. ACOT2.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrion Source: HGNC

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672653.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 483Acyl-coenzyme A thioesterase 2, mitochondrialPRO_0000202147
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041N6-acetyllysineBy similarity
    Modified residuei470 – 4701N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP49753.
    PRIDEiP49753.

    PTM databases

    PhosphoSiteiP49753.

    Expressioni

    Tissue specificityi

    Strongest expression in heart, liver, muscle and kidney. Weak in placenta and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiP49753.
    BgeeiP49753.
    CleanExiHS_ACOT2.
    GenevestigatoriP49753.

    Organism-specific databases

    HPAiHPA043705.

    Interactioni

    Protein-protein interaction databases

    BioGridi116164. 3 interactions.
    MINTiMINT-5004303.
    STRINGi9606.ENSP00000238651.

    Structurei

    Secondary structure

    1
    483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi66 – 716
    Beta strandi82 – 876
    Beta strandi93 – 1019
    Beta strandi107 – 1159
    Turni124 – 1263
    Beta strandi131 – 1333
    Helixi141 – 1444
    Beta strandi147 – 1504
    Beta strandi164 – 17411
    Beta strandi181 – 19212
    Beta strandi197 – 2037
    Beta strandi206 – 2127
    Beta strandi214 – 2163
    Beta strandi221 – 2255
    Helixi235 – 2417
    Turni242 – 2443
    Beta strandi246 – 2505
    Beta strandi253 – 2553
    Beta strandi263 – 2664
    Helixi267 – 27812
    Beta strandi286 – 2938
    Helixi295 – 30612
    Beta strandi310 – 3178
    Beta strandi324 – 3296
    Beta strandi332 – 3343
    Helixi341 – 3433
    Beta strandi348 – 3503
    Helixi364 – 3696
    Helixi373 – 3753
    Beta strandi378 – 3858
    Helixi393 – 40614
    Beta strandi413 – 4175
    Helixi450 – 47122

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HLKX-ray2.10A/B46-483[»]
    ProteinModelPortaliP49753.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49753.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi481 – 4833Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the C/M/P thioester hydrolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOGENOMiHOG000116219.
    HOVERGENiHBG000331.
    InParanoidiP49753.
    KOiK01068.
    OMAiQWSLKSS.
    PhylomeDBiP49753.
    TreeFamiTF314911.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR016662. Acyl-CoA_thioEstase_long-chain.
    IPR014940. BAAT_C.
    IPR006862. Thio_Ohase/aa_AcTrfase.
    [Graphical view]
    PfamiPF08840. BAAT_C. 1 hit.
    PF04775. Bile_Hydr_Trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
    SUPFAMiSSF53474. SSF53474. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49753-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL    50
    RQVGQIIRVP ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL 100
    RDEKGALFQA HARYRADTLG ELDLERAPAL GGSFAGLEPM GLLWALEPEK 150
    PLVRLVKRDV RTPLAVELEV LDGHDPDPGR LLCQTRHERY FLPPGVRREP 200
    VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL AGKGFAVMAL 250
    AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC 300
    LSMASFLKGI TAAVVINGSV ANVGGTLHYK GETLPPVGVN RNRIKVTKDG 350
    YADIVDVLNS PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA 400
    CKRLQAHGRR KPQIICYPET GHYIEPPYFP LCRASLHALV GSPIIWGGEP 450
    RAHAMAQVDA WKQLQTFFHK HLGGHEGTIP SKV 483
    Length:483
    Mass (Da):53,218
    Last modified:November 24, 2009 - v6
    Checksum:iFAEDD42BBBD935E4
    GO
    Isoform 2 (identifier: P49753-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: Missing.
         53-214: Missing.

    Show »
    Length:301
    Mass (Da):32,959
    Checksum:iD157DF13EAF26EC6
    GO

    Sequence cautioni

    The sequence AAC42007.1 differs from that shown. Reason: Frameshift at positions 215 and 226.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671E → V in AAZ31237. (PubMed:16940157)Curated
    Sequence conflicti167 – 1671E → V in BAA91989. (PubMed:14702039)Curated
    Sequence conflicti328 – 3281H → R in AAZ31237. (PubMed:16940157)Curated
    Sequence conflicti328 – 3281H → R in BAA91989. (PubMed:14702039)Curated
    Sequence conflicti328 – 3281H → R in BAD97355. 1 PublicationCurated
    Sequence conflicti328 – 3281H → R in AAH04436. (PubMed:15489334)Curated
    Sequence conflicti328 – 3281H → R in AAH06335. (PubMed:15489334)Curated
    Sequence conflicti328 – 3281H → R in AAH06500. (PubMed:15489334)Curated
    Sequence conflicti328 – 3281H → R in AAF97985. (PubMed:10944470)Curated
    Sequence conflicti454 – 4541A → V in AAH06335. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161R → S.
    Corresponds to variant rs11545741 [ dbSNP | Ensembl ].
    VAR_057271
    Natural varianti475 – 4751H → R.4 Publications
    Corresponds to variant rs7494 [ dbSNP | Ensembl ].
    VAR_016136

