Signal peptide peptidase-like 3 (SPPL3)

Signal peptide peptidase-like 3 (SPPL3) is a member of the signal peptide peptidase family of intramembrane-cleaving aspartic proteases, related to presenilins[3][4]. SPPL3 is predominantly located in the Golgi apparatus and acts as a sheddase, releasing the active site-containing ectodomains of glycan-modifying glycosidases, thereby regulating glycosylation and protein secretion[6]. Unlike some family members, SPPL3 is not primarily involved in immune surveillance or peptide antigen processing but rather in the modulation of glycosylation patterns, which has implications for cell signaling, tumor biology, and immunomodulation[6][3][4][5]. As of current literature, SPPL3 is not a direct drug target, nor are there established drugs or biomarkers based on its activity, but it is a relevant emerging target for research at the intersection of enzymology, glycomics, and disease biology.

Other names

SPPL3Signal peptide peptidase like 3Q8TCT6 (UniProt Accession)

no drugs targeting SPPL3; general mechanism is intramembrane aspartyl protease activity