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A0A7J7Y9K3 · A0A7J7Y9K3_PIPKU

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.

TypeIDPosition(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

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

    • ORF names
      mPipKuh1_011635

Organism names

  • Taxonomic identifier
  • Strain
    • MPipKuh1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yangochiroptera > Vespertilionidae > Pipistrellus

Accessions

  • Primary accession
    A0A7J7Y9K3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-20
ChainPRO_502991667021-726Matrix metalloproteinase-9
Disulfide bond231↔257
Disulfide bond245↔272
Disulfide bond289↔315
Disulfide bond303↔330
Disulfide bond348↔374
Disulfide bond362↔389

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
Domain343-391Fibronectin type-II
Region437-527Disordered
Compositional bias448-463Pro residues
Compositional bias481-497Pro residues
Compositional bias498-520Polar residues
Repeat537-582Hemopexin
Repeat583-627Hemopexin
Repeat629-676Hemopexin
Repeat677-723Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    726
  • Mass (Da)
    80,490
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    7721606C4F362E7294F6DDE8A45B091E
MSPWLSLVLALLVLGNDCSAAPRPRQPTVVVFPGDLRTDLTNKQLAEEYLYRYGYTQVAELSDDKQSLSRALRVLQKRLSLPETGELDSTTLAAMRAPRCGVPDVGRFQTFEGDLKWHHQNLTYWIQNYSEDLPRNVIDDAFARAFAVWSAVTPLTFTRVYGVEADIIIQFGVREHGDGYPFDGKDGLLAHAFPPGQGIQGDAHFDDEELWSLGKGVVVPTFFGNADGAPCHFPFTFEGRNYSACTTDGRSDGQLWCSTTADYDTDRRFGFCPSERLYTEHGNSDGKPCVFPFTFEGRSYSACTTDGRSDGYRWCATTANYDQDKLYGFCPTRVDTTVTGGNSAGELCVFPFVFLGQEYSTCTRDGRTDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYSYTEKPPLHEDDVKGIQHLYGGPRPKPEPRPPTTTPETQPTAPPTVCATVRPSEGPTAGPTGPPSPGPTNAPTAGPTGAPTAGPTDSPTRAPTAGPSVAPTESLDPADNVCNVDIFDAIAEIGNYLHLFKDGRYWRFSEAQGRLVQGPFLIRDKWPALPSKLDSVFEEPQSKKIFFFSGRQVWVYTGATVLGPRRLDKLGFGPEVAQVTGALPRGGGKVLLFSRQNFWRFDAKSQMVDPKSASRVDRTFPGVPTNMHDVFLYRDKAYFCQDRYYWRMNLQNGINQVEEVNYVTYDLLQCPEN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias448-463Pro residues
Compositional bias481-497Pro residues
Compositional bias498-520Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACAGB010000006
EMBL· GenBank· DDBJ
KAF6358622.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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