PLA2G15
entrez
23659
canonical
uniprot
Q8NCC3
canonical
ensembl
ENSG00000103066
resolver
ensp
ENSP00000219345
resolver
ensp
ENSP00000394197
resolver
ensp
ENSP00000455461
resolver
ensp
ENSP00000457034
resolver
ensp
ENSP00000563687
resolver
enst
ENST00000566188
resolver
genesymbol
PLA2G15
resolver
genesymbol_syn
LYPLA3
resolver
hgnc
HGNC:17163
resolver
uniprot
B3KMF3
resolver
uniprot
B4DJW4
resolver
uniprot
B4DUD1
resolver
uniprot
H3BT59
resolver
uniprot
Q53GZ1
resolver
uniprot
Q9NPQ6
resolver
uniprot
Q9UG04
resolver
uniprot
Q9Y2B3
resolver
uniprot_entry
B4DJW4_HUMAN
resolver
uniprot_entry
H3BT59_HUMAN
resolver
uniprot_entry
PAG15_HUMAN
resolver
uniprot_sec
B3KMF3
resolver
uniprot_sec
B4DUD1
resolver
uniprot_sec
Q53GZ1
resolver
uniprot_sec
Q9NPQ6
resolver
uniprot_sec
Q9UG04
resolver
uniprot_sec
Q9Y2B3
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by zinc ions at neutral pH. Zinc ions in plasma may keep the enzyme from hydrolyzing inappropriate substrates. {ECO:0000269|PubMed:30830753}.
uniprot
proteins
amino_acid_sequence
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
3.1.1.32
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
function
FUNCTION: Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:25727495, PubMed:29724779). Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity) (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:25727495, PubMed:29724779, PubMed:36823305). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines (PubMed:29724779, PubMed:36823305). Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines, phosphatidylethanolamines, and phosphatidylglycerols (PubMed:36823305). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide (PubMed:29724779). Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress (PubMed:30830753). Required for normal phospholipid degradation in alveolar macrophages with potential implications in the clearance of pulmonary surfactant, which is mainly composed of dipalmitoylphosphatidylcholine (1,2-dihexadecanoyl-sn-glycero-3-phosphocholine) (By similarity). Involved in the first step of bis(monoacylglycero)phosphate (BMP) de novo synthesis from phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (PubMed:36823305). BMP is an important player in cargo sorting and degradation, regulation of cellular cholesterol levels and intercellular communication (PubMed:36823305). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (PubMed:10092508). {ECO:0000250|UniProtKB:Q8VEB4, ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020, ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495, ECO:0000269|PubMed:29724779, ECO:0000269|PubMed:30830753, ECO:0000269|PubMed:36823305}.
uniprot
proteins
mass_dalton
46658
uniprot
proteins
mutagenesis
MUTAGEN 46; /note="D->A,C: Decreases membrane binding, phospholipase and transacylase activity at acidic pH."; /evidence="ECO:0000269|PubMed:25727495, ECO:0000269|PubMed:29724779"; MUTAGEN 46; /note="D->F: Has no effect on membrane binding or transacylase activity at acidic pH. Increases membrane binding and transacylase activity at neutral pH by 2-fold and 8-fold, respectively."; /evidence="ECO:0000269|PubMed:29724779"; MUTAGEN 83; /note="L->S: No effect on phospholipase activity. Strongly decreases transacylase activity and association with membranes."; /evidence="ECO:0000269|PubMed:25727495"; MUTAGEN 85; /note="V->S: No effect on phospholipase activity. Strongly decreases transacylase activity and association with membranes."; /evidence="ECO:0000269|PubMed:25727495"; MUTAGEN 99; /note="N->A: Loss of glycosylation site. Leads to retention in the endoplasmic reticulum and nearly abolishes the production of the mature, active enzyme."; /evidence="ECO:0000269|PubMed:23958596"; MUTAGEN 198; /note="S->A: Abolishes phospholipase and transacylase activity. Abolishes association with membranes."; /evidence="ECO:0000269|PubMed:25727495"; MUTAGEN 235; /note="K->A: No effect on phospholipase activity. Abolishes transacylase activity. Has no effect on association with membranes."; /evidence="ECO:0000269|PubMed:25727495"; MUTAGEN 273; /note="N->A: Loss of glycosylation site. Mildly reduces production of the mature, active enzyme."; /evidence="ECO:0000269|PubMed:23958596"; MUTAGEN 289; /note="N->A: Loss of glycosylation site. Mildly reduces production of the mature, active enzyme."; /evidence="ECO:0000269|PubMed:23958596"; MUTAGEN 362; /note="T->A: No effect on phospholipase activity. Strongly decreases transacylase activity and abolishes association with membranes."; /evidence="ECO:0000269|PubMed:25727495"; MUTAGEN 398; /note="N->A: Loss of glycosylation site. Slightly reduces production of the mature, active enzyme."; /evidence="ECO:0000269|PubMed:23958596
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:11790796, PubMed:23958596). N-glycosylation is important for maturation of the enzyme and normal subcellular location (PubMed:23958596). {ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:23958596}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
10092508
uniprot
proteins
pubmed
11790796
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
20410020
uniprot
proteins
pubmed
23958596
uniprot
proteins
pubmed
25727495
uniprot
proteins
pubmed
29724779
uniprot
proteins
pubmed
30830753
uniprot
proteins
pubmed
36823305
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:23958596}. Secreted {ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:20410020}. Membrane {ECO:0000269|PubMed:25727495}; Peripheral membrane protein {ECO:0000269|PubMed:25727495}.
uniprot
proteins