A0A974HXJ5 · A0A974HXJ5_XENLA
- ProteinPeptidase M12B domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids928 (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 | 169 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 211 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 211 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 294 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 294 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 301 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 351 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 352 | ||||
Binding site | 355 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 361 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 412 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 415 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 415 | Ca2+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 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
- Recommended namePeptidase M12B domain-containing protein
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionA0A974HXJ5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-22 | ||||
Chain | PRO_5036823464 | 23-928 | Peptidase M12B domain-containing protein | ||
Disulfide bond | 283↔335 | ||||
Disulfide bond | 312↔317 | ||||
Disulfide bond | 329↔412 | ||||
Disulfide bond | 367↔396 | ||||
Disulfide bond | 438↔461 | ||||
Disulfide bond | 449↔471 | ||||
Disulfide bond | 456↔490 | ||||
Disulfide bond | 484↔495 | ||||
Disulfide bond | 521↔558 | ||||
Disulfide bond | 525↔563 | ||||
Disulfide bond | 536↔548 | ||||
Glycosylation | 670 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 167-202 | Disordered | |||
Compositional bias | 179-202 | Polar residues | |||
Domain | 208-417 | Peptidase M12B | |||
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length928
- Mass (Da)102,180
- Last updated2023-02-22 v1
- ChecksumDE2FA6C25A238341
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 179-202 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM004468 EMBL· GenBank· DDBJ | OCT93860.1 EMBL· GenBank· DDBJ | Genomic DNA |