Q9NPJ3 (ACO13_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acyl-coenzyme A thioesterase 13 Short name=Acyl-CoA thioesterase 13 EC=3.1.2.- Alternative name(s): Thioesterase superfamily member 2 | ||||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 140 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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 and 3,4-dihydrohyphenylacetyl-CoA (in vitro). Ref.7 Ref.8 |
| Subunit structure | |
| Subcellular location | Cytoplasm By similarity. Mitochondrion By similarity. |
| Sequence similarities | Belongs to the thioesterase PaaI family. |
| Biophysicochemical properties | Kinetic parameters: KM=4.9 µM for n-decanoyl-CoA Ref.8 KM=26 µM for n-octanoyl-CoA KM=5 µM for myristoyl-CoA KM=9 µM for palmitoyl-CoA KM=9 µM for oleoyl-CoA KM=10 µM for 3,4-dihydrohyphenylacetyl-CoA KM=40 µM for 3-hydrohyphenylacetyl-CoA |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Mitochondrion |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | protein homotetramerization Inferred from physical interaction Ref.7Ref.8. Source: UniProtKB |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acyl-CoA hydrolase activity Inferred from direct assay Ref.7Ref.8. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 140 | 140 | Acyl-coenzyme A thioesterase 13 | PRO_0000156697 | ||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||
| Binding site | 50 | 1 | Substrate | |||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||
| Mutagenesis | 50 | 1 | N → A: Reduced activity. Ref.8 | |||||||||||||||||||||||||||||||
| Mutagenesis | 56 | 1 | H → A: Decreases affinity for substrate. Ref.8 | |||||||||||||||||||||||||||||||
| Mutagenesis | 65 | 1 | D → A: Loss of activity. Ref.7 Ref.8 | |||||||||||||||||||||||||||||||
| Mutagenesis | 65 | 1 | D → E or N: Reduced activity. Ref.7 Ref.8 | |||||||||||||||||||||||||||||||
| Mutagenesis | 83 | 1 | S → A: Reduced activity. Ref.8 | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Helix | 4 – 17 | 14 | ||||||||||||||||||||||||||||||||
| Helix | 21 – 25 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 29 – 34 | 6 | ||||||||||||||||||||||||||||||||
| Beta strand | 37 – 43 | 7 | ||||||||||||||||||||||||||||||||
| Helix | 46 – 48 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 53 – 55 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 57 – 73 | 17 | ||||||||||||||||||||||||||||||||
| Beta strand | 75 – 77 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 82 – 90 | 9 | ||||||||||||||||||||||||||||||||
| Beta strand | 99 – 109 | 11 | ||||||||||||||||||||||||||||||||
| Beta strand | 111 – 122 | 12 | ||||||||||||||||||||||||||||||||
| Turn | 123 – 125 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 128 – 137 | 10 | ||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland and Hypothalamus. |
| [2] | "Human acute promyelocytic leukemia cell line NB4's apoptosis related genes." Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Promyelocytic leukemia. |
| [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | "The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix. |
| [6] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [7] | "Crystal structure of human thioesterase superfamily member 2." Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D., Gong W. Biochem. Biophys. Res. Commun. 349:172-177(2006) [PubMed: 16934754] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT. |
| [8] | "The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis." Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D. Biochemistry 48:1293-1304(2009) [PubMed: 19170545] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT. |
| [9] | "The crystal structure of human thioesterase superfamily member 2." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF155649 mRNA. Translation: AAF67006.1. AF220186 mRNA. Translation: AAF67651.1. AF274952 mRNA. Translation: AAK07529.1. AK000508 mRNA. Translation: BAA91215.1. AL031775 Genomic DNA. Translation: CAD92509.1. BC000894 mRNA. Translation: AAH00894.1. | ||||||||||||||||||||||||
| IPI | IPI00020530. | ||||||||||||||||||||||||
| RefSeq | NP_060943.1. NM_018473.3. | ||||||||||||||||||||||||
| UniGene | Hs.727546. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q9NPJ3. | ||||||||||||||||||||||||
| SMR | Q9NPJ3. Positions 2-139. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | Q9NPJ3. 2 interactions. | ||||||||||||||||||||||||
| STRING | Q9NPJ3. | ||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||
| DMDM | 23396822. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PeptideAtlas | Q9NPJ3. | ||||||||||||||||||||||||
| PRIDE | Q9NPJ3. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000230048; ENSP00000230048; ENSG00000112304. | ||||||||||||||||||||||||
| GeneID | 55856. | ||||||||||||||||||||||||
| KEGG | hsa:55856. | ||||||||||||||||||||||||
| UCSC | uc003nek.1. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 55856. | ||||||||||||||||||||||||
| GeneCards | GC06P024667. | ||||||||||||||||||||||||
| H-InvDB | HIX0005626. | ||||||||||||||||||||||||
| HGNC | HGNC:20999. ACOT13. | ||||||||||||||||||||||||
| HPA | HPA019881. | ||||||||||||||||||||||||
| neXtProt | NX_Q9NPJ3. | ||||||||||||||||||||||||
| PharmGKB | PA128394691. PA165617655. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | prNOG20053. | ||||||||||||||||||||||||
| GeneTree | ENSGT00390000013934. | ||||||||||||||||||||||||
| InParanoid | Q9NPJ3. | ||||||||||||||||||||||||
| OMA | MKVEEQH. | ||||||||||||||||||||||||
| OrthoDB | EOG4SQWZ8. | ||||||||||||||||||||||||
| PhylomeDB | Q9NPJ3. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | Q9NPJ3. | ||||||||||||||||||||||||
| Bgee | Q9NPJ3. | ||||||||||||||||||||||||
| CleanEx | HS_THEM2. | ||||||||||||||||||||||||
| Genevestigator | Q9NPJ3. | ||||||||||||||||||||||||
| GermOnline | ENSG00000112304. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR003736. PAAI. IPR006683. Thioestr_supf. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF03061. 4HBT. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| TIGRFAMs | TIGR00369. Unchar_dom_1. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| NextBio | 61135. | ||||||||||||||||||||||||
Entry information
| Entry name | ACO13_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NPJ3 Secondary accession number(s): O95549 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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