Tissue Specificity | |
Post Translational Modifications | N- and O-glycosylated.contains about 50% carbohydrate. This is composed of highly fucosylated N-linked saccharides, the major structure is a biantennary asialosaccharide containing 2 fucose residues on one antenna and an unsubstituted terminal lactosamine sequence on the other. The Gram-negative bacterium F.nucleatum binds to carbohydrates containing unsubstituted GalBeta1,4GlcNAc residues. N-glycosylation on Asn-87 is prevalent in head and neck cancer patients. Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P(3) position is mostly lysine. The endoprotease may be of microbial origin. Besides on the N-terminal of mature PRB3, pyroglutamate formation found on at least Gln-67, Gln-88, Gln-256 and Gln-337. |
Function | Acts as a receptor for the Gram-negative bacterium F.nucleatum. |
Protein Name | Basic Salivary Proline-Rich Protein 3Parotid Salivary Glycoprotein G1Proline-Rich Protein G1 |
Database Links | |
Cellular Localisation | Secreted |
Alternative ELISA Names | Basic Salivary Proline-Rich Protein 3 ELISA kitParotid Salivary Glycoprotein G1 ELISA kitProline-Rich Protein G1 ELISA kitPRB3 ELISA kit |
output | |
Information sourced from Uniprot.org