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QuickView for Thrombospondin-2 (biogroup)
- Description:
- Thrombospondin-2 (TSP2) is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. It has been shown to inhibit tumour growth and angiogenesis. Thrombospondins are multimeric multidomain glycoproteins that function at cell surfaces and in the extracellular matrix milieu. They act as regulators of cell interactions in vertebrates. They are divided into two subfamilies, A and B, according to their overall molecular organisation. The subgroup A proteins TSP-1 and -2 contain an N-terminal domain, a VWFC domain, three TSP1 repeats, three EGF-like domains, TSP3 repeats and a C-terminal domain. They are assembled as trimer. The subgroup B thrombospondins, designated TSP-3, -4, and COMP (cartilage oligomeric matrix protein, also designated TSP-5) are distinct in that they contain unique N-terminal regions, lack the VWFC domain and TSP1 repeats, contain four copies of EGF-like domains, and are assembled as pentamers. EGF, TSP3 repeats and the C-terminal domain are thus the hallmark of a thrombospondin.
- Taxonomy/Path:
- InterPro : Thrombospondin / Thrombospondin-2
SELECTED ORGANISM:
