Overview
| Uniprot ID | F1RSG9 |
|---|
| Protein Name | Acyl-protein thioesterase 1 |
|---|
| Gene Name | LYPLA1 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 190 |
SLTVERLKTLVNPAN |
Function
Acts as an acyl-protein thioesterase. Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1. 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. Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS). Has much higher thioesterase activity than lysophospholipase activity. 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
Protein Sequence
10
MCGNNMSAPL
20
PAVVPAARKA
30
TAAVIFLHGL
40
GDTGHGWAEA
50
FAGIRSAHIK
60
YICPHAPVMP
70
VTLNMNMAMP
80
SWFNIIGLSP
90
DSLEDETGIK
100
QAAENVKSLI
110
EQEVKNGIPS
120
NRIILGGFSQ
130
GGALSLYTAL
140
TTHQKLAGVT
150
ALSCWLPLRS
160
SFPECPISGV
170
NRDIPILQCH
180
GVLDPLVPLM
190
FGSLTVERLK
200
TLVNPANVTF
210
KTYEGMMHSS
220
CQQEMLDVKQ
230
FIEKLLPPID
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0031965 |
nuclear membrane |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0008474 |
palmitoyl-(protein) hydrolase activity |
| Biological Process |
GO:0006631 |
fatty acid metabolic process |
| Biological Process |
GO:0042997 |
negative regulation of Golgi to plasma membrane protein transport |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.