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Q8N9L9

- ACOT4_HUMAN

UniProt

Q8N9L9 - ACOT4_HUMAN

Protein

Acyl-coenzyme A thioesterase 4

Gene

ACOT4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      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 By similarity. Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs.By similarity

    Catalytic activityi

    Palmitoyl-CoA + H2O = CoA + palmitate.

    Kineticsi

    1. KM=14 µM for succinyl-CoA1 Publication
    2. KM=147 µM for glutaryl-CoA1 Publication
    3. KM=3.4 µM for C14-acyl-CoA1 Publication

    Vmax=581 nmol/min/mg enzyme toward succinyl-CoA1 Publication

    Vmax=132 nmol/min/mg enzyme toward glutaryl-CoA1 Publication

    Vmax=137 nmol/min/mg enzyme toward C14-acyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321Charge relay systemBy similarity
    Active sitei326 – 3261Charge relay systemBy similarity
    Active sitei360 – 3601Charge relay systemBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. acyl-CoA metabolic process Source: HGNC
    2. dicarboxylic acid catabolic process Source: UniProtKB
    3. dicarboxylic acid metabolic process Source: HGNC
    4. long-chain fatty acid metabolic process Source: HGNC
    5. saturated monocarboxylic acid metabolic process Source: HGNC
    6. short-chain fatty acid metabolic process Source: HGNC
    7. succinyl-CoA metabolic process Source: HGNC
    8. unsaturated monocarboxylic acid metabolic process Source: HGNC
    9. very long-chain fatty acid metabolic process Source: HGNC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS16863-MONOMER.
    SABIO-RKQ8N9L9.

    Protein family/group databases

    MEROPSiS09.029.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 4 (EC:3.1.2.2)
    Short name:
    Acyl-CoA thioesterase 4
    Alternative name(s):
    PTE-2b
    Peroxisomal acyl coenzyme A thioester hydrolase Ib
    Peroxisomal long-chain acyl-CoA thioesterase Ib
    Short name:
    PTE-Ib
    Gene namesi
    Name:ACOT4
    Synonyms:PTE2B, PTEIB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:19748. ACOT4.

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672654.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 421421Acyl-coenzyme A thioesterase 4PRO_0000202149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei313 – 3131N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ8N9L9.
    PaxDbiQ8N9L9.
    PRIDEiQ8N9L9.

    PTM databases

    PhosphoSiteiQ8N9L9.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ8N9L9.
    CleanExiHS_ACOT4.
    GenevestigatoriQ8N9L9.

    Organism-specific databases

    HPAiHPA000779.

    Interactioni

    Protein-protein interaction databases

    BioGridi125809. 1 interaction.
    STRINGi9606.ENSP00000323071.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi20 – 256
    Beta strandi31 – 399
    Beta strandi45 – 539
    Turni62 – 643
    Beta strandi69 – 724
    Helixi79 – 824
    Beta strandi85 – 884
    Beta strandi102 – 11211
    Beta strandi119 – 13012
    Beta strandi135 – 1417
    Beta strandi144 – 1507
    Beta strandi152 – 1543
    Beta strandi159 – 1635
    Helixi173 – 1797
    Turni180 – 1823
    Beta strandi184 – 1896
    Beta strandi191 – 1933
    Helixi206 – 21611
    Beta strandi224 – 2318
    Helixi233 – 24412
    Beta strandi246 – 25510
    Beta strandi265 – 2673
    Beta strandi270 – 2723
    Helixi279 – 2813
    Helixi302 – 3043
    Helixi311 – 3133
    Beta strandi318 – 3236
    Beta strandi327 – 3293
    Helixi331 – 34414
    Beta strandi351 – 3555
    Beta strandi372 – 3754
    Turni376 – 3794
    Beta strandi380 – 3834
    Helixi388 – 40922

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3K2IX-ray2.40A/B1-421[»]
    ProteinModelPortaliQ8N9L9.
    SMRiQ8N9L9. Positions 3-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N9L9.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi419 – 4213Microbody targeting signalSequence Analysis

