Signal peptidase complex catalytic subunit SEC11A (SEC11A)

Signal peptidase complex catalytic subunit SEC11A is an 18 kDa serine-type peptidase that forms part of the signal peptidase complex (SPC) in the endoplasmic reticulum. Its primary function is to catalyze the cleavage of N-terminal signal peptides from nascent proteins during translocation, a critical step for protein maturation, folding, and cellular trafficking. SEC11A has additional roles in cell migration and invasion and has been directly implicated in gastric cancer and metastasis. As a protein essential to core cellular processes, SEC11A is an emerging therapeutic target, especially in cancers and protein-misfolding diseases, though direct clinical inhibitors remain undeveloped. Current research leverages AI-powered drug discovery to identify new small molecule modulators, but therapeutic application will depend on balancing efficacy with safety due to the fundamental role of SEC11A in normal cellular biology

Other names

SEC11ASEC11 homolog AEndopeptidase SP18Microsomal signal peptidase 18 kDa subunitSEC11-like protein 1SPC18Previous symbol: SEC11L1

Enzyme inhibition: Modulators typically act by inhibiting the signal peptidase activity, preventing signal peptide cleavage and interfering with protein maturation. Potential allosteric modulation or disruption of the signal peptidase complex assembly (inferred from drug discovery workflows).