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MGP001940

UniProt Annotations

Entry Information
Gene Namematrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
Protein EntryMMP9_HUMAN
UniProt IDP14780
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityCleavage of gelatin types I and V and collagen types IV and V. {ECO:0000269|PubMed:1480034}.
CofactorName=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 3 Ca(2+) ions per subunit.;
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
DiseaseIntervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:18455130}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
DiseaseMetaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainThe conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Enzyme RegulationInhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. {ECO:0000269|PubMed:11179305, ECO:0000269|PubMed:16512877}.
FunctionMay play 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 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. {ECO:0000269|PubMed:1480034}.
InductionActivated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. {ECO:0000269|PubMed:1371271, ECO:0000269|PubMed:1400481, ECO:0000269|PubMed:19893577}.
InteractionSelf; NbExp=2; IntAct=EBI-1382326, EBI-1382326; Q16819:MEP1A; NbExp=2; IntAct=EBI-1382326, EBI-8153734; Q16820:MEP1B; NbExp=2; IntAct=EBI-1382326, EBI-968418; Q8IX30:SCUBE3; NbExp=2; IntAct=EBI-1382326, EBI-4479975; P01033:TIMP1; NbExp=2; IntAct=EBI-1382326, EBI-712536; P13611:VCAN; NbExp=3; IntAct=EBI-1382326, EBI-8515977;
MiscellaneousIn the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.
PtmN- and O-glycosylated. {ECO:0000269|PubMed:1464361}.
PtmProcessing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9. {ECO:0000269|PubMed:12879005, ECO:0000269|PubMed:1371271, ECO:0000269|PubMed:1400481}.
SimilarityBelongs to the peptidase M10A family. {ECO:0000305}.
SimilarityContains 3 fibronectin type-II domains. {ECO:0000255|PROSITE-ProRule:PRU00479}.
SimilarityContains 4 hemopexin repeats. {ECO:0000305}.
Subcellular LocationSecreted, extracellular space, extracellular matrix {ECO:0000305}.
SubunitExists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1. {ECO:0000269|PubMed:10644727, ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439, ECO:0000269|PubMed:12126625, ECO:0000269|PubMed:16512877}.
Tissue SpecificityProduced by normal alveolar macrophages and granulocytes.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MMP9ID41408ch20q11.html";
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp9/";
Web ResourceName=SeattleSNPs; URL="http://pga.gs.washington.edu/data/mmp9/";
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