PA24A_BOVIN
ID PA24A_BOVIN Reviewed; 749 AA.
AC A4IFJ5; Q1XD55;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Follicular cell;
RX PubMed=16510840; DOI=10.1095/biolreprod.105.048579;
RA Diouf M.N., Sayasith K., Lefebvre R., Silversides D.W., Sirois J.,
RA Lussier J.G.;
RT "Expression of phospholipase A2 group IVA (PLA2G4A) is upregulated by human
RT chorionic gonadotropin in bovine granulosa cells of ovulatory follicles.";
RL Biol. Reprod. 74:1096-1103(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 = (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate
CC + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC 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: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000250|UniProtKB:P47713}.
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000250|UniProtKB:P47712}.
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: Detected in granulosa cells after stimulation with
CC chorionic gonadotropin (at protein level).
CC {ECO:0000269|PubMed:16510840}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in granulosa cells of ovulatory
CC follicles. Detected at low levels in granulosa cells during the rest of
CC the estrous cycle. {ECO:0000269|PubMed:16510840}.
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; AY363688; AAR17479.1; -; mRNA.
DR EMBL; BC134610; AAI34611.1; -; mRNA.
DR RefSeq; NP_001069332.1; NM_001075864.1.
DR AlphaFoldDB; A4IFJ5; -.
DR SMR; A4IFJ5; -.
DR STRING; 9913.ENSBTAP00000017685; -.
DR BindingDB; A4IFJ5; -.
DR ChEMBL; CHEMBL2304401; -.
DR PaxDb; A4IFJ5; -.
DR PeptideAtlas; A4IFJ5; -.
DR PRIDE; A4IFJ5; -.
DR Ensembl; ENSBTAT00000017685; ENSBTAP00000017685; ENSBTAG00000013298.
DR Ensembl; ENSBTAT00000078329; ENSBTAP00000056878; ENSBTAG00000013298.
DR GeneID; 525072; -.
DR KEGG; bta:525072; -.
DR CTD; 5321; -.
DR VEuPathDB; HostDB:ENSBTAG00000013298; -.
DR VGNC; VGNC:32960; PLA2G4A.
DR eggNOG; KOG1012; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_1_1_1; -.
DR InParanoid; A4IFJ5; -.
DR OMA; KFFMGKV; -.
DR OrthoDB; 302848at2759; -.
DR TreeFam; TF325228; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA00662; -.
DR UniPathway; UPA00878; -.
DR UniPathway; UPA00940; -.
DR PRO; PR:A4IFJ5; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000013298; Expressed in lung and 100 other tissues.
DR ExpressionAtlas; A4IFJ5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:1902387; F:ceramide 1-phosphate binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
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:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0034478; P:phosphatidylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0010572; P:positive regulation of platelet activation; IEA:Ensembl.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR CDD; cd04036; C2_cPLA2; 1.
DR Gene3D; 2.60.40.150; -; 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 Pfam; PF00168; C2; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52151; SSF52151; 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..749
FT /note="Cytosolic phospholipase A2"
FT /id="PRO_0000345133"
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:0000250"
FT REGION 426..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..457
FT /note="Basic and acidic residues"
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:0000250|UniProtKB:P50393"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT MOD_RES 505
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50393"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47712"
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 581
FT /note="S -> G (in Ref. 1; AAR17479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 85350 MW; C44BF7E4C40959BF CRC64;
MSFIDPYQHI IVEHHYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI SSTPDSRKRT
RHFNNDINPV WNETFEFILD PNQENILEIT LMDANYVMDE TLGTTTFPIS SMKVGEKKQV
PFIFNQVTEM ILEMSLEVCS SPDLRFSMAL CDQEKAFRQQ RKENIKENMK KLLGPKNSEG
LHSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH
PDFPEKGPEE INKELMKNVS HNPLLLLTPQ KIKRYVESLW RKKSSGQPVT FTDIFGMLIG
ETLIHNRMNT TLSSLKEKVN TGQCPLPLFT CLHVKPDVSE LMFADWVEFS PFEIGMAKYG
TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QSKGSTMEEE
LENITAKHIV SNDSSDSDDE SQGPKGTEHE EAEREYQNDN QASWVQRMLM ALVSDSALFN
TREGRAGKVH NFMLGLNLNT SYPMSPLRDF TMQESLDEDE LDAAVADPDE FEQIYEPLDV
KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN
KLPFPKIDPY VFDREGLKEC YVFKPKNPDV EKDCPTIIHF VLANINFRKY KAPGVPRETN
EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMYFN TLNNIDVIKN AIVESIEYRR
QNPSRCSVSL SSVEARRFFN KEFLSKPTA
