Pla2g1b
entrez
18778
canonical
uniprot
Q9Z0Y2
canonical
ensembl
ENSMUSG00000029522
resolver
ensp
ENSMUSP00000031495
resolver
ensp
ENSMUSP00000107702
resolver
ensp
ENSMUSP00000120743
resolver
enst
ENSMUST00000031495
resolver
enst
ENSMUST00000112071
resolver
genesymbol
Pla2g1b
resolver
genesymbol_syn
Pla2
resolver
uniprot
A6H6K5
resolver
uniprot
D3Z1N8
resolver
uniprot
Q9D7E2
resolver
uniprot
Q9D884
resolver
uniprot_entry
D3Z1N8_MOUSE
resolver
uniprot_entry
PA21B_MOUSE
resolver
uniprot_sec
A6H6K5
resolver
uniprot_sec
Q9D7E2
resolver
uniprot_sec
Q9D884
resolver
amino_acid_sequence
MKLLLLAALLTAGAAAHSISPRAVWQFRNMIKCTIPGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKLESCKFLIDNPYTNTYSYSCSGSEITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLDTGKFC
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
function
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (By similarity). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (PubMed:10066760). Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis (By similarity). Has anti-helminth activity in a process regulated by gut microbiota (PubMed:29024642). Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (PubMed:29024642). {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000269|PubMed:10066760, ECO:0000269|PubMed:29024642}.
uniprot
proteins
mass_dalton
16290
uniprot
proteins
post_translational_modification
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}.
uniprot
proteins
protein_family
Phospholipase A2 family
uniprot
proteins
pubmed
10066760
uniprot
proteins
pubmed
10531350
uniprot
proteins
pubmed
10689188
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21908646
uniprot
proteins
pubmed
29024642
uniprot
proteins
sequence_length
146
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
uniprot
proteins