Protein O-glucosyltransferase 3 (POGLUT3)

Protein O-glucosyltransferase 3 (POGLUT3) is an endoplasmic reticulum–resident glycosyltransferase enzyme that adds O-linked glucose (O-Glc) to specific serine residues within the consensus sequence of epidermal growth factor-like (EGF) repeats in various proteins, notably NOTCH receptors and extracellular matrix components such as fibrillin-1 (FBN1), fibrillin-2 (FBN2), and latent TGF-β binding protein 1 (LTBP1). POGLUT3, a homolog of POGLUT1 and POGLUT2, features a CAP10 catalytic domain and a C-terminal KDEL-like ER retention signal, aiding its localization and retrieval to the ER. It is essential for proper secretion and folding of its substrates. By modifying key signaling and structural proteins, POGLUT3 indirectly influences Notch and TGF-β pathways and may play roles in tissue development, homeostasis, and potentially disease processes linked to aberrant signaling or extracellular matrix organization. No direct pharmacological inhibitors or drugs are documented for POGLUT3, and its safety profile as a therapeutic target is currently unknown.

Other names

KDELC2KDEL motif-containing protein 2Protein O-xylosyltransferase POGLUT3MGC33424UNQ1904/PRO4350

Not applicable: No drugs currently target POGLUT3 directly, so no established mechanisms of action for pharmacological modulators.