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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | SPARC (also known as BM-40 or osteonectin) is a matricellular protein essential for embryo development in invertebrates and highly expressed in bone [ ]. It participates in normal tissue remodeling as it regulates the deposition of extracellular matrix, as well as in neoplastic transformation []. It is involved in extracellular matrix (ECM) assembly and fibrosis through binding both fibrillar collagen and basal lamina collagen IV []. It regulates the activity of matrix metalloproteinases (MMPs), as well as the growth factor signaling mediated by cell surface receptors including vascular endothelial growth factor (VEGF) receptor, basic fibroblast growth factor (bFGF), and transforming growth factor (TGF) beta1. Overexpression of SPARC has been linked to cancers []. SPARC is also a bone-associated protein that has a major role in bone development and mineralisation. It is involved in the initiation and progression of vascular calcification and upregulated by adiponectin []. Furthermore, SPARC may be one of the molecules that govern the uptake and delivery of proteins from blood to the cerebrospinal fluid (CSF) during brain development [].SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an α-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site [ ]. Platelet-derived growth factor (PDGF) interacts with its EC domain, but in a calcium-independent manner, whereas collagen binding is calcium-dependent [, , ].This entry represents the FS domain of SPARC. | Name | SPARC, follistatin-like domain |
| Short Name | SPARC_FS | Type | Domain |
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