A0A218U9Y4 · A0A218U9Y4_9PASE

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Cleavage of gelatin types I and V and collagen types IV and V.
    EC:3.4.24.35 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Can bind about 5 Ca2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site102Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site134Ca2+ 1 (UniProtKB | ChEBI)
Binding site168Ca2+ 2 (UniProtKB | ChEBI)
Binding site178Zn2+ 1 (UniProtKB | ChEBI)
Binding site180Zn2+ 1 (UniProtKB | ChEBI)
Binding site185Ca2+ 3 (UniProtKB | ChEBI)
Binding site186Ca2+ 3 (UniProtKB | ChEBI)
Binding site190Ca2+ 3 (UniProtKB | ChEBI)
Binding site193Zn2+ 1 (UniProtKB | ChEBI)
Binding site204Ca2+ 2 (UniProtKB | ChEBI)
Binding site206Zn2+ 1 (UniProtKB | ChEBI)
Binding site208Ca2+ 3 (UniProtKB | ChEBI)
Binding site209Ca2+ 1 (UniProtKB | ChEBI)
Binding site211Ca2+ 3 (UniProtKB | ChEBI)
Binding site211Ca2+ 1 (UniProtKB | ChEBI)
Binding site225Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site234Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site404
Binding site523Ca2+ 4 (UniProtKB | ChEBI)
Binding site525Ca2+ 5 (UniProtKB | ChEBI)
Binding site569Ca2+ 4 (UniProtKB | ChEBI)
Binding site615Ca2+ 4 (UniProtKB | ChEBI)
Binding site617Ca2+ 5 (UniProtKB | ChEBI)
Binding site665Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processextracellular matrix organization
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Matrix metalloproteinase-9
  • EC number
  • Alternative names
    • 92 kDa gelatinase
    • 92 kDa type IV collagenase
    • Gelatinase B

Gene names

    • Name
      MMP9
    • ORF names
      RLOC_00013543

Organism names

  • Taxonomic identifier
  • Strain
    • White83orange57
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Estrildidae > Estrildinae > Lonchura

Accessions

  • Primary accession
    A0A218U9Y4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_501239748320-705Matrix metalloproteinase-9
Disulfide bond233↔259
Disulfide bond247↔274
Disulfide bond291↔317
Disulfide bond305↔332
Disulfide bond349↔375
Disulfide bond363↔390

Keywords

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

Family & Domains

Features

Showing features for motif, domain, region, compositional bias, repeat.

Type
IDPosition(s)Description
Motif100-107Cysteine switch
Domain228-276Fibronectin type-II
Domain286-334Fibronectin type-II
Domain344-392Fibronectin type-II
Region442-513Disordered
Compositional bias453-481Pro residues
Repeat519-564Hemopexin
Repeat565-609Hemopexin
Repeat611-658Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    705
  • Mass (Da)
    78,283
  • Last updated
    2017-09-27 v1
  • Checksum
    5BB3150D83399315
MALLLAPLVVGLLAVSCGAAPLQGKPQAVVTFPGDLISTLPDLELAERYLQRFGYTTETEAKIGGRHVSLGKALLKMQKQLGLEETGELDAATLEAMRAPRCGVPDVGTFLTFEGDLKWDHMDLTYRVMNYSPDLDRAVIDDAFRRAFQVWSDVTPLTFTQIYSGEADIMIMFGSQEHGDGYPFDGKDGLLAHAFPPGKGIQGDAHFDDDEFWTLGTGLVVKTRHGNANGAECHFPFIFEGRSYSRCTTEGRKDGLPWCATTSNYDRDKKYGFCPSELLYTNGGNSDGAPCVFPFVFDGTSYDTCTTDGRSDGYRWCATTSSFDQDKKYGFCPNRDTAVIGGNSQGDPCVFPFTFLGQSYSACTSQGRQDGKLWCATTSNYDTDKKWGFCPDRGYSIFLVAAHEFGHSLGLDHSSVREALMYPMYSYIQDFQLHPDDVQGIQYLYGRGSGPKPTAPAPAPTEEPQPLPTEEPQPVPTEEPQPVPTEAGSTSTTEEEEEETPEPTVGPIPVDPSRDACMERNFDAITEISGELYFFKDGKYWTYSSFWKSGVQGAFSVADTWPGLPDTIDAVFQDLLTKRVFFFAGRQFWVFSGKSVLGPRGIEKLGIGKEAGRLSGALQRGRGKVLLFSGESYWRLDVKVQRVDKGYPRATDDVFTGVPLDARNVFLYQGKYHFCRGSFYWRMTPRYQVDRVGYVKYDILQCPQN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias453-481Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MUZQ01000528
EMBL· GenBank· DDBJ
OWK50549.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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