LYPLA1
Function
Acts as an acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (PubMed:22399288, PubMed:27481942, PubMed:37802024). Acts as a negative regulator of autophagy by mediating palmitoylation of SQSTM1, decreasing affinity between SQSTM1 and ATG8 proteins and recruitment of ubiquitinated cargo proteins to autophagosomes (PubMed:37802024). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (PubMed:19439193). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (PubMed:19439193). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (PubMed:21393252).
Sequence Similarities
Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
Tissue Specificity
Platelets.
Cellular localization
- Cytoplasm
- Cell membrane
- Nucleus membrane
- Endoplasmic reticulum
- Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum.
Alternative names
APT1, LPL1, LYPLA1, Acyl-protein thioesterase 1, APT-1, hAPT1, Lysophospholipase 1, Lysophospholipase I, Palmitoyl-protein hydrolase, LPL-I, LysoPLA I