Signal peptidase complex catalytic subunit SEC11C (SEC11C)

Signal peptidase complex catalytic subunit SEC11C (SEC11C) is an enzyme found in the endoplasmic reticulum membrane that functions as a catalytic component of the signal peptidase complex (SPC)[1][3][5]. It enables serine-type endopeptidase activity and is directly involved in the crucial maturation step of secretory and membrane proteins by cleaving their N-terminal signal peptides as they are translocated into the lumen of the endoplasmic reticulum[1][3][4][5]. SEC11C recognizes and specifically cleaves the signal peptides containing hydrophobic alpha-helices, particularly those with h-regions shorter than 18–20 amino acids[3][5]. SEC11C, in coordination with the other SPC subunits, forms a unique transmembrane window to ensure substrate specificity and proper processing of newly synthesized proteins[1]. Dysregulation of SPC components, including SEC11C, has been associated with disease contexts such as lung adenocarcinoma, stressing its role in both fundamental cell biology and disease mechanisms[1][3].

Other names

SEC11 homolog CSEC11L3SPC21SPCS4Csignal peptidase complex 21microsomal signal peptidase 21 kDa subunitSEC11-like protein 3SPase 21 kDa subunitMICROSOMAL SIGNAL PEPTIDASE subunit1810029G24Rik