May 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. Exists 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. Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Produced by normal alveolar macrophages and granulocytes. Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Belongs to the peptidase M10A family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; EC 188.8.131.52; Protease; Secreted; Secreted, signal peptide
Cellular Component: extracellular space; proteinaceous extracellular matrix; extracellular region
Molecular Function: collagen binding; identical protein binding; protein binding; zinc ion binding; metalloendopeptidase activity
Biological Process: positive regulation of keratinocyte migration; extracellular matrix disassembly; collagen catabolic process; extracellular matrix organization and biogenesis; macrophage differentiation; positive regulation of apoptosis; proteolysis; skeletal development; embryo implantation
SS: 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.