| Primary information |
|---|
| ID | 33289 |
| Uniprot ID | P35052 |
| Description | Glypican-1 [Cleaved into- Secreted glypican-1] |
| Organism | Homo sapiens |
| Txonomy | Homo ; Homininae ; Hominidae ; Hominoidea ; Catarrhini ; Simiiformes ; Haplorrhini ; Primates ; Euarchontoglires ; Boreoeutheria ; Eutheria ; Theria ; Mammalia ; Amniota ; Tetrapoda ; Dipnotetrapodomorpha ; Sarcopterygii ; Euteleostomi ; Teleostomi ; Gnathostomata ; Vertebrata ; Craniata ; Chordata ; Deuterostomia ; Bilateria ; Eumetazoa ; Metazoa ; Opisthokonta ; Eukaryota ; cellular organisms |
| Subcellular Location | Cell membrane; Lipid-anchor; GPI-anchor; Extracellular side. Endosome. Note=S-nitrosylated form recy |
| Developmental Stage | NA |
| Similarity | NA |
| Post Translational Modification | S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent; in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.; N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or; degraded by |
| Function | Cell surface proteoglycan that bears heparan sulfate. Binds; via the heparan sulfate side chains; alpha-4 (V) collagen and participates in Schwann cell myelination. May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN; targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. |
| Length | 558 |
| Molecular Weight | 61680 |
| Reference | 2148568; 14702039; 1 |
| Hormone | NA |
| PDB ID | NA
|