Lctl Gene Summary [Rat]
Predicted to enable hydrolase activity, hydrolyzing O-glycosyl compounds. Predicted to be involved in lens morphogenesis in camera-type eye. Predicted to be located in brush border and endoplasmic reticulum. Orthologous to human LCTL (lactase like). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Lctl |
| Official Name | lactase-like [Source:RGD Symbol;Acc:1305177] |
| Ensembl ID | ENSRNOG00000009193 |
| Bio databases IDs | |
| Aliases | lactase-like |
| Synonyms | E130104I05Rik, KLG, KLPH, lactase-like |
| 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 Lctl often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- enzyme
- Glycosyl hydrolase family 1
- beta-galactosidase
- Glycosyl hydrolases
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
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
- cellular membrane
- Endoplasmic Reticulum
- brush border
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Lctl gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- carbohydrate metabolic process
- visual perception
- lens morphogenesis in camera-type eye
Cellular Component
Where in the cell the gene product is active
- endoplasmic reticulum membrane
- brush border
Molecular Function
What the gene product does at the molecular level
- beta-glucosidase activity