Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. Interacts (via the C-terminal) with MMP2 (via the C- terminal PEX domain); the interaction inhibits the MMP2 activity. Down-regulated by TGFB1. Belongs to the protease inhibitor I35 (TIMP) family. Note: This description may include information from UniProtKB.
Protein type: Extracellular matrix; Cell development/differentiation; Secreted, signal peptide; Inhibitor; Secreted; Motility/polarity/chemotaxis
Molecular Function: enzyme activator activity; integrin binding; metal ion binding; metalloendopeptidase inhibitor activity; protease binding; protein binding
Biological Process: aging; central nervous system development; extracellular matrix disassembly; extracellular matrix organization and biogenesis; negative regulation of cell proliferation; negative regulation of membrane protein ectodomain proteolysis; negative regulation of metalloenzyme activity; negative regulation of mitotic cell cycle; negative regulation of Ras protein signal transduction; positive regulation of adenylate cyclase activity; positive regulation of MAPKKK cascade; positive regulation of neuron differentiation; regulation of Rap protein signal transduction; response to cytokine stimulus; response to drug; response to hormone stimulus
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.