Adamts5 Gene Summary [Rat]
Predicted to enable several functions, including heparin binding activity; identical protein binding activity; and metalloendopeptidase activity. Predicted to be involved in several processes, including heart development; myoblast fusion; and negative regulation of cold-induced thermogenesis. Predicted to act upstream of or within defense response to bacterium. Predicted to be located in extracellular space. Predicted to be active in extracellular matrix. Used to study osteoarthritis. Biomarker of degenerative disc disease; mucopolysaccharidosis VI; and osteoarthritis. Human ortholog(s) of this gene implicated in osteoarthritis. Orthologous to human ADAMTS5 (ADAM metallopeptidase with thrombospondin type 1 motif 5). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Adamts5 |
| Official Name | ADAM metallopeptidase with thrombospondin type 1 motif, 5 [Source:RGD Symbol;Acc:735196] |
| Ensembl ID | ENSRNOG00000057794 |
| Bio databases IDs | |
| Aliases | ADAM metallopeptidase with thrombospondin type 1 motif, 5 |
| Synonyms | 9530092O11RIK, ADAM metallopeptidase with thrombospondin type 1 motif 5, ADAM metallopeptidase with thrombospondin type 1 motif, 5, ADAMTS1, ADAM-TS 11, ADMP-2, ASMP-2, LOC107987291 |
| 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 Adamts5 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- Thrombospondin type 1 repeats
- Thrombospondin type 1 domain
- Reprolysin family propeptide
- thrombospondin type 1 repeat
- catalytic domain
- ADAMTS cysteine-rich domain 2
- extracellular matrix binding
- ADAMTS cysteine-rich domain
- peptidase
- protein binding
- identical protein binding
- disintergrin domain
- metallopeptidase
- ADAM-TS Spacer 1
- ZnMc
- endopeptidase
- Metallo-peptidase family M12B Reprolysin-like
- integrin binding
- Reprolysin (M12B) family zinc metalloprotease
- disintegrin-like domain
- Spondin-like TSP1 domain
- heparin binding
- metalloendopeptidase
Pathways
Biological processes and signaling networks where the Adamts5 gene in rat plays a role, providing insight into its function and relevance in health or disease.
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- cancer
- lung adenocarcinoma
- lung adenocarcinoma formation
- osteoarthritis
- aortic valve calcification
- major depression
- breast carcinoma
- degenerative disc disease
- glioblastoma
- glioblastoma cancer
role in cell
- accumulation
- expression in
- accumulation in
- signaling in
- growth
- quantity
- contractility
- motility
- fusion
- endocytosis by
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Extracellular Space
- endoplasmic reticulum lumen
- extracellular matrix
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Adamts5 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- endocardial cushion morphogenesis
- aortic valve morphogenesis
- extracellular matrix disassembly
- proteolysis
- pulmonary valve morphogenesis
- extracellular matrix organization
- myoblast fusion
- defense response to bacterium
Cellular Component
Where in the cell the gene product is active
- endoplasmic reticulum lumen
- extracellular space
- extracellular matrix
- extracellular region
Molecular Function
What the gene product does at the molecular level
- extracellular matrix binding
- zinc ion binding
- identical protein binding
- protein binding
- endopeptidase activity
- heparin binding
- integrin binding
- peptidase activity
- metalloendopeptidase activity
- metallopeptidase activity