SPPL2

SPPL2, or signal peptide peptidase-like 2, is a protein-coding gene found in humans and other organisms. It is a member of the SPPL protein family, which are intramembrane-cleaving proteases. These proteases are unique because they cleave their substrates within the lipid bilayer of cell membranes. SPPL2 is primarily located in the endoplasmic reticulum.

The main known function of SPPL2 is to cleave amyloid precursor protein (APP) and its derivatives. This cleavage is believed to play a role in the processing of APP, a protein implicated in Alzheimer's disease. SPPL2's activity on APP may influence the production of amyloid-beta peptides, which form plaques in the brain of Alzheimer's patients. Research is ongoing to fully elucidate the specific pathways and consequences of SPPL2 activity.

Dysregulation or mutations in the SPPL2 gene have been associated with certain neurological conditions, though the exact clinical significance is still under investigation. Studies have explored its potential involvement in neurodegenerative diseases and other cellular processes related to membrane protein trafficking and turnover. The SPPL2 protein itself is a type II transmembrane protein, meaning its N-terminus is in the cytoplasm and its C-terminus is in the lumen of the endoplasmic reticulum.