A0A6I8SZK6 · A0A6I8SZK6_XENTR
- ProteinMatrix metalloproteinase-9
- Genemmp9.1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids681 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves NINJ1 to generate the Secreted ninjurin-1 form. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
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 | 98 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 130 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 164 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 174 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 176 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 181 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 182 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 186 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 189 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 200 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 202 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 204 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 207 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 207 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 230 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Active site | 400 | ||||
Binding site | 499 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 501 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 545 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 547 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 641 | Ca2+ 5 (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 | collagen catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMatrix metalloproteinase-9
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Silurana
Accessions
- Primary accessionA0A6I8SZK6
Organism-specific databases
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 | ||||
Chain | PRO_5030156177 | 20-681 | Matrix metalloproteinase-9 | ||
Disulfide bond | 229↔255 | ||||
Disulfide bond | 243↔270 | ||||
Disulfide bond | 287↔313 | ||||
Disulfide bond | 301↔328 | ||||
Disulfide bond | 345↔371 | ||||
Disulfide bond | 359↔386 | ||||
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with LCN2. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 224-272 | Fibronectin type-II | |||
Domain | 282-330 | Fibronectin type-II | |||
Domain | 340-388 | Fibronectin type-II | |||
Region | 440-485 | Disordered | |||
Compositional bias | 458-485 | Polar residues | |||
Repeat | 495-540 | Hemopexin | |||
Repeat | 541-585 | Hemopexin | |||
Repeat | 587-634 | Hemopexin | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length681
- Mass (Da)76,307
- Last updated2021-06-02 v2
- Checksum6F7FD6EDBD7617C2
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 458-485 | Polar residues | |||