Prodh2 Gene Summary [Rat]
Predicted to enable FAD binding activity and proline dehydrogenase activity. Predicted to be involved in proline catabolic process to glutamate. Predicted to be active in mitochondrion. Orthologous to human PRODH2 (proline dehydrogenase 2). [provided by Alliance of Genome Resources, Apr 2025]
Details
| Type | Protein Coding |
| Official Symbol | Prodh2 |
| Official Name | proline dehydrogenase 2 [Source:RGD Symbol;Acc:1306761] |
| Ensembl ID | ENSRNOG00000057578 |
| Bio databases IDs | |
| Aliases | proline dehydrogenase 2 |
| Synonyms | 2510028N04Rik, 2510038B11Rik, HSPOX1, HYPDH, MmPOX, MmPOX1, POX1, proline dehydrogenase 2, proline dehydrogenase (oxidase) 2 |
| 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 Prodh2 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- proline dehydrogenase
- enzyme
- CH-NH group oxidoreductase
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
- mitochondrial inner membrane
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Prodh2 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- proline catabolic process
- proline catabolic process to glutamate
Cellular Component
Where in the cell the gene product is active
- mitochondrion
- mitochondrial inner membrane
Molecular Function
What the gene product does at the molecular level
- oxidoreductase activity, acting on the CH-NH group of donors
- FAD binding
- proline dehydrogenase activity