Tars3 Gene Summary [Rat]
Predicted to enable threonine-tRNA ligase activity. Predicted to be involved in threonyl-tRNA aminoacylation. Predicted to be located in cytoplasm and nucleus. Predicted to be active in mitochondrion. Orthologous to human TARS3 (threonyl-tRNA synthetase 3). [provided by Alliance of Genome Resources, Apr 2025]
Details
| Type | Protein Coding |
| Official Symbol | Tars3 |
| Official Name | threonyl-tRNA synthetase 3 [Source:RGD Symbol;Acc:1311308] |
| Ensembl ID | ENSRNOG00000024460 |
| Bio databases IDs | |
| Aliases | threonyl-tRNA synthetase 3 |
| Synonyms | A530046H20Rik, LOC108349769, RGD1311308, TARSL2, threonyl-tRNA synthetase 3, ThrRS-L |
| Species | Rat, Rattus norvegicus |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Tars3 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- threonine-tRNA ligase
- tRNA synthetase class II core domain (G, H, P, S and T)
- HGTP_anticodon
- threonyl-tRNA synthetase
- TGS domain
- class_II_aaRS-like_core
- Anticodon binding domain
- Ubl1_cv_Nsp3_N-like
- Threonyl and Alanyl tRNA synthetase second additional domain
- enzyme
- protein binding
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Cytoplasm
- Nucleus
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Tars3 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- threonyl-tRNA aminoacylation
Cellular Component
Where in the cell the gene product is active
- nucleus
- cytoplasm
Molecular Function
What the gene product does at the molecular level
- ATP binding
- identical protein binding
- protein binding
- threonine-tRNA ligase activity