Pla2g15
entrez
192654
canonical
uniprot
Q8VEB4
canonical
ensembl
ENSMUSG00000031903
resolver
ensp
ENSMUSP00000034377
resolver
ensp
ENSMUSP00000148565
resolver
enst
ENSMUST00000034377
resolver
enst
ENSMUST00000212963
resolver
genesymbol
Pla2g15
resolver
genesymbol_syn
Lypla3
resolver
uniprot
A0A1D5RLZ5
resolver
uniprot
Q3TCB1
resolver
uniprot
Q3U303
resolver
uniprot_entry
A0A1D5RLZ5_MOUSE
resolver
uniprot_entry
PAG15_MOUSE
resolver
uniprot_sec
Q3TCB1
resolver
uniprot_sec
Q3U303
resolver
activity_regulation
ACTIVITY REGULATION: Phospholipase sn-2 versus sn-1 positional specificity is affected by the phospholipid composition of membranes. Phospholipase A2 activity toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (PAPE) is enhanced in the presence of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), which promotes lipid bilayer formation (PubMed:16837646). O-acyltransferase activity is inhibited by antiarrhythmic drug amiodarone (PubMed:27993948). {ECO:0000269|PubMed:16837646, ECO:0000269|PubMed:27993948}.
uniprot
proteins
amino_acid_sequence
MDRHLCTCRETQLRSGLLLPLFLLMMLADLTLPAQRHPPVVLVPGDLGNQLEAKLDKPKVVHYLCSKKTDSYFTLWLNLELLLPVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVPGFGETFSMEFLDPSKRNVGSYFYTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQMYGGPVVLVAHSMGNVYMLYFLQRQPQVWKDKYIHAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNHTWSHEKVFVYTPTTNYTLRDYHRFFRDIGFEDGWFMRQDTEGLVEAMTPPGVELHCLYGTGVPTPNSFYYESFPDRDPKICFGDGDGTVNLESVLQCQAWQSRQEHRVSLQELPGSEHIEMLANATTLAYLKRVLLEP
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:11790796, PubMed:16106046, PubMed:16837646, PubMed:16880524, PubMed:17626977, PubMed:19017977, PubMed:20410020). 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). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines (PubMed:15294901, PubMed:20410020). Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines, phosphatidylethanolamines, and phosphatidylglycerols (By similarity) (PubMed:16837646, PubMed:17626977). 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:16837646, PubMed:17626977). 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:27993948). 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) (PubMed:15294901, PubMed:16880524, PubMed:19017977). 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) (By similarity). BMP is an important player in cargo sorting and degradation, regulation of cellular cholesterol levels and intercellular communication. At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (By similarity). {ECO:0000250|UniProtKB:Q8NCC3, ECO:0000269|PubMed:15294901, ECO:0000269|PubMed:16837646, ECO:0000269|PubMed:16880524, ECO:0000269|PubMed:17626977, ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020, ECO:0000269|PubMed:27993948}.
uniprot
proteins
mass_dalton
47307
uniprot
proteins
mutagenesis
MUTAGEN 65; /note="C->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:16106046"; MUTAGEN 89; /note="C->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:16106046"; MUTAGEN 198; /note="S->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:16106046"; MUTAGEN 360; /note="D->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:16106046"; MUTAGEN 392; /note="H->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:16106046
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:11790796). N-glycosylation is important for maturation of the enzyme and normal subcellular location (By similarity). {ECO:0000250|UniProtKB:Q8NCC3, ECO:0000269|PubMed:11790796}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
11790796
uniprot
proteins
pubmed
15294901
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16106046
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16837646
uniprot
proteins
pubmed
16880524
uniprot
proteins
pubmed
17626977
uniprot
proteins
pubmed
19017977
uniprot
proteins
pubmed
20410020
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27993948
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020}. Lysosome {ECO:0000269|PubMed:19017977}. Membrane {ECO:0000250|UniProtKB:Q8NCC3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NCC3}.
uniprot
proteins