ID   PA24A_RAT               Reviewed;         752 AA.
AC   P50393;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Cytosolic phospholipase A2;
DE            Short=cPLA2;
DE   AltName: Full=Phospholipase A2 group IVA;
DE   Includes:
DE     RecName: Full=Phospholipase A2;
DE              EC=3.1.1.4 {ECO:0000250|UniProtKB:P47712};
DE     AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Includes:
DE     RecName: Full=Lysophospholipase;
DE              EC=3.1.1.5 {ECO:0000250|UniProtKB:P47712};
GN   Name=Pla2g4a; Synonyms=Cpla2, Pla2g4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Brain;
RX   PubMed=7808237; DOI=10.1016/0169-328x(94)90174-0;
RA   Owada Y., Tominaga T., Yoshimoto T., Kondo H.;
RT   "Molecular cloning of rat cDNA for cytosolic phospholipase A2 and the
RT   increased gene expression in the dentate gyrus following transient
RT   forebrain ischemia.";
RL   Brain Res. Mol. Brain Res. 25:364-368(1994).
RN   [2]
RP   ERRATUM OF PUBMED:7808237.
RX   PubMed=7898324; DOI=10.1016/0169-328x(94)90023-x;
RA   Owada Y., Tominaga T., Yoshimoto T., Kondo H.;
RL   Brain Res. Mol. Brain Res. 27:355-355(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Pancreatic islet;
RX   PubMed=9555100; DOI=10.1016/s0005-2760(98)00027-7;
RA   Ma Z., Ramanadham S., Hu Z., Turk J.;
RT   "Cloning and expression of a group IV cytosolic Ca2+-dependent
RT   phospholipase A2 from rat pancreatic islets. Comparison of the expressed
RT   activity with that of an islet group VI cytosolic Ca2+-independent
RT   phospholipase A2.";
RL   Biochim. Biophys. Acta 1391:384-400(1998).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-437; SER-511;
RP   SER-515 AND SER-727, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Has primarily calcium-dependent phospholipase and
CC       lysophospholipase activities, with a major role in membrane lipid
CC       remodeling and biosynthesis of lipid mediators of the inflammatory
CC       response (By similarity). Plays an important role in embryo
CC       implantation and parturition through its ability to trigger prostanoid
CC       production (By similarity). Preferentially hydrolyzes the ester bond of
CC       the fatty acyl group attached at sn-2 position of phospholipids
CC       (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl
CC       group from membrane phospholipids, providing the precursor for
CC       eicosanoid biosynthesis via the cyclooxygenase pathway. In an
CC       alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty
CC       acyl chain of eicosanoid lysophopholipids to release free bioactive
CC       eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached
CC       at sn-1 position of phospholipids (phospholipase A1 activity) only if
CC       an ether linkage rather than an ester linkage is present at the sn-2
CC       position. This hydrolysis is not stereospecific. Has calcium-
CC       independent phospholipase A2 and lysophospholipase activities in the
CC       presence of phosphoinositides. Has O-acyltransferase activity.
CC       Catalyzes the transfer of fatty acyl chains from phospholipids to a
CC       primary hydroxyl group of glycerol (sn-1 or sn-3), potentially
CC       contributing to monoacylglycerol synthesis (By similarity).
