Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Widely expressed, at a low level, and the highest expression is observed in skeletal muscle and brain. Also detected in fetal liver. Inhibited by N-ethylmaleimide. Belongs to the peptidase C54 family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.22.-; Autophagy; Protease; Microtubule-binding
Molecular Function: protein binding; cysteine-type endopeptidase activity; cysteine-type peptidase activity
Biological Process: protein delipidation; mitochondrion degradation; protein processing; C-terminal protein lipidation; proteolysis; protein targeting to membrane; cellular response to nitrogen starvation; autophagic vacuole formation
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.