A0A7K9XKW4 · A0A7K9XKW4_9GRUI
- ProteinMatrix metalloproteinase-9
- GeneMmp9
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids684 (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 | 100 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | |||
Binding site | 132 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 166 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 176 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 178 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 183 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 184 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 188 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 191 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 202 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 204 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 206 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 207 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 209 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 209 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 232 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Active site | 402 | ||||
Binding site | 502 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 504 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 548 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 550 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 594 | Ca2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 596 | Ca2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 644 | 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 > Gruiformes > Psophiidae > Psophia
Accessions
- Primary accessionA0A7K9XKW4
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 | 1-17 | ||||
Chain | PRO_5029867663 | 18-684 | Matrix metalloproteinase-9 | ||
Disulfide bond | 231↔257 | ||||
Disulfide bond | 245↔272 | ||||
Disulfide bond | 289↔315 | ||||
Disulfide bond | 303↔330 | ||||
Disulfide bond | 347↔373 | ||||
Disulfide bond | 361↔388 | ||||
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.
Structure
Family & Domains
Features
Showing features for motif, domain, region, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Motif | 98-105 | Cysteine switch | |||
Domain | 226-274 | Fibronectin type-II | |||
Domain | 284-332 | Fibronectin type-II | |||
Domain | 342-390 | Fibronectin type-II | |||
Region | 444-492 | Disordered | |||
Repeat | 498-543 | Hemopexin | |||
Repeat | 544-588 | Hemopexin | |||
Repeat | 590-637 | Hemopexin | |||
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length684
- Mass (Da)76,026
- Last updated2021-04-07 v1
- MD5 ChecksumFAA27A3E1B5339E9A10F51C041427609
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Non-terminal residue | 684 | ||||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VWZZ01005577 EMBL· GenBank· DDBJ | NXI98164.1 EMBL· GenBank· DDBJ | Genomic DNA |