Thrombospondin, C-terminal (IPR008859)

Short name: Thrombospondin_C

Overlapping homologous superfamilies


Domain relationships



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 [PMID: 11687483]. EGF, TSP3 repeats and the C-terminal domain are thus the hallmark of a thrombospondin.

The globular C-terminal domain is a beta sandwich of two curved antiparallel beta-sheets [PMID: 15014436]. The fold is an elaboration of the jelly role topology, with strand B3-B7, B11 and B14-B15 forming the eight-stranded jelly roll motif. The function of the C-terminal domain is not yet known.

GO terms

Biological Process

GO:0007155 cell adhesion

Molecular Function

GO:0005509 calcium ion binding

Cellular Component

GO:0005576 extracellular region

Contributing signatures

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