Reviewed,
UniProtKB/Swiss-Prot Q86TX2 (ACOT1_HUMAN)
Last modified
November 3, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Acyl-coenzyme A thioesterase 1 Short name=Acyl-CoA thioesterase 1 EC=3.1.2.2 Alternative name(s): Inducible cytosolic acyl-coenzyme A thioester hydrolase Long chain acyl-CoA thioester hydrolase Short name=Long chain acyl-CoA hydrolase CTE-I CTE-Ib | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 421 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. Active towards fatty acyl-CoA with chain-lengths of C12-C16 By similarity. |
| Catalytic activity | Palmitoyl-CoA + H2O = CoA + palmitate. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the C/M/P thioester hydrolase family. |
| Biophysicochemical properties | Kinetic parameters: KM=35.8 µM for C10-acyl-CoA KM=3.6 µM for C12-acyl-CoA KM=2.8 µM for C14-acyl-CoA KM=3.6 µM for C16-acyl-CoA KM=2.4 µM for C18-acyl-CoA KM=2 µM for C20-acyl-CoA KM=2.4 µM for C16:1-acyl-CoA KM=4.1 µM for C18:1-acyl-CoA KM=2.1 µM for C18:1-trans-acyl-CoA Vmax=224 nmol/min/mg enzyme toward C10-acyl-CoA Vmax=700 nmol/min/mg enzyme toward C12-acyl-CoA Vmax=912 nmol/min/mg enzyme toward C14-acyl-CoA Vmax=691 nmol/min/mg enzyme toward C16-acyl-CoA Vmax=597 nmol/min/mg enzyme toward C18-acyl-CoA Vmax=520 nmol/min/mg enzyme toward C20-acyl-CoA Vmax=577 nmol/min/mg enzyme toward C16:1-acyl-CoA Vmax=258 nmol/min/mg enzyme toward C18:1-acyl-CoA Vmax=309 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| Molecular function | Hydrolase Serine esterase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | acyl-CoA metabolic process Ref.1 Inferred from direct assay. Source: HGNC long-chain fatty acid metabolic process Ref.1Inferred from direct assay. Source: HGNC very-long-chain fatty acid metabolic process Ref.1Inferred from direct assay. Source: HGNC |
| Cellular component | cytosol Ref.1 Inferred from direct assay. Source: HGNC |
| Molecular function | carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-CoA hydrolase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 421 | 421 | Acyl-coenzyme A thioesterase 1 | PRO_0000202155 | |||||
Sites | |||||||||
| Active site | 232 | 1 | Charge relay system By similarity | ||||||
| Active site | 326 | 1 | Charge relay system By similarity | ||||||
| Active site | 360 | 1 | Charge relay system By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 266 | 1 | R → H: dbSNP rs1049568. | VAR_059830 | |||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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: 16940157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. |
| [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. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| DQ082754 mRNA. Translation: AAZ31236.1. BX161396 mRNA. Translation: CAD61883.1. BC127748 mRNA. Translation: AAI27749.1. BC132889 mRNA. Translation: AAI32890.1. BC132891 mRNA. Translation: AAI32892.1. BC143042 mRNA. Translation: AAI43043.1. | |
| IPI | IPI00333838. |
| RefSeq | NP_001032238.1. |
| UniGene | Hs.568046 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q86TX2. |
PTM databases | |
| PhosphoSite | Q86TX2. |
Proteomic databases | |
| PRIDE | Q86TX2. |
Genome annotation databases | |
| Ensembl | ENST00000311148; ENSP00000311224; ENSG00000184227; Homo sapiens. [Genome view] |
| GeneID | 641371. |
| KEGG | hsa:641371. |
| UCSC | uc001xol.1. human. |
Organism-specific databases | |
| CTD | 641371. |
| GeneCards | GC14P073074. |
| HGNC | HGNC:33128. ACOT1. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q86TX2. |
| HOVERGEN | Q86TX2. |
| OMA | LEPAGGC. |
Enzyme and pathway databases | |
| BRENDA | 3.1.2.2. 247. |
Gene expression databases | |
| Bgee | Q86TX2. |
| CleanEx | HS_ACOT1. |
| Genevestigator | Q86TX2. |
| GermOnline | ENSG00000184227. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR016662. Acyl-CoA_thioEstase_long-chain. IPR014940. BAAT_C. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view] |
| Pfam | PF08840. BAAT_C. 1 hit. PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view] |
| PIRSF | PIRSF016521. Acyl-CoA_hydro. 1 hit. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 113125. |
Entry information
| Entry name | ACOT1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q86TX2 Secondary accession number(s): A1L173, Q3I5F9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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 14 Human chromosome 14: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| SIMILARITY comments Index of protein domains and families |

Clusters with


