SPPL2A
Description
The SPPL2A (signal peptide peptidase like 2A) is a protein-coding gene located on chromosome 15.
SPPL2A, also known as Signal peptide peptidase-like 2A, is a human gene. It is a member of the signal peptide peptidase-like protease (SPPL) family and encodes a lysosomal/late endosomal membrane protein with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs). SPPL2A plays a role in innate and adaptive immunity by cleaving TNFα in activated dendritic cells. A pseudogene of this gene also lies on chromosome 15.
SPPL2A is an intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides within the hydrophobic plane of the membrane. It plays a role in the processing of FASLG, ITM2B, and TNF. SPPL2A catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha, promoting the release of the intracellular domain (ICD) for nuclear signaling. It also cleaves Fas antigen ligand FASLG, releasing the intracellular FasL domain (FasL ICD). SPPL2A is essential for the degradation of the invariant chain CD74, which is crucial for antigen-presenting cells in the immune system. SPPL2A contributes to the regulation of innate and adaptive immunity. It cleaves the simian foamy virus envelope glycoprotein gp130 independently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis. SPPL2A interacts with ITM2B.
SPPL2A is also known as IMD86, IMP3, PSL2.
