SEC11C is a catalytic subunit of the signal peptidase complex (SPC), an essential endoplasmic reticulum (ER) membrane complex that removes signal peptides from nascent secretory proteins during translocation 1. SEC11C specifically cleaves N-terminal signal peptides containing hydrophobic alpha-helices shorter than 18-20 amino acids through a catalytic triad mechanism 1. The active site architecture creates a transmembrane window that locally thins the ER bilayer, generating specificity for signal peptide recognition and removal 1. Beyond its canonical protein maturation role, SEC11C appears to participate in broader physiological processes. Differential expression analysis identified SEC11C among genes potentially contributing to parathyroid adenoma pathogenesis 2, and it emerged as a candidate gene associated with growth traits in pig breeding programs 3. SEC11C was also identified as a key regulatory gene affecting intramuscular lipid content and fatty acid composition in pigs 4, and included in a prognostic risk model for lung adenocarcinoma predicting patient survival outcomes 5. These findings suggest SEC11C functions extend beyond canonical signal peptide processing to involve metabolic regulation and potential disease-associated dysregulation, though mechanistic details linking altered SEC11C expression to these phenotypes require further investigation.