LYPLA1

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. The use of alternate polyadenylation sites has been found for this gene. There are alternatively spliced transcript variants described for this gene but the full length nature is not known yet. [provided by RefSeq]

lysophospholipase I

Acts as a 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).
Has depalmitoylating activity toward KCNMA1 (PubMed:22399288).
Could also depalmitoylate ADRB2 (PubMed:27481942).
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).By Similarity5 Publications

Fatty acid metabolic processIEA:UniProtKB-KW
Negative regulation of Golgi to plasma membrane protein transportIEA:Ensembl
Protein depalmitoylationManual Assertion Based On ExperimentIDA:UniProtKB

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.