PLA2G2A
entrez
5320
canonical
uniprot
P14555
canonical
ensembl
ENSG00000188257
resolver
ensp
ENSP00000364252
resolver
ensp
ENSP00000383364
resolver
ensp
ENSP00000504762
resolver
ensp
ENSP00000577343
resolver
ensp
ENSP00000577344
resolver
ensp
ENSP00000577345
resolver
ensp
ENSP00000577346
resolver
ensp
ENSP00000602075
resolver
ensp
ENSP00000632682
resolver
enst
ENST00000375111
resolver
enst
ENST00000400520
resolver
enst
ENST00000482011
resolver
enst
ENST00000907283
resolver
enst
ENST00000907285
resolver
enst
ENST00000907286
resolver
enst
ENST00000907287
resolver
enst
ENST00000932016
resolver
enst
ENST00000962623
resolver
genesymbol
PLA2G2A
resolver
genesymbol_syn
PLA2B
resolver
genesymbol_syn
PLA2L
resolver
genesymbol_syn
RASF-A
resolver
hgnc
HGNC:9031
resolver
uniprot
A8K5I7
resolver
uniprot
Q6DN24
resolver
uniprot
Q6IBD9
resolver
uniprot
Q9UCD2
resolver
uniprot_entry
PA2GA_HUMAN
resolver
uniprot_sec
A8K5I7
resolver
uniprot_sec
Q6DN24
resolver
uniprot_sec
Q6IBD9
resolver
uniprot_sec
Q9UCD2
resolver
amino_acid_sequence
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHCRGSTPRC
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
function
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (PubMed:10455175, PubMed:10681567, PubMed:2925633). 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:10455175, PubMed:10681567). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:10358193, PubMed:11694541). Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (PubMed:25082876). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (PubMed:14998370). Independent of its catalytic activity, acts as a ligand for integrins (PubMed:18635536, PubMed:25398877). Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 (PubMed:18635536, PubMed:25398877). Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:25398877). Induces cell proliferation in an integrin-dependent manner (PubMed:18635536). {ECO:0000250|UniProtKB:P31482, ECO:0000269|PubMed:10358193, ECO:0000269|PubMed:10455175, ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:11694541, ECO:0000269|PubMed:14998370, ECO:0000269|PubMed:25082876, ECO:0000269|PubMed:2925633}.
uniprot
proteins
mass_dalton
16083
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="R->E: Reduces bactericidal activity to 20% against B.subtilis and to 4% against S.aureus. Complete loss of bactericidal activity; when associated with E-30 and E-35."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 30; /note="K->E: Complete loss of bactericidal activity; when associated with E-27 and E-35."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 35; /note="K->E: Complete loss of bactericidal activity; when associated with E-27 and E-30."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 49; /note="G->S: No effect on integrin binding; when associated with K-68."; /evidence="ECO:0000269|PubMed:25398877"; MUTAGEN 57; /note="K->E: Impairs bactericidal activity; when associated with E-128."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 62; /note="R->E: No effect on integrin binding."; /evidence="ECO:0000269|PubMed:18635536"; MUTAGEN 67; /note="H->Q: Catalytically inactive but does not affect integrin binding. Impairs leukotriene B4 synthesis in activated neutrophils."; /evidence="ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:25082876, ECO:0000269|PubMed:25398877"; MUTAGEN 68; /note="D->K: No effect on integrin binding; when associated with S-49."; /evidence="ECO:0000269|PubMed:25398877"; MUTAGEN 72; /note="K->E: Impairs bactericidal activity; when associated with E-73 and E-77."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 73; /note="R->E: Impairs bactericidal activity; when associated with E-72 and E-77."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 73; /note="R->E: Slightly reduced integrin binding."; /evidence="ECO:0000269|PubMed:18635536"; MUTAGEN 77; /note="R->E: Impairs bactericidal activity; when associated with E-72 and E-73."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 87; /note="K->E: Reduces bactericidal activity to 20% against B.subtilis and to 10% against S.aureus. Complete loss of bactericidal activity; when associated with E-99 and E-104."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 94; /note="R->E: Moderately reduced integrin binding. Greatly reduced integrin binding but no effect on catalytic activity; when associated with E-120."; /evidence="ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:25398877"; MUTAGEN 99; /note="K->E: Reduces bactericidal activity to 25% against B.subtilis and to 10% against S.aureus. Complete loss of bactericidal activity; when associated with E-87 and E-104."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 104; /note="R->E: Reduces bactericidal activity to 18% against B.subtilis and to 12% against S.aureus. Complete loss of bactericidal activity; when associated with E-87 and E-99."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 120; /note="R->E: Moderately reduced integrin binding. Greatly reduced integrin binding but no effect on catalytic activity; when associated with E-94."; /evidence="ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:25398877"; MUTAGEN 122; /note="K->E: Impairs bactericidal activity; when associated with E-127."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 127; /note="K->E: Impairs bactericidal activity; when associated with E-122."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 128; /note="K->E: Impairs bactericidal activity; when associated with E-57."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 135; /note="K->E: Impairs bactericidal activity; when associated with D-138."; /evidence="ECO:0000269|PubMed:11694541"; MUTAGEN 138; /note="R->D: Impairs bactericidal activity; when associated with E-135."; /evidence="ECO:0000269|PubMed:11694541
uniprot
proteins
protein_family
Phospholipase A2 family
uniprot
proteins
pubmed
10358193
uniprot
proteins
pubmed
10455175
uniprot
proteins
pubmed
10681567
uniprot
proteins
pubmed
11694541
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14998370
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18635536
uniprot
proteins
pubmed
1948070
uniprot
proteins
pubmed
2062381
uniprot
proteins
pubmed
2239446
uniprot
proteins
pubmed
23164706
uniprot
proteins
pubmed
25082876
uniprot
proteins
pubmed
25398877
uniprot
proteins
pubmed
2775276
uniprot
proteins
pubmed
2925608
uniprot
proteins
pubmed
2925633
uniprot
proteins
pubmed
3202859
uniprot
proteins
pubmed
3240982
uniprot
proteins
pubmed
7664108
uniprot
proteins
pubmed
8399335
uniprot
proteins
pubmed
9538252
uniprot
proteins
sequence_length
144
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2925608, ECO:0000269|PubMed:2925633}. Cell membrane {ECO:0000269|PubMed:2775276}; Peripheral membrane protein {ECO:0000305}. Mitochondrion outer membrane {ECO:0000269|PubMed:25082876}; Peripheral membrane protein {ECO:0000305}.
uniprot
proteins