Gene
acot13
- ID
- ZDB-GENE-060503-437
- Name
- acyl-CoA thioesterase 13
- Symbol
- acot13 Nomenclature History
- Previous Names
-
- si:dkey-218n20.4
- them2
- Type
- protein_coding_gene
- Location
- Chr: 19 Mapping Details/Browsers
- Description
- Enables long-chain fatty acyl-CoA hydrolase activity. Orthologous to human ACOT13 (acyl-CoA thioesterase 13).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Yu et al., 2015
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- 1 Figure from Yu et al., 2015
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
Human Disease
Domain, Family, and Site Summary
Domain Details Per Protein
Protein | Additional Resources | Length | Acyl-coenzyme A thioesterase 13 | HotDog domain superfamily | Phenylacetic acid degradation-related domain | Thioesterase domain |
---|---|---|---|---|---|---|
UniProtKB:F6P1Y9 | InterPro PDB | 146 | ||||
UniProtKB:Q1LWU4 | InterPro | 144 |
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Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
---|---|---|---|---|---|
mRNA |
acot13-201
(1)
|
Ensembl | 505 nt | ||
mRNA |
acot13-202
(1)
|
Ensembl | 580 nt |
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Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Contained in | BAC | DKEY-218N20 | ZFIN Curated Data |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_001080803 (1) | 505 nt | ||
Genomic | GenBank:BX511258 (1) | 200076 nt | ||
Polypeptide | UniProtKB:F6P1Y9 (1) | 146 aa |
- Anticevic, I., Otten, C., Popovic, M. (2024) Tyrosyl-DNA phosphodiesterase 2 (Tdp2) repairs DNA-protein crosslinks and protects against double strand breaks in vivo. Frontiers in cell and developmental biology. 12:13945311394531
- Bayés, À., Collins, M.O., Reig-Viader, R., Gou, G., Goulding, D., Izquierdo, A., Choudhary, J.S., Emes, R.D., Grant, S.G. (2017) Evolution of complexity in the zebrafish synapse proteome. Nature communications. 8:14613
- Yu, S., Li, H., Gao, F., Zhou, Y. (2015) Crystal structure and potential physiological role of zebra fish thioesterase superfamily member 2 (fTHEM2). Biochemical and Biophysical Research Communications. 463:912-6
- Li, H., Gao, F., Yu, S., Jia, M., and Gong, W. (2012) Molecular cloning, expression, purification and crystallographic analysis of zebrafish THEM2. Acta crystallographica. Section F, Structural biology and crystallization communications. 68(12):1525-1528
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