A0A7J7EZ65 · A0A7J7EZ65_DICBM
- ProteinCollagenase 3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids428 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
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 | 96 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 128 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 162 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 172 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 174 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 179 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 180 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 182 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 184 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 187 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 194 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 196 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 198 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 200 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 202 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 203 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 205 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 205 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 222 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 223 | |||||
Sequence: E | ||||||
Binding site | 226 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 232 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 240 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: M | ||||||
Binding site | 291 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 293 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 335 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 337 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 389 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 391 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: V |
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 |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCollagenase 3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7EZ65
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MHPGVLAAFLFLSWTHCWS | ||||||
Chain | PRO_5029647997 | 20-428 | Collagenase 3 | |||
Sequence: LPLPNDDDDDDTSEEDFQLAERYLKSYYYPLNPAGILKKSATNSVVDRLREMQSFFGLEVTGKLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRLHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETLVFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSQDLIFIFRGAIISLVSFLRYDDTNHMMDEDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC | ||||||
Disulfide bond | 284↔428 | |||||
Sequence: CDPSLSLDAITSLRGETLVFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSQDLIFIFRGAIISLVSFLRYDDTNHMMDEDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for motif, domain, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 94-101 | Cysteine switch | ||||
Sequence: PRCGVPDV | ||||||
Domain | 109-268 | Peptidase metallopeptidase | ||||
Sequence: RTLKWSKMNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRLHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGP | ||||||
Region | 263-284 | Disordered | ||||
Sequence: QSLYGPGDEDPNPKHPKTPDKC | ||||||
Repeat | 281-330 | Hemopexin | ||||
Sequence: PDKCDPSLSLDAITSLRGETLVFKDRFFWRLHPQQVDAELFLTKSFWPEL | ||||||
Repeat | 331-384 | Hemopexin | ||||
Sequence: PNRIDAAYEHPSQDLIFIFRGAIISLVSFLRYDDTNHMMDEDYPRLIEEEFPGI | ||||||
Repeat | 385-428 | Hemopexin | ||||
Sequence: GDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)48,989
- Last updated2021-04-07 v1
- ChecksumF32EB350E3FB9494
Keywords
- Technical term