Thrombospondin-1 (IPR028499)

Short name: Thrombospondin-1

Overlapping homologous superfamilies

Family relationships


Thrombospondin 1 (TSP-1) is a member of the thrombospondin (TSP) family, which consists of five extracellular calcium-binding multifunctional proteins: TSP-1, TSP-2, TSP-3, TSP-4, and TSP-5. TSP-1 t is involved in angiogenesis, cancer, and inflammation. It is a major activator of transforming growth factor (TGFbeta1), which mediates wound healing, cell proliferation, extracellular matrix formation, and the immune respose [PMID: 9657149].

TSP-1 is a large, homotrimeric molecule. Each monomer consists of an N-terminal globular domain that binds heparin, type I, type II, and type III repeats, and a C-terminal globular domain. All five members of the TSP family have the repeat domains type II and III, but only TSP-1 and TSP-2 contain the type I repeats [PMID: 2430973]. TSP-1-specific domains bind to proteoglycans, membrane proteins such as integrins, and other matrix proteins expressed by a variety of cells [PMID: 19830595, PMID: 21765615]. Type I repeats, also called thrombospondin structural homology repeats (TSRs), inhibit angiogenesis by activating CD36 and inducing apoptosis in endothelial cells [PMID: 10613822].

GO terms

Biological Process

GO:0006954 inflammatory response
GO:0016525 negative regulation of angiogenesis

Molecular Function

GO:0050840 extracellular matrix binding
GO:0008201 heparin binding

Cellular Component

GO:0005615 extracellular space

Contributing signatures

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