LYPLA1
entrez
10434
canonical
uniprot
O75608
canonical
ensembl
ENSG00000120992
resolver
ensp
ENSP00000320043
resolver
ensp
ENSP00000344477
resolver
ensp
ENSP00000428729
resolver
ensp
ENSP00000482430
resolver
ensp
ENSP00000484280
resolver
ensp
ENSP00000543127
resolver
enst
ENST00000618741
resolver
enst
ENST00000618914
resolver
genesymbol
LYPLA1
resolver
genesymbol_syn
APT1
resolver
genesymbol_syn
LPL1
resolver
hgnc
HGNC:6737
resolver
uniprot
A0A087WZ75
resolver
uniprot
A0A087X1K9
resolver
uniprot
B4DP64
resolver
uniprot
O43202
resolver
uniprot
Q6IAQ1
resolver
uniprot
Q9UQF9
resolver
uniprot_entry
A0A087WZ75_HUMAN
resolver
uniprot_entry
A0A087X1K9_HUMAN
resolver
uniprot_entry
B4DP64_HUMAN
resolver
uniprot_entry
LYPA1_HUMAN
resolver
uniprot_entry
Q6IAQ1_HUMAN
resolver
uniprot_sec
O43202
resolver
uniprot_sec
Q9UQF9
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by palmostatin-B, leading to impair depalmitoylating of Ras. {ECO:0000269|PubMed:20418879}.
uniprot
proteins
amino_acid_sequence
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
uniprot
proteins
ec_number
3.1.2.-
uniprot
proteins
ec_number
3.1.2.22
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:19439193, ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:21393252, ECO:0000269|PubMed:22399288, ECO:0000269|PubMed:27481942, ECO:0000269|PubMed:37802024}.
uniprot
proteins
mass_dalton
24670
uniprot
proteins
mutagenesis
MUTAGEN 119; /note="S->A: Loss of thioesterase and lysophospholipase activity."; /evidence="ECO:0000269|PubMed:19439193, ECO:0000269|PubMed:37802024
uniprot
proteins
protein_family
AB hydrolase 2 family
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11080636
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19439193
uniprot
proteins
pubmed
20418879
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21393252
uniprot
proteins
pubmed
22399288
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27481942
uniprot
proteins
pubmed
37802024
uniprot
proteins
sequence_length
230
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19439193}. Cell membrane {ECO:0000269|PubMed:19439193}. Nucleus membrane {ECO:0000269|PubMed:19439193}. Endoplasmic reticulum {ECO:0000269|PubMed:19439193}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000269|PubMed:19439193}.
uniprot
proteins