Overview
| Uniprot ID | A0A5G2RCG0 |
|---|
| Protein Name | Acyl-protein thioesterase 1 |
|---|
| Gene Name | LYPLA1 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 253 |
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
MRARGPRGQP
20
GPPGAGWPDI
30
VTRAAGGADG
40
EARARGPGGR
50
RGGGAHAPER
60
APVRGSDSPF
70
ARPWAAAGSR
80
SAFRFRRAVC
90
RAGVCAAITC
100
RRLCPPSCPP
110
PGRPPPRHGW
120
AEAFAGIRSA
130
HIKYICPHDF
140
ALFSRFNIIG
150
LSPDSLEDET
160
GIKQAAENVK
170
SLIEQEVKNG
180
IPSNRIILGG
190
FSQGGALSLY
200
TALTTHQKLA
210
GVTALSCWLP
220
LRSSFPECPI
230
SGVNRDIPIL
240
QCHGVLDPLV
250
PLMFGSLTVE
260
RLKTLVNPAN
270
VTFKTYEGMM
280
HSSCQQEMLD
290
VKQFIEKLLP
PID
Gene Ontology
| Classification |
GO ID |
Description |
| 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 |
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.