PLA2G1B
entrez
5319
canonical
uniprot
P04054
canonical
ensembl
ENSG00000170890
resolver
ensp
ENSP00000312286
resolver
enst
ENST00000308366
resolver
genesymbol
PLA2G1B
resolver
genesymbol_syn
PLA2
resolver
genesymbol_syn
PLA2A
resolver
genesymbol_syn
PPLA2
resolver
hgnc
HGNC:9030
resolver
uniprot
B2R4H5
resolver
uniprot
Q3KPI1
resolver
uniprot_entry
PA21B_HUMAN
resolver
uniprot_sec
B2R4H5
resolver
uniprot_sec
Q3KPI1
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by bile acid salts. Up-regulated by cholate and down-regulated by taurochenodeoxycholate. Cholate-activated rate of hydrolysis is lowered by hypolipidemic drug ezetimibe. {ECO:0000269|PubMed:17603006}.
uniprot
proteins
amino_acid_sequence
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNCDRNAAICFSKAPYNKAHKNLDTKKYCQS
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 (PubMed:10681567, PubMed:1420353, PubMed:17603006). 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 (PubMed:10681567, PubMed:1420353, PubMed:17603006). 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:25335547, PubMed:7721806). Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis (PubMed:25335547). Has anti-helminth activity in a process regulated by gut microbiota. 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 (By similarity). {ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:1420353, ECO:0000269|PubMed:17603006, ECO:0000269|PubMed:25335547, ECO:0000269|PubMed:7721806}.
uniprot
proteins
mass_dalton
16360
uniprot
proteins
post_translational_modification
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000269|PubMed:19297324, ECO:0000269|PubMed:6349696}.
uniprot
proteins
protein_family
Phospholipase A2 family
uniprot
proteins
pubmed
10681567
uniprot
proteins
pubmed
1420353
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17603006
uniprot
proteins
pubmed
19297324
uniprot
proteins
pubmed
25335547
uniprot
proteins
pubmed
3028739
uniprot
proteins
pubmed
6349696
uniprot
proteins
pubmed
7060561
uniprot
proteins
pubmed
7721806
uniprot
proteins
sequence_length
148
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19297324}. Note=Secreted from pancreatic acinar cells in its inactive form.
uniprot
proteins