MMP3 - matrix metallopeptidase 3 (stromelysin 1, progelatinase)
Entrez Gene Name: matrix metallopeptidase 3 (stromelysin 1, progelatinase)
Entrez GeneID: Human(4314)
, Mouse(17392), Rat(171045)
, Mouse(17392), Rat(171045) Synonyms: CHDS6, MGC126102, MGC126103, MGC126104, MMP3, MT3-MMP, SL-1, SLN-1, STMY, STMY1, STR-1, STROMELYSIN, STROMELYSIN1, Transin, Transin-1 Metalloprotease
Gene Summary
- Human (4314): Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq]
- Rat (171045): endopeptidase that degrades extracellular matrix proteins [RGD]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
collagen catabolic process, metabolic process, proteolysis, response to amino acid stimulus, response to cytokine stimulus
Cellular Components
extracellular region, extracellular space, intracellular membrane-bounded organelle, proteinaceous extracellular matrix
Literature References
- 11687497Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior.Annu Rev Cell Dev Biol 2001;17:463-516
- 11244034Feldmann M, Maini RN. Anti-TNF alpha therapy of rheumatoid arthritis: what have we learned?Annu Rev Immunol 2001;19:163-96
- 16146796Richardson J, Viswanathan K, Lucas A. Serpins, the vasculature, and viral therapeutics.Front Biosci 2006 Jan 01;11:1042-56 View 1432 categorized literature findings and their references in IPA
Molecular Functions
calcium ion binding, hydrolase activity, metal ion binding, metalloendopeptidase activity, metallopeptidase activity, peptidase activity, zinc ion binding
Protein Domains
catalytic domain, hemopexin-like domain, Metalloendopeptidase, peptidase, Stromelysin 1
