Family

Matrix metalloproteinase-16 (IPR028697)

Short name: MMP16

Family relationships

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 [PMID: 12801404]. 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 [PMID: 12027585]. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages [PMID: 12801404].

Matrix metalloproteinase-16 (MMP16; MEROPS identifier M10.016), also called MT3-MMP, degrades various components of the extracellular matrix, such as collagen type III and fibronectin. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells [PMID: 11278606]. MMP-16 can not only directly degrade some matrix molecules, but can also activate pro-MMP-2 (gelatinase A), one of the most important MMPs in tissue remodelling and cell migration [PMID: 14681236, PMID: 17616928].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PANTHER