| Post Translational Modifications | The proenzyme is activated by removal of the propeptide.this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro). N-glycosylated. Tyrosine phosphorylated by PKDCC/VLK. |
| Function | Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. |
| Protein Name | Collagenase 3Matrix Metalloproteinase-13Mmp-13 |
| Database Links | Reactome: R-HSA-1442490Reactome: R-HSA-1474228Reactome: R-HSA-1592389Reactome: R-HSA-2022090Reactome: R-HSA-8941332 |
| Cellular Localisation | SecretedExtracellular SpaceExtracellular Matrix |
| Alternative Protein Names | Collagenase 3 proteinMatrix Metalloproteinase-13 proteinMmp-13 proteinMMP13 protein |
Information sourced from Uniprot.org
