PLA2G3
entrez
50487
canonical
uniprot
Q9NZ20
canonical
ensembl
ENSG00000100078
resolver
ensp
ENSP00000215885
resolver
enst
ENST00000215885
resolver
genesymbol
PLA2G3
resolver
hgnc
HGNC:17934
resolver
uniprot
O95768
resolver
uniprot_entry
PA2G3_HUMAN
resolver
uniprot_sec
O95768
resolver
activity_regulation
ACTIVITY REGULATION: Arachidonic acid release is markedly increased by glypican, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan. {ECO:0000269|PubMed:12522102}.
uniprot
proteins
amino_acid_sequence
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHARWDAHRRLQSCSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRALEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVLEIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPPKPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWVCRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPLRGPMSFYNQCLQLTQAARRPDRQQKSWSQ
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
function
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids without apparent head group selectivity (PubMed:12522102, PubMed:15863501, PubMed:18801741, PubMed:28947740). Contributes to phospholipid remodeling of low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (PubMed:18801741). May act in an autocrine and paracrine manner (PubMed:23624557). Secreted by immature mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2 (PGD2), which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). Secreted by epididymal epithelium, acts on immature sperm cells within the duct, modulating the degree of unsaturation of the fatty acyl components of phosphatidylcholines required for acrosome assembly and sperm cell motility. Facilitates the replacement of fatty acyl chains in phosphatidylcholines in sperm membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6 PUFAs to generate oxygenated lipid mediators in the male reproductive tract (By similarity). At pericentrosomal preciliary compartment, negatively regulates ciliogenesis likely by regulating endocytotic recycling of ciliary membrane protein (PubMed:20393563). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (PubMed:12522102, PubMed:15863501). At colonic epithelial barrier, preferentially hydrolyzes phospholipids having arachidonate and docosahexaenoate at sn-2 position, contributing to the generation of oxygenated metabolites involved in colonic stem cell homeostasis (PubMed:28947740). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (PubMed:17868035). {ECO:0000250|UniProtKB:Q8BZT7, ECO:0000269|PubMed:12522102, ECO:0000269|PubMed:15863501, ECO:0000269|PubMed:17868035, ECO:0000269|PubMed:18801741, ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:23624557, ECO:0000269|PubMed:28947740}.
uniprot
proteins
mass_dalton
57167
uniprot
proteins
mutagenesis
MUTAGEN 167; /note="N->S: Loss of glycosylation."; /evidence="ECO:0000269|PubMed:15863501"; MUTAGEN 184; /note="H->Q: Impairs PGE2 synthesis. Impairs PGD2 synthesis. Impairs mast cell degranulation. Impairs neurite outgrowth."; /evidence="ECO:0000269|PubMed:12522102, ECO:0000269|PubMed:15863501, ECO:0000269|PubMed:17868035, ECO:0000269|PubMed:23624557"; MUTAGEN 280; /note="N->S: Loss of glycosylation."; /evidence="ECO:0000269|PubMed:15863501
uniprot
proteins
post_translational_modification
PTM: N-glycosylation does not affect the catalytic activity, but is required for proper secretion. A nonglycosylated form is observed in several cell types. {ECO:0000269|PubMed:15863501}.; PTM: In several cell types, the N- and C-termini are cleaved off. {ECO:0000305|PubMed:15863501}.
uniprot
proteins
protein_family
Phospholipase A2 family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10713052
uniprot
proteins
pubmed
12522102
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15863501
uniprot
proteins
pubmed
17868035
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18801741
uniprot
proteins
pubmed
20393563
uniprot
proteins
pubmed
23624557
uniprot
proteins
pubmed
28947740
uniprot
proteins
sequence_length
509
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12522102}. Cell membrane {ECO:0000269|PubMed:12522102}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:20393563}. Recycling endosome {ECO:0000269|PubMed:20393563}. Note=Localized at pericentrosomal preciliary compartment. {ECO:0000269|PubMed:20393563}.
uniprot
proteins