PLA2G4A
entrez
5321
canonical
uniprot
P47712
canonical
ensembl
ENSG00000116711
resolver
ensp
ENSP00000356436
resolver
ensp
ENSP00000521173
resolver
ensp
ENSP00000521174
resolver
ensp
ENSP00000521175
resolver
ensp
ENSP00000614362
resolver
ensp
ENSP00000718144
resolver
enst
ENST00000367466
resolver
enst
ENST00000851114
resolver
enst
ENST00000851115
resolver
enst
ENST00000944303
resolver
genesymbol
PLA2G4A
resolver
genesymbol_syn
CPLA2
resolver
genesymbol_syn
PLA2G4
resolver
hgnc
HGNC:9035
resolver
uniprot
B1AKG4
resolver
uniprot
B4DZI4
resolver
uniprot
Q29R80
resolver
uniprot_entry
B4DZI4_HUMAN
resolver
uniprot_entry
PA24A_HUMAN
resolver
uniprot_sec
B1AKG4
resolver
uniprot_sec
Q29R80
resolver
activity_regulation
ACTIVITY REGULATION: Activated by cytosolic calcium, which is necessary for binding to membrane lipids (PubMed:12672805). Activated by phosphorylation in response to mitogenic stimuli (PubMed:8381049). Activated by ceramide-1-phosphate. Binding (via C2 domain) to ceramide-1-phosphate increases the affinity for membrane lipids (PubMed:17472963). Can be activated by phosphoinositides in the absence of calcium (PubMed:12672805). Inhibited by ANXA5 in a calcium- and substrate-dependent way (PubMed:9425121). {ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:8381049, ECO:0000269|PubMed:9425121}.
uniprot
proteins
amino_acid_sequence
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEVPFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEGLHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEELENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYRAPGVPRETEEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLSKPKA
uniprot
proteins
disease_involvement
DISEASE: Gastrointestinal ulceration, recurrent, with dysfunctional platelets (GURDP) [MIM:618372]: An autosomal recessive disorder characterized by recurrent gastrointestinal mucosal ulcers, gastrointestinal bleeding, chronic anemia, iron deficiency, and abdominal pain. Disease features also include platelet dysfunction, and globally decreased eicosanoid synthesis. {ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:23268370, ECO:0000269|PubMed:25102815}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
function
FUNCTION: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:10358058, PubMed:14709560, PubMed:16617059, PubMed:17472963, PubMed:18451993, PubMed:27642067, PubMed:7794891, PubMed:8619991, PubMed:8702602, PubMed:9425121). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:8619991, PubMed:9425121). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:9425121). In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophospholipids to release free bioactive eicosanoids (PubMed:27642067). Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific (PubMed:7794891). Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides (PubMed:12672805). Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (PubMed:7794891). {ECO:0000250|UniProtKB:P47713, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:27642067, ECO:0000269|PubMed:7794891, ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602, ECO:0000269|PubMed:9425121}.