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1073.
    HOGENOMiHOG000116219.
    HOVERGENiHBG000331.
    InParanoidiQ8N9L9.
    KOiK01068.
    OMAiCPASLHR.
    OrthoDBiEOG75TMC9.
    PhylomeDBiQ8N9L9.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q8N9L9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSATLILEPP GRCCWNEPVR IAVRGLAPEQ RVTLRASLRD EKGALFRAHA    50
    RYCADARGEL DLERAPALGG SFAGLEPMGL LWALEPEKPF WRFLKRDVQI 100
    PFVVELEVLD GHDPEPGRLL CQAQHERHFL PPGVRRQSVR AGRVRATLFL 150
    PPGPGPFPGI IDIFGIGGGL LEYRASLLAG HGFATLALAY YNFEDLPNNM 200
    DNISLEYFEE AVCYMLQHPQ VKGPGIGLLG ISLGADICLS MASFLKNVSA 250
    TVSINGSGIS GNTAINYKHS SIPPLGYDLR RIKVAFSGLV DIVDIRNALV 300
    GGYKNPSMIP IEKAQGPILL IVGQDDHNWR SELYAQTVSE RLQAHGKEKP 350
    QIICYPGTGH YIEPPYFPLC PASLHRLLNK HVIWGGEPRA HSKAQEDAWK 400
    QILAFFCKHL GGTQKTAVPK L 421
    Length:421
    Mass (Da):46,327
    Last modified:July 19, 2004 - v2
    Checksum:i41BBE5AA826A9F2C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301L → P in BAC04313. (PubMed:14702039)Curated
    Sequence conflicti187 – 1904ALAY → DLQS in BAC04313. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571R → C.1 Publication
    Corresponds to variant rs3742819 [ dbSNP | Ensembl ].
    VAR_052300
    Natural varianti187 – 1871A → D.
    Corresponds to variant rs35724886 [ dbSNP | Ensembl ].
    VAR_052301

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK094223 mRNA. Translation: BAC04313.1.
    AK055797 mRNA. Translation: BAB71017.1.
    BX248023 mRNA. Translation: CAD62346.1.
    BX248047 mRNA. Translation: CAD62354.1.
    BC031799 mRNA. Translation: AAH31799.2.
    BC090945 mRNA. Translation: AAH90945.1.
    BC117341 mRNA. Translation: AAI17342.1.
    BC117343 mRNA. Translation: AAI17344.1.
    CCDSiCCDS9817.1.
    RefSeqiNP_689544.3. NM_152331.3.
    UniGeneiHs.49433.

    Genome annotation databases

    EnsembliENST00000326303; ENSP00000323071; ENSG00000177465.
    GeneIDi122970.
    KEGGihsa:122970.
    UCSCiuc001xoo.3. human.

    Polymorphism databases

    DMDMi50401071.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK094223 mRNA. Translation: BAC04313.1 .
    AK055797 mRNA. Translation: BAB71017.1 .
    BX248023 mRNA. Translation: CAD62346.1 .
    BX248047 mRNA. Translation: CAD62354.1 .
    BC031799 mRNA. Translation: AAH31799.2 .
    BC090945 mRNA. Translation: AAH90945.1 .
    BC117341 mRNA. Translation: AAI17342.1 .
    BC117343 mRNA. Translation: AAI17344.1 .
    CCDSi CCDS9817.1.
    RefSeqi NP_689544.3. NM_152331.3.
    UniGenei Hs.49433.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3K2I X-ray 2.40 A/B 1-421 [» ]
    ProteinModelPortali Q8N9L9.
    SMRi Q8N9L9. Positions 3-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125809. 1 interaction.
    STRINGi 9606.ENSP00000323071.

    Protein family/group databases

    MEROPSi S09.029.

    PTM databases

    PhosphoSitei Q8N9L9.

    Polymorphism databases

    DMDMi 50401071.

    Proteomic databases

    MaxQBi Q8N9L9.
    PaxDbi Q8N9L9.
    PRIDEi Q8N9L9.

    Protocols and materials databases

    DNASUi 122970.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326303 ; ENSP00000323071 ; ENSG00000177465 .
    GeneIDi 122970.
    KEGGi hsa:122970.
    UCSCi uc001xoo.3. human.

    Organism-specific databases

    CTDi 122970.
    GeneCardsi GC14P074058.
    H-InvDB HIX0202062.
    HGNCi HGNC:19748. ACOT4.
    HPAi HPA000779.
    MIMi 614314. gene.
    neXtProti NX_Q8N9L9.
    PharmGKBi PA142672654.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1073.
    HOGENOMi HOG000116219.
    HOVERGENi HBG000331.
    InParanoidi Q8N9L9.
    KOi K01068.
    OMAi CPASLHR.
    OrthoDBi EOG75TMC9.
    PhylomeDBi Q8N9L9.
    TreeFami TF314911.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS16863-MONOMER.
    SABIO-RK Q8N9L9.

    Miscellaneous databases

    EvolutionaryTracei Q8N9L9.
    GeneWikii ACOT4.
    GenomeRNAii 122970.
    NextBioi 81045.
    PROi Q8N9L9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8N9L9.
    CleanExi HS_ACOT4.
    Genevestigatori Q8N9L9.

    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. "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].
      Tissue: Cerebellum and Kidney.
    2. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Neuroblastoma and Placenta.
    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 CYS-57.
      Tissue: Colon and Urinary bladder.
    4. "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: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiACOT4_HUMAN
    AccessioniPrimary (citable) accession number: Q8N9L9
    Secondary accession number(s): Q17RF4
    , Q5BKT6, Q86TX0, Q86TX1, Q96N88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 103 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

    Miscellaneous

    Human ACOT4 may have acquired the combined activities of mouse ACOT3, ACOT4, and ACOT5.

    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