A0A6I8SZK6 · A0A6I8SZK6_XENTR

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

  • 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 site98Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site130Ca2+ 1 (UniProtKB | ChEBI)
Binding site164Ca2+ 2 (UniProtKB | ChEBI)
Binding site174Zn2+ 1 (UniProtKB | ChEBI)
Binding site176Zn2+ 1 (UniProtKB | ChEBI)
Binding site181Ca2+ 3 (UniProtKB | ChEBI)
Binding site182Ca2+ 3 (UniProtKB | ChEBI)
Binding site186Ca2+ 3 (UniProtKB | ChEBI)
Binding site189Zn2+ 1 (UniProtKB | ChEBI)
Binding site200Ca2+ 2 (UniProtKB | ChEBI)
Binding site202Zn2+ 1 (UniProtKB | ChEBI)
Binding site204Ca2+ 3 (UniProtKB | ChEBI)
Binding site207Ca2+ 3 (UniProtKB | ChEBI)
Binding site207Ca2+ 1 (UniProtKB | ChEBI)
Binding site230Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site400
Binding site499Ca2+ 4 (UniProtKB | ChEBI)
Binding site501Ca2+ 5 (UniProtKB | ChEBI)
Binding site545Ca2+ 4 (UniProtKB | ChEBI)
Binding site547Ca2+ 5 (UniProtKB | ChEBI)
Binding site641Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentextracellular region
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
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
      mmp9.1

Organism names

Accessions

  • Primary accession
    A0A6I8SZK6

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_503015617720-681Matrix metalloproteinase-9
Disulfide bond229↔255
Disulfide bond243↔270
Disulfide bond287↔313
Disulfide bond301↔328
Disulfide bond345↔371
Disulfide bond359↔386

Keywords

Expression

Gene expression databases

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 domain, region, compositional bias, repeat.

Type
IDPosition(s)Description
Domain224-272Fibronectin type-II
Domain282-330Fibronectin type-II
Domain340-388Fibronectin type-II
Region440-485Disordered
Compositional bias458-485Polar residues
Repeat495-540Hemopexin
Repeat541-585Hemopexin
Repeat587-634Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    681
  • Mass (Da)
    76,307
  • Last updated
    2021-06-02 v2
  • Checksum
    6F7FD6EDBD7617C2
MGELGVLAIVAILCSRGHSVPTNSKTPLSITFPGEIQSSMTNAELAERYLLQFGYMTQEQGSNVTLKNALTLMQQKLGLTRTGVLDTETLEAMRRPRCGFPDIGKFNTFDGDLKWDHNDITYRILSYSPDLDPEVIDDAFARAFKVWSDVTPLTFTRIYSGEPDINILFGPEDHGDPYPFDGKDGLLAHAYPPGPGVQGDAHFDEDEFWTLGTGTVVKTRFGNAEGALCHFPFIFDGQSYSSCTTSGRSDGLPWCSTTPSYDQDKKYGFCPSELLYTYGGNSEGQPCVFPFIFDGVSYNGCTKEGRQDGYRWCSTTADYDQDQKYGFCPNRDTAVIGGNSQGEPCVFPFTFQGKRFNSCTTDGRDDRKLWCATTSSYDQDRKWGFCPDQGYSLFLVAAHEFGHALGLEHSDVKDALMYPMYSYVKDFQLHEDDVRGIQYLYGSGPHPAPPKPSDKPIPTTTTPSTRTPTTTPSTRAPTTTPLTPSVNPALDACKVKMFDAITELQGALHFFKDGLYWSVTSKNKNALQSPRNISDTWPALPTKIDTAFQDPTSKNIFFFSGRKFWQYTGKSVLGPRSIEKLGLSKDVEGIMGSFARDNGKALLFNGERYWRLNVKTLTVDKGYPRLTDVDYAGVPSDSHDVFLYQGKYYFCQDRFFWRMTSRKQVDRVGYVKYDLLHCPEH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias458-485Polar residues

Genome annotation databases

Similar Proteins

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