InterPro : IPR015455

Name  Thrombospondin-2 Short Name  Thrombospondin-2
Type  Family Description  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.The gene encoding thrombospondin 2, THBS2, was originally identified by screening of a human fibroblast library []. The cDNA encoding THBS2 showed close homology to THBS1. In gene disruption studies it has been shown that THBS2 null mice were overtly normal, but actually had a number of altered phenotypes []. These included abnormalities in connective tissue resulting in fragile skin with reduced tensile strength. The tail was unusually flexible and the long bones denser and thicker. Mutant mice also displayed abnormal bleeding times and there was an increase in the number of blood vessels suggesting an antiangiogenic role for THBS2.Further evidence supporting an inhibitory role for THBS2 in angiogenesis has shown by the injection of squamous cell carcinomas stably expressing THBS2 in the dermis of nude mice, resulting in inhibition of tumour growth []. The areas around the THBS2 expressing tumours were necrotic while the density and number of tumour vessels was reduced.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

6 Contains

Id Name Short Name Type
IPR000884 Thrombospondin, type 1 repeat Thrombospondin_1_rpt Repeat
IPR013032 EGF-like, conserved site EGF-like_CS Conserved_site
IPR000742 Epidermal growth factor-like domain EG-like_dom Domain
IPR003367 Thrombospondin, type 3-like repeat Thrombospondin_3-like_rpt Repeat
IPR008859 Thrombospondin, C-terminal Thrombospondin_C Domain
IPR017897 Thrombospondin, type 3 repeat Thrombospondin_3_rpt Repeat

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Adams JC Thrombospondins: multifunctional regulators of cell interactions. 2001 Annu Rev Cell Dev Biol 17 25-51
LaBell TL Thrombospondin II: partial cDNA sequence, chromosome location, and expression of a second member of the thrombospondin gene family in humans. 1992 Genomics 12 421-9
Kyriakides TR Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis. 1998 J Cell Biol 140 419-30
Streit M Thrombospondin-2: a potent endogenous inhibitor of tumor growth and angiogenesis. 1999 Proc Natl Acad Sci U S A 96 14888-93

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)