Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A7K5CJU0 · A0A7K5CJU0_MOTAL

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 site100Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site132Ca2+ 1 (UniProtKB | ChEBI)
Binding site166Ca2+ 2 (UniProtKB | ChEBI)
Binding site176Zn2+ 1 (UniProtKB | ChEBI)
Binding site178Zn2+ 1 (UniProtKB | ChEBI)
Binding site183Ca2+ 3 (UniProtKB | ChEBI)
Binding site184Ca2+ 3 (UniProtKB | ChEBI)
Binding site188Ca2+ 3 (UniProtKB | ChEBI)
Binding site191Zn2+ 1 (UniProtKB | ChEBI)
Binding site202Ca2+ 2 (UniProtKB | ChEBI)
Binding site204Zn2+ 1 (UniProtKB | ChEBI)
Binding site206Ca2+ 3 (UniProtKB | ChEBI)
Binding site207Ca2+ 1 (UniProtKB | ChEBI)
Binding site209Ca2+ 3 (UniProtKB | ChEBI)
Binding site209Ca2+ 1 (UniProtKB | ChEBI)
Binding site232Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site240Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site402
Binding site521Ca2+ 4 (UniProtKB | ChEBI)
Binding site523Ca2+ 5 (UniProtKB | ChEBI)
Binding site567Ca2+ 4 (UniProtKB | ChEBI)
Binding site613Ca2+ 4 (UniProtKB | ChEBI)
Binding site615Ca2+ 5 (UniProtKB | ChEBI)
Binding site663Ca2+ 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
      MOTALB_R12120

Organism names

  • Taxonomic identifier
  • Strain
    • B10K-DU-001-75
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Motacillidae > Motacilla

Accessions

  • Primary accession
    A0A7K5CJU0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-17
ChainPRO_502984513918-703Matrix metalloproteinase-9
Disulfide bond231↔257
Disulfide bond245↔272
Disulfide bond289↔315
Disulfide bond303↔330
Disulfide bond347↔373
Disulfide bond361↔388

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.

Family & Domains

Features

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

Type
IDPosition(s)Description
Motif98-105Cysteine switch
Domain226-274Fibronectin type-II
Domain284-332Fibronectin type-II
Domain342-390Fibronectin type-II
Region440-511Disordered
Compositional bias451-479Pro residues
Repeat517-562Hemopexin
Repeat563-607Hemopexin
Repeat609-656Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    703
  • Mass (Da)
    78,153
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    097D0676BF911838FBD68297E3A5C252
LLLAPLVAGLLAVSCWAAPLQGKPQAVVTFPGDLISTLPDLQLAERYLQRFGYTTEAEAKIGGRHVSLGKALLKMQKQLGLEETGELDAATLEAMRAPRCGVPDVGTFLTFEGDLKWDHMDLTYRVMNYSPDLDRAVIDDAFRRAFQVWSDVTPLTFTQIYSGEADIMIMFGSQEHGDGYPFDGKDGLLAHAFPPGQGIQGDAHFDDDEFWTLGTGLVVKTRHGNANGAECHFPFIFEGHSYSRCTTEGRKDGLPWCATTPNYDRDKKYGFCPSELLYTNGGNSDGAPCVFPFVFEGTSYNTCTTDGRSDGYRWCATTSSFDQDKKYGFCPNRDTAVIGGNSQGDPCVFPFTFLGQSYSACTSQGRQDGKLWCATTSNYDTDKKWGFCPDRGYSIFLVAAHEFGHSLGLDHSSVREALMYPMYSYIQDFQLHPDDVQGIQYLYGRGSGPKPTAPAPAPTEEPQPVPTEEPQPVPTEEPQPVPTEAGSTSTTEEEEEETPEPTVGPIPVDPSRDACMERNFDAITEINGELYFFKDGKYWTYSSFWKSGIQGAFSVADTWPGLPDTIDAVFQDLLTKRVFFFAGRQFWVFSGKSALGPRGIEKLGIGKEAGRLSGALQRGRGKVLLFSGESYWRLDVKVQRVDKGYPRATDDVFTGVPLDARNVFLYQGKYHFCRGSFYWRMTPRYQVDRVGYVKYDILQCPQN

Features

Showing features for non-terminal residue, compositional bias.

Type
IDPosition(s)Description
Non-terminal residue1
Compositional bias451-479Pro residues
Non-terminal residue703

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VXBE01011785
EMBL· GenBank· DDBJ
NWS08441.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help