A0A8P0SDL0 · A0A8P0SDL0_CANLF
- ProteinADAM metallopeptidase with thrombospondin type 1 motif 5
- GeneADAMTS5
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids934 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 213 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 274 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 274 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 357 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 357 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 364 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 414 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 415 | ||||
Binding site | 418 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 424 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 475 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 478 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 478 | Ca2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular region | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | extracellular matrix organization | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionA0A8P0SDL0
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-20 | ||||
Chain | PRO_5039933770 | 21-934 | |||
Disulfide bond | 346↔398 | ||||
Disulfide bond | 375↔380 | ||||
Disulfide bond | 392↔475 | ||||
Disulfide bond | 430↔459 | ||||
Disulfide bond | 501↔523 | ||||
Glycosylation | 502 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 512↔533 | ||||
Disulfide bond | 518↔552 | ||||
Disulfide bond | 546↔557 | ||||
Disulfide bond | 583↔620 | ||||
Disulfide bond | 587↔625 | ||||
Disulfide bond | 598↔610 | ||||
Glycosylation | 732 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 20-71 | Disordered | |||
Region | 207-259 | Disordered | |||
Compositional bias | 213-252 | Pro residues | |||
Domain | 271-480 | Peptidase M12B | |||
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length934
- Mass (Da)101,775
- Last updated2023-06-28 v1
- Checksum3209D009F8AFEB92
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 213-252 | Pro residues | |||