Gulo Gene Summary [Mouse]
Enables L-gulonolactone oxidase activity and flavin adenine dinucleotide binding activity. Involved in L-ascorbic acid biosynthetic process. Predicted to be located in endoplasmic reticulum membrane. Is expressed in several structures, including cranium; liver; nasal septum; nervous system; and pancreas. Orthologous to human GULOP (gulonolactone (L-) oxidase, pseudogene). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Gulo |
| Official Name | gulonolactone (L-) oxidase [Source:MGI Symbol;Acc:MGI:1353434] |
| Ensembl ID | ENSMUSG00000034450 |
| Bio databases IDs | |
| Aliases | gulonolactone (L-) oxidase |
| Synonyms | 5730581M22, AU018375, D-Arabino-1,4-lactone oxidase (GULO) similar, GLO, gulonolactone (L-) oxidase, LGO, L-gulono-gamma-lactone oxidase, L-Gulonolactone oxidase, L-gulono-γ-lactone oxidase, LOC100505222, sfx, unh, unhip |
| Species | Mouse, Mus musculus |
| 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 mouse Gulo often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- plant-specific FAD-dependent oxidoreductase
- D-arabinono-1,4-lactone oxidase
- FAD binding domain
- flavin adenine dinucleotide binding
- galactonolactone dehydrogenase
- enzyme
- L-gulonolactone oxidase
- FAD-linked oxidoreductase
- sugar 1,4-lactone oxidases
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- weight loss
- bleeding
- rachitic rosary
- anemia
- hemarthrosis
- growth failure
- desquamation
role in cell
- proliferation
- expression in
- number
- survival
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
- microsomal membrane