PA24A_RABIT
ID PA24A_RABIT Reviewed; 748 AA.
AC Q9TT38;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Heart;
RA Al-Khalili O.K., Eaton D.C.;
RT "Molecular cloning of cDNA coding for phospholipase A2.";
RL Submitted (NOV-1999) 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 -!- 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-726 in response to
CC mitogenic stimuli. {ECO:0000250|UniProtKB:P47712}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF204923; AAF15299.1; -; mRNA.
DR RefSeq; NP_001075541.1; NM_001082072.1.
DR AlphaFoldDB; Q9TT38; -.
DR SMR; Q9TT38; -.
DR STRING; 9986.ENSOCUP00000012590; -.
DR GeneID; 100008748; -.
DR KEGG; ocu:100008748; -.
DR CTD; 5321; -.
DR eggNOG; KOG1012; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR InParanoid; Q9TT38; -.
DR OrthoDB; 302848at2759; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA00662; -.
DR UniPathway; UPA00878; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0034478; P:phosphatidylglycerol catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript 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..748
FT /note="Cytosolic phospholipase A2"
FT /id="PRO_0000345135"
FT DOMAIN 6..122
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 138..739
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 1..178
FT /note="Phospholipid binding"
FT /evidence="ECO:0000250"
FT REGION 428..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 228
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 548
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 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50393"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT CROSSLNK 540
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT CROSSLNK 605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P47712"
SQ SEQUENCE 748 AA; 85235 MW; 7661A3EFC41FF668 CRC64;
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI ATTPDSRKRT
RHFNNDINPV WNEAFEFILD PNQGNVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV
PFIFNQVTEM ILEMSLEVCS SPDLRFSMAL CDQEKAFRQQ RKENIKENMR KLLGPKKSEG
LYSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH
PDFPEKGPQE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
ETLIHNRMHT TLSSLKEKVS SAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS HNKGSTMEEE
LENITAKHIV SNDSSDSDDE SQEPKGTEGE DAEREYQNDH QASWVHRMLM ALVSDSALFN
TREGRAGKVH NFMLGLNLNT SYPLSPLRDF TQESFDDDEL DAAVADPDEF ERIYEPLDVK
SKKIHVVDSG LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK
LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPIIIHFV LANINFRKYK SPGVPRETKE
EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT LNNIDVIKDA MVESIEYRRQ
NPSRCSVSLS NVEARRFFNK EFLSKPTA
