A0A5N4DQ20 · A0A5N4DQ20_CAMDR
- Protein72 kDa type IV collagenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids661 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
Cofactor
Protein has several cofactor binding sites:
Note: Can bind about 5 Ca2+ ions per subunit.
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 103 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 135 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 169 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 179 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 181 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 186 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 187 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 191 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 194 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 203 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 205 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 207 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 209 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 210 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 212 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 212 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Active site | 232 | ||||
Active site | 405 | ||||
Binding site | 477 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 479 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 522 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 572 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 619 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 621 | Ca2+ 5 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | collagen catabolic process | |
Biological Process | extracellular matrix organization | |
Biological Process | proteolysis | |
Biological Process | response to hypoxia | |
Biological Process | tissue remodeling |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name72 kDa type IV collagenase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Tylopoda > Camelidae > Camelus
Accessions
- Primary accessionA0A5N4DQ20
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-30 | ||||
Chain | PRO_5024278471 | 31-661 | 72 kDa type IV collagenase | ||
Disulfide bond | 234↔260 | ||||
Disulfide bond | 248↔275 | ||||
Disulfide bond | 292↔318 | ||||
Disulfide bond | 306↔333 | ||||
Disulfide bond | 350↔376 | ||||
Disulfide bond | 364↔391 | ||||
Disulfide bond | 470↔661 | ||||
Modified residue | 553 | Phosphotyrosine; by PKDCC | |||
Keywords
- PTM
Interaction
Subunit
Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Motif | 101-108 | Cysteine switch | |||
Domain | 229-277 | Fibronectin type-II | |||
Domain | 287-335 | Fibronectin type-II | |||
Domain | 345-393 | Fibronectin type-II | |||
Repeat | 473-517 | Hemopexin | |||
Repeat | 518-564 | Hemopexin | |||
Repeat | 566-614 | Hemopexin | |||
Repeat | 615-661 | Hemopexin | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length661
- Mass (Da)73,834
- Last updated2020-02-26 v1
- Checksum9F7507B4371E1846
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JWIN03000009 EMBL· GenBank· DDBJ | KAB1273157.1 EMBL· GenBank· DDBJ | Genomic DNA |