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020Missing in isoform 2. 1 PublicationVSP_012225Add
    BLAST
    Alternative sequencei53 – 214162Missing in isoform 2. 1 PublicationVSP_012226Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40401 mRNA. Translation: AAC42007.1. Frameshift.
    DQ082755 mRNA. Translation: AAZ31237.1.
    AK001939 mRNA. Translation: BAA91989.1.
    AK223635 mRNA. Translation: BAD97355.1.
    BC004436 mRNA. Translation: AAH04436.2.
    BC006335 mRNA. Translation: AAH06335.1.
    BC006500 mRNA. Translation: AAH06500.4.
    AY005822 mRNA. Translation: AAF97985.1.
    CCDSiCCDS9816.1. [P49753-1]
    PIRiJC7367.
    RefSeqiNP_006812.3. NM_006821.5. [P49753-1]
    UniGeneiHs.446685.

    Genome annotation databases

    EnsembliENST00000238651; ENSP00000238651; ENSG00000119673. [P49753-1]
    GeneIDi10965.
    KEGGihsa:10965.
    UCSCiuc001xon.5. human. [P49753-1]

    Polymorphism databases

    DMDMi269849771.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40401 mRNA. Translation: AAC42007.1 . Frameshift.
    DQ082755 mRNA. Translation: AAZ31237.1 .
    AK001939 mRNA. Translation: BAA91989.1 .
    AK223635 mRNA. Translation: BAD97355.1 .
    BC004436 mRNA. Translation: AAH04436.2 .
    BC006335 mRNA. Translation: AAH06335.1 .
    BC006500 mRNA. Translation: AAH06500.4 .
    AY005822 mRNA. Translation: AAF97985.1 .
    CCDSi CCDS9816.1. [P49753-1 ]
    PIRi JC7367.
    RefSeqi NP_006812.3. NM_006821.5. [P49753-1 ]
    UniGenei Hs.446685.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HLK X-ray 2.10 A/B 46-483 [» ]
    ProteinModelPortali P49753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116164. 3 interactions.
    MINTi MINT-5004303.
    STRINGi 9606.ENSP00000238651.

    Chemistry

    ChEMBLi CHEMBL2189135.

    Protein family/group databases

    MEROPSi S09.028.

    PTM databases

    PhosphoSitei P49753.

    Polymorphism databases

    DMDMi 269849771.

    Proteomic databases

    MaxQBi P49753.
    PRIDEi P49753.

    Protocols and materials databases

    DNASUi 10965.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238651 ; ENSP00000238651 ; ENSG00000119673 . [P49753-1 ]
    GeneIDi 10965.
    KEGGi hsa:10965.
    UCSCi uc001xon.5. human. [P49753-1 ]

    Organism-specific databases

    CTDi 10965.
    GeneCardsi GC14P074036.
    H-InvDB HIX0011795.
    HIX0172385.
    HGNCi HGNC:18431. ACOT2.
    HPAi HPA043705.
    MIMi 609972. gene.
    neXtProti NX_P49753.
    PharmGKBi PA142672653.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000116219.
    HOVERGENi HBG000331.
    InParanoidi P49753.
    KOi K01068.
    OMAi QWSLKSS.
    PhylomeDBi P49753.
    TreeFami TF314911.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04318-MONOMER.
    BRENDAi 3.1.2.2. 2681.
    SABIO-RK P49753.

    Miscellaneous databases

    EvolutionaryTracei P49753.
    GeneWikii ACOT2.
    GenomeRNAii 10965.
    NextBioi 41670.
    PROi P49753.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49753.
    Bgeei P49753.
    CleanExi HS_ACOT2.
    Genevestigatori P49753.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR016662. Acyl-CoA_thioEstase_long-chain.
    IPR014940. BAAT_C.
    IPR006862. Thio_Ohase/aa_AcTrfase.
    [Graphical view ]
    Pfami PF08840. BAAT_C. 1 hit.
    PF04775. Bile_Hydr_Trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016521. Acyl-CoA_hydro. 1 hit.
    SUPFAMi SSF53474. SSF53474. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs."
      Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.
      FASEB J. 20:1855-1864(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "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] (ISOFORM 1), VARIANT ARG-475.
      Tissue: Placenta.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
      Tissue: Spleen.
    5. "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] (ISOFORM 1), VARIANT ARG-475.
      Tissue: Lung and Uterus.
    6. "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase."
      Jones J.M., Gould S.J.
      Biochem. Biophys. Res. Commun. 275:233-240(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-483 (ISOFORM 1), FUNCTION, VARIANT ARG-475.

    Entry informationi

    Entry nameiACOT2_HUMAN
    AccessioniPrimary (citable) accession number: P49753
    Secondary accession number(s): Q3I5F8, Q53EK4, Q9NUX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 6 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

    Caution

    Was originally (PubMed:10944470) thought to be peroxisomal but was later shown (PubMed:16940157) to be mitochondrial.2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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

    External Data

    Dasty 3