GenomeNet

Database: UniProt
Entry: A0A096MUP7_PAPAN
LinkDB: A0A096MUP7_PAPAN
Original site: A0A096MUP7_PAPAN 
ID   A0A096MUP7_PAPAN        Unreviewed;       754 AA.
AC   A0A096MUP7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU362102};
DE            EC=3.1.1.4 {ECO:0000256|RuleBase:RU362102};
GN   Name=PLA2G4A {ECO:0000313|Ensembl:ENSPANP00000003563.3};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000003563.3, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000003563.3, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000003563.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036248};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41076;
CC         Evidence={ECO:0000256|ARBA:ARBA00036248};
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:0000256|ARBA:ARBA00036487};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41124;
CC         Evidence={ECO:0000256|ARBA:ARBA00036487};
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:0000256|ARBA:ARBA00036365};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272;
CC         Evidence={ECO:0000256|ARBA:ARBA00036365};
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:0000256|ARBA:ARBA00035962};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41072;
CC         Evidence={ECO:0000256|ARBA:ARBA00035962};
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:0000256|ARBA:ARBA00036736};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC         Evidence={ECO:0000256|ARBA:ARBA00036736};
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:0000256|ARBA:ARBA00023922};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000256|ARBA:ARBA00023922};
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:0000256|ARBA:ARBA00023408};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000256|ARBA:ARBA00023408};
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:0000256|ARBA:ARBA00000597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000256|ARBA:ARBA00000597};
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:0000256|ARBA:ARBA00036986};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40452;
CC         Evidence={ECO:0000256|ARBA:ARBA00036986};
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:0000256|ARBA:ARBA00036574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520;
CC         Evidence={ECO:0000256|ARBA:ARBA00036574};
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:0000256|ARBA:ARBA00035999};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41100;
CC         Evidence={ECO:0000256|ARBA:ARBA00035999};
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:0000256|ARBA:ARBA00036797};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41308;
CC         Evidence={ECO:0000256|ARBA:ARBA00036797};
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:0000256|ARBA:ARBA00036898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41088;
CC         Evidence={ECO:0000256|ARBA:ARBA00036898};
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:0000256|ARBA:ARBA00036679};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53693;
CC         Evidence={ECO:0000256|ARBA:ARBA00036679};
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:0000256|ARBA:ARBA00036609};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53705;
CC         Evidence={ECO:0000256|ARBA:ARBA00036609};
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:0000256|ARBA:ARBA00036785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53689;
CC         Evidence={ECO:0000256|ARBA:ARBA00036785};
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:0000256|ARBA:ARBA00035771};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53697;
CC         Evidence={ECO:0000256|ARBA:ARBA00035771};
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:0000256|ARBA:ARBA00036533};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53701;
CC         Evidence={ECO:0000256|ARBA:ARBA00036533};
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:0000256|ARBA:ARBA00023422};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000256|ARBA:ARBA00023422};
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:0000256|ARBA:ARBA00000150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000256|ARBA:ARBA00000150};
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000256|ARBA:ARBA00037916}.
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004716}.
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004702}.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00037925}.
CC   -!- SUBUNIT: Interacts with KAT5. {ECO:0000256|ARBA:ARBA00038814}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. {ECO:0000256|RuleBase:RU362102}.
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DR   AlphaFoldDB; A0A096MUP7; -.
DR   STRING; 9555.ENSPANP00000003563; -.
DR   Ensembl; ENSPANT00000012118.3; ENSPANP00000003563.3; ENSPANG00000021907.3.
DR   eggNOG; KOG1012; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   GeneTree; ENSGT01030000234606; -.
DR   HOGENOM; CLU_011663_1_1_1; -.
DR   OMA; NFMRGLS; -.
DR   OrthoDB; 4250045at2759; -.
DR   Proteomes; UP000028761; Chromosome 1.
DR   Bgee; ENSPANG00000021907; Expressed in cornea and 63 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IEA:Ensembl.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:Ensembl.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
DR   GO; GO:1902387; F:ceramide 1-phosphate binding; IEA:Ensembl.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:Ensembl.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:Ensembl.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Ensembl.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR   GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:Ensembl.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR   GO; GO:0034478; P:phosphatidylglycerol catabolic process; IEA:Ensembl.
DR   GO; GO:0006663; P:platelet activating factor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR   GO; GO:0010572; P:positive regulation of platelet activation; IEA:Ensembl.
DR   GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
DR   GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
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   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU362102};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362102};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362102};
KW   Phospholipid degradation {ECO:0000256|ARBA:ARBA00022668};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW   Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761}.
FT   DOMAIN          6..122
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          140..754
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          426..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  86055 MW;  10A26C31F115154F CRC64;
     MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI STTPDSRKRT
     RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV
     PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKENIRESMK KLLGPKNSEG
     LNSARDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH
     PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
     ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
     TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QSRGCTMEEE
     LENITTKHIV SNDSSDSDDE SQEPKGTENE DAGRDYQSDN QASWIHRMIM AFMSDSALFN
     TREGRAGKVH NFMLGLNLNT SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV
     KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN
     KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EQDCPTIIHF VLANINFRKY KAPEESLDSC
     VSWKMLINQR RSKDLHAECL RLQKPYFGTR KCVFHFMNGK TQKIGRVFQG KLRKRKKSLT
     LIFLMTRNHH FQPSIFNIQI KHSKDYMILC TSIL
//
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