uniprot
proteins
mass_dalton
85239
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="D->N: Impairs phospholipase A2 and lysophospholipase activities in the absence of phosphoinositides. Has full activity in the presence of phosphoinositides."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 57..59; /note="RKR->AAA: Impairs binding to ceramide-1-phosphate."; /evidence="ECO:0000269|PubMed:17472963"; MUTAGEN 139; /note="C->A: No effect on phospholipase activity; when associated with A-141 and A-151."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 141; /note="C->A: No effect on phospholipase activity; when associated with A-139 and A-151."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 151; /note="C->A: No effect on phospholipase activity; when associated with A-139 and A-141."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 195; /note="S->A: 5-fold reduced phospholipase and lysophospholipase activities. 100-fold reduced phospholipase and lysophospholipase activities; when associated with A-577."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 200; /note="R->A,H: Abolishes phospholipase activity."; /evidence="ECO:0000269|PubMed:8702602"; MUTAGEN 200; /note="R->K: Reduces phospholipase activity 200-fold."; /evidence="ECO:0000269|PubMed:8702602"; MUTAGEN 215; /note="S->A: No effect on phospholipase or lysophospholipase activity."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 220; /note="C->A: No effect on phospholipase activity."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 228; /note="S->A,C,T: Abolishes both phospholipase and lysophospholipase activities."; /evidence="ECO:0000269|PubMed:8083230, ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602"; MUTAGEN 324; /note="C->A: No effect on phospholipase activity; when associated with A-331."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 331; /note="C->A: No effect on phospholipase activity; when associated with A-324."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 437; /note="S->A: Reduces phospholipase A2 activity; when associated with A-454; A-505 and A-727."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 454; /note="S->A: Reduces phospholipase A2 activity; when associated with A-437; A-505 and A-727."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 488; /note="K->E: Impairs phosphoinositide-stimulated phospholipase A2 activity."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 505; /note="S->A: Decreases agonist-stimulated release of arachidonic acid. Reduces phospholipase A2 activity; when associated with A-437; A-454 and A-727."; /evidence="ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:8381049"; MUTAGEN 541; /note="K->A: Impairs phosphoinositide-stimulated phospholipase A2 activity; when associated with A-543 and A-544."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 543; /note="K->A: Impairs phosphoinositide-stimulated phospholipase A2 activity.; when associated with A-541 and A-544."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 544; /note="K->A: Impairs phosphoinositide-stimulated phospholipase A2 activity.; when associated with A-541 and A-543."; /evidence="ECO:0000269|PubMed:12672805"; MUTAGEN 549; /note="D->A: Abolishes phospholipiase activity."; /evidence="ECO:0000269|PubMed:8702602"; MUTAGEN 549; /note="D->E: Reduces phospholipase activity 2000-fold."; /evidence="ECO:0000269|PubMed:8702602"; MUTAGEN 549; /note="D->N: Reduces phospholipase activity 300-fold."; /evidence="ECO:0000269|PubMed:8702602"; MUTAGEN 577; /note="S->A: 7-fold reduced phospholipase and lysophospholipase activities. 100-fold reduced phospholipase and lysophospholipase activities; when associated with A-195."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 620; /note="C->A: No effect on phospholipase activity; when associated with A-634."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 634; /note="C->A: No effect on phospholipase activity; when associated with A-620."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 726; /note="C->A: No effect on phospholipase activity."; /evidence="ECO:0000269|PubMed:8083230"; MUTAGEN 727; /note="S->A: Reduces phospholipase A2 activity; when associated with A-437; A-455 and A-505."; /evidence="ECO:0000269|PubMed:12672805
uniprot
proteins
pathway_participation
PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000250|UniProtKB:P47713}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000269|PubMed:18451993}.; PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000269|PubMed:18451993}.; PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. {ECO:0000269|PubMed:18451993}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli. {ECO:0000269|PubMed:8381049, ECO:0000269|PubMed:9468497}.
uniprot
proteins
pubmed
10319815
uniprot
proteins
pubmed
10358058
uniprot
proteins
pubmed
11375391
uniprot
proteins
pubmed
11416127
uniprot
proteins
pubmed
12672805
uniprot
proteins
pubmed
14709560
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16617059
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17472963
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18451993
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1869522
uniprot
proteins
pubmed
1904318
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23268370
uniprot
proteins
pubmed
25102815
uniprot
proteins
pubmed
27642067
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
7794891
uniprot
proteins
pubmed
8083230
uniprot
proteins
pubmed
8381049
uniprot
proteins
pubmed
8619991
uniprot
proteins
pubmed
8702602
uniprot
proteins
pubmed
9425121
uniprot
proteins
pubmed
9430701
uniprot
proteins
pubmed
9468497
uniprot
proteins
pubmed
9665851
uniprot
proteins
sequence_length
749
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11375391}. Golgi apparatus membrane {ECO:0000269|PubMed:11375391}. Nucleus envelope. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000269|PubMed:11375391}.
uniprot
proteins