A0A218U9Y4 · A0A218U9Y4_9PASE
- ProteinMatrix metalloproteinase-9
- GeneMMP9
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids705 (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 | 102 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 134 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 168 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 178 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 180 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 185 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 186 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 190 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 193 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 204 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 206 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 208 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 209 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 211 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 211 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 225 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 234 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Active site | 404 | ||||
Binding site | 523 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 525 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 569 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 615 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 617 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 665 | 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 |
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 > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Estrildidae > Estrildinae > Lonchura
Accessions
- Primary accessionA0A218U9Y4
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 | ||||
Chain | PRO_5012397483 | 20-705 | Matrix metalloproteinase-9 | ||
Disulfide bond | 233↔259 | ||||
Disulfide bond | 247↔274 | ||||
Disulfide bond | 291↔317 | ||||
Disulfide bond | 305↔332 | ||||
Disulfide bond | 349↔375 | ||||
Disulfide bond | 363↔390 | ||||
Keywords
- PTM
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Motif | 100-107 | Cysteine switch | |||
Domain | 228-276 | Fibronectin type-II | |||
Domain | 286-334 | Fibronectin type-II | |||
Domain | 344-392 | Fibronectin type-II | |||
Region | 442-513 | Disordered | |||
Compositional bias | 453-481 | Pro residues | |||
Repeat | 519-564 | Hemopexin | |||
Repeat | 565-609 | Hemopexin | |||
Repeat | 611-658 | Hemopexin | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length705
- Mass (Da)78,283
- Last updated2017-09-27 v1
- Checksum5BB3150D83399315
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 453-481 | Pro residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MUZQ01000528 EMBL· GenBank· DDBJ | OWK50549.1 EMBL· GenBank· DDBJ | Genomic DNA |