| ID | Sequence | Length | GC content |
|---|---|---|---|
| AGGUAGCUGCGAGGAAACUUUUGCAGCGGCUGGGUAGCAGCACGUCUCU… | 2336 nt | 0.4692 | |
| AGGUAGCUGCGAGGAAACUUUUGCAGCGGCUGGGUAGCAGCACGUCUCU… | 2219 nt | 0.4736 | |
| AGGUAGCUGCGAGGAAACUUUUGCAGCGGCUGGGUAGCAGCACGUCUCU… | 2105 nt | 0.4755 | |
| AGGUAGCUGCGAGGAAACUUUUGCAGCGGCUGGGUAGCAGCACGUCUCU… | 2267 nt | 0.4720 |
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation. The protein encoded by this gene can bind to and inhibit the dipeptidyl peptidase activity of CD26, and it can induce apoptosis in certain cell types. Deletion mutations in this gene are associated with Simpson-Golabi-Behmel syndrome, also known as Simpson dysmorphia syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2009]
A single-cell transcriptomic analysis in a rat model of radiation-induced lung injury identified the GPC3 as an orthologous rat gene associated with inflammatory processes [Shi et al. DOI:10.17305/bb.2024.10357]. A review of wound age estimation literature notes that heparan sulphate proteoglycan, an extracellular matrix protein, has been studied via immunohistochemistry for its role in wound healing [Cecchi DOI:10.1007/S00414-010-0505-X].