4 GO Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR028733 |
| GO:0006508 | IPR028733 |
| GO:0006954 | IPR028733 |
| GO:0016021 | IPR028733 |
4 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR028733 |
| GO:0006508 | IPR028733 |
| GO:0006954 | IPR028733 |
| GO:0016021 | IPR028733 |
| Type: | Family | Name: | Matrix metalloproteinase-25 |
| Description: | Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules []. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. Matrix metalloproteinase-25 (MMP25) or membrane-type matrix metalloproteinase 6 (MT6-MMP) is, as well as MT4-MMP, a glycosyl-phosphatidyl inositol (GPI)-anchored MMP []. It may facilitate tumour progression through its ability to activate progelatinase A [] and may be part of the leukocytes proteolytic arsenal during inflammatory responses []. | Short Name: | MMP25 |
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR028733 |
| GO:0006508 | IPR028733 |
| GO:0006954 | IPR028733 |
| GO:0016021 | IPR028733 |
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR028733 |
| GO:0006508 | IPR028733 |
| GO:0006954 | IPR028733 |
| GO:0016021 | IPR028733 |