CC       {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:41075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:60657, ChEBI:CHEBI:74344;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41076;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         octadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC         glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC         ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1-
CC         octadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:41307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32387, ChEBI:CHEBI:73858, ChEBI:CHEBI:78022;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41308;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-hexadecanoyl-sn-glycero-
CC         3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC         glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41071, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:77694;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41072;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC         phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-
CC         hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:55430, ChEBI:CHEBI:64496;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol)
CC         + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:41123,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:72828, ChEBI:CHEBI:75163;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41124;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         octadecanoyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:40451,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:74565, ChEBI:CHEBI:77091;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40452;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphoethanolamine + H2O =
CC         H(+) + prostaglandin E2 + sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:53704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:137581, ChEBI:CHEBI:143890, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53705;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-
CC         3-phosphocholine + H2O = (15S)-hydroxy-(5Z,8Z,11Z,13E)-
CC         eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:53700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:57409, ChEBI:CHEBI:137584;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53701;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-
CC         3-phosphocholine + H2O = (15R)-hydroxy-(5Z,8Z,11Z,13E)-
CC         eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:53696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:78837, ChEBI:CHEBI:137583;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53697;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphocholine + H2O = H(+)
CC         + prostaglandin E2 + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:53692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:137585, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53693;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-
CC         3-phosphocholine + H2O = (11R)-hydroxy-(5Z,8Z,12E,14Z)-
CC         eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:53688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:78836, ChEBI:CHEBI:137582;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53689;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-
CC         phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-
CC         hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41271,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:77695, ChEBI:CHEBI:77696;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-
CC         glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine;
CC         Xref=Rhea:RHEA:41099, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858,
CC         ChEBI:CHEBI:74965, ChEBI:CHEBI:75612;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41100;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC         phosphocholine + glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-glycerol
CC         + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41087,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:75610,
CC         ChEBI:CHEBI:78022; Evidence={ECO:0000250|UniProtKB:P47712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41088;
CC         Evidence={ECO:0000250|UniProtKB:P47712};
CC   -!- ACTIVITY REGULATION: Activated by cytosolic calcium, which is necessary
CC       for binding to membrane lipids. Activated by phosphorylation in
CC       response to mitogenic stimuli. {ECO:0000250|UniProtKB:P47712,
CC       ECO:0000250|UniProtKB:P47713}.
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000250|UniProtKB:P47712}.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000250|UniProtKB:P47713}.
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000250|UniProtKB:P47712}.
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC       {ECO:0000250|UniProtKB:P47712}.
CC   -!- SUBUNIT: Interacts with KAT5. {ECO:0000250|UniProtKB:P47712}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi
CC       apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope
CC       {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular
CC       membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
CC   -!- TISSUE SPECIFICITY: In brain tissue, expressed in low levels in
CC       olfactory mitral and granule cells, in hippocampal pyramidal cells and
CC       in dentate and cerebellar granule cells. {ECO:0000269|PubMed:7808237}.
CC   -!- INDUCTION: Levels of rat CPLA2 are increased in dentate granule cells
CC       during ischemia. {ECO:0000269|PubMed:7808237}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. It modulates enzyme activity by presenting the active
CC       site to its substrate in response to elevations of cytosolic calcium.
CC       In the presence of phosphoinositides, regulates phospholipase A2 and
CC       lysophospholipase activities in a calcium-independent way.
CC       {ECO:0000250|UniProtKB:P47712}.
CC   -!- PTM: Phosphorylated at both Ser-505 and Ser-727 in response to
CC       mitogenic stimuli. {ECO:0000250|UniProtKB:P47712}.
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DR   EMBL; S77829; AAB33847.1; -; mRNA.
DR   EMBL; U38376; AAC21591.1; -; mRNA.
DR   AlphaFoldDB; P50393; -.
DR   BMRB; P50393; -.
DR   SMR; P50393; -.
DR   STRING; 10116.ENSRNOP00000075329; -.
DR   iPTMnet; P50393; -.
DR   PhosphoSitePlus; P50393; -.
DR   PaxDb; 10116-ENSRNOP00000003630; -.
DR   UCSC; RGD:67366; rat.
DR   AGR; RGD:67366; -.
DR   RGD; 67366; Pla2g4a.
DR   eggNOG; KOG1012; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   InParanoid; P50393; -.
DR   PhylomeDB; P50393; -.
DR   Reactome; R-RNO-111995; phospho-PLA2 pathway.
DR   Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-RNO-1482798; Acyl chain remodeling of CL.
DR   Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-RNO-1483115; Hydrolysis of LPC.
DR   Reactome; R-RNO-1483166; Synthesis of PA.
DR   Reactome; R-RNO-2142753; Arachidonic acid metabolism.
DR   Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-RNO-432142; Platelet sensitization by LDL.
DR   Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   UniPathway; UPA00383; -.
DR   UniPathway; UPA00662; -.
DR   UniPathway; UPA00878; -.
DR   UniPathway; UPA00940; -.
DR   PRO; PR:P50393; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:RGD.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISO:RGD.
DR   GO; GO:1902387; F:ceramide 1-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IPI:RGD.
DR   GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR   GO; GO:0008374; F:O-acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0004623; F:phospholipase A2 activity; ISO:RGD.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IMP:RGD.
DR   GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR   GO; GO:0071236; P:cellular response to antibiotic; ISO:RGD.
DR   GO; GO:0046697; P:decidualization; IMP:RGD.
DR   GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0046456; P:icosanoid biosynthetic process; ISO:RGD.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; ISO:RGD.
DR   GO; GO:0001554; P:luteolysis; IEP:RGD.
DR   GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; IMP:RGD.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISO:RGD.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR   GO; GO:0034478; P:phosphatidylglycerol catabolic process; ISS:UniProtKB.
DR   GO; GO:0006663; P:platelet activating factor biosynthetic process; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IEP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0031622; P:positive regulation of fever generation; IEP:RGD.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD.
DR   GO; GO:0010572; P:positive regulation of platelet activation; ISO:RGD.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:RGD.
DR   GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:RGD.
DR   GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; ISO:RGD.
DR   GO; GO:0031340; P:positive regulation of vesicle fusion; IMP:RGD.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0051592; P:response to calcium ion; IMP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IMP:RGD.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR   GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR   GO; GO:0043129; P:surfactant homeostasis; IMP:RGD.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   CDD; cd07200; cPLA2_Grp-IVA; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF13; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Glycerol metabolism; Golgi apparatus; Hydrolase; Isopeptide bond;
KW   Leukotriene biosynthesis; Lipid biosynthesis; Lipid degradation;
KW   Lipid metabolism; Lipid-binding; Membrane; Metal-binding; Nucleus;
KW   Phospholipid degradation; Phospholipid metabolism; Phosphoprotein;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..752
FT                   /note="Cytosolic phospholipase A2"
FT                   /id="PRO_0000187264"
FT   DOMAIN          6..122
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          140..740
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   REGION          1..178
FT                   /note="Phospholipid binding"
FT                   /evidence="ECO:0000305"
FT   REGION          427..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        228
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        549
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   MOD_RES         268
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         505
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         515
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         727
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   CROSSLNK        541
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   CROSSLNK        606
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   CONFLICT        139
FT                   /note="C -> S (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="R -> Q (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="Q -> L (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308..310
FT                   /note="MST -> IVP (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        410
FT                   /note="S -> L (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="E -> V (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        635
FT                   /note="P -> T (in Ref. 3; AAC21591)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   752 AA;  85707 MW;  C68F71BB05FBF732 CRC64;
     MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI STTPDSRKRT
     RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV
     PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL CDQEKTFRRQ RKENIKENMK KLLGPKKSEG
     LYSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH
     PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
     ETLIQNRMST TLSSLKEKVS AARCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
     TFMTPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QNKGSTMEEE
     LENITAKHIV SNDSSDSDDE AQGPKGTENE DAEREYQNDN QASWVHRMLM ALVSDSALFN
     TREGRAGKEH NFMLGLNLNT SYPLSPLRDF SPQDSFDDDE LDAAVADPDE FERIYEPLDV
     KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDTSPPFKEL LLAEKWAKMN
     KLPFPKIDPY VFDREGLKEC YVFKPKNPDV EKDCPTIIHF VLANINFRKY KAPGVLRETK
     EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMYFN TLNNIDVIKD AIVESIEYRR
     QNPSRCSVSL SNVEARKFFN KEFLSKPTAE SI
//