ID F7CBU9_MONDO Unreviewed; 713 AA.
AC F7CBU9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 64.
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:ENSMODP00000014773.2};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000014773.2, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000014773.2, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000014773.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; F7CBU9; -.
DR STRING; 13616.ENSMODP00000014773; -.
DR Ensembl; ENSMODT00000015045.3; ENSMODP00000014773.2; ENSMODG00000011791.4.
DR eggNOG; KOG1012; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_1_1_1; -.
DR InParanoid; F7CBU9; -.
DR OMA; YSLPRMK; -.
DR TreeFam; TF325228; -.
DR Proteomes; UP000002280; Chromosome 2.
DR Bgee; ENSMODG00000011791; Expressed in uterine wall and 17 other cell types or tissues.
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; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
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: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; 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; 2.
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:ARBA00023160};
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:UP000002280}.
FT DOMAIN 6..122
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 134..704
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 713 AA; 81110 MW; 9B18BCED645BB218 CRC64;
MSCIDPYQHI IVEHQYSHKF TVNVLRATKV TKGAFGDMLD TPDPYVELFI SSTPDSRKRT
RHFNNDVNPV WNETFEFILD PNQENILEIT LMDANYVMDE TLGTATFPIS SMKVGEKKEV
PFIFNEVFMS LSVLHTSSSP DLRFSMALCD QEKIFRQQRK ENIKESMKKL LGPKKSEGLC
SARDVPVIAV LGSGGGFRAM VGFSGVMKAL YESGILDCAT YVAGLSGSTW YMSSLYSHPD
FPEKGPKEIN EELMASVSHN PLLLLTPQKV KRYIESLWKK KSSGQPVTFT DIFGMLIGET
LINNRMSSTL SSLKEKVNEA QCPLPLFTCL HVKPDVSELM FADWVEFSPY EIGMAKYGTF
MAPDLFGSKF FMGTVVKKYE ENPLHFLMGV WGSAFSILFN RGSTMEEELG TENADAEKEY
QNNNQASWVQ RMLMALVSDS TLFNTREGRA GKVHNFMLGL NLNTSYPLSP LRGISTQDSM
EEDELDAAVA DPDEFERIYE PLDVKSKKIH VVDSGLTFNL PYPLILRPQR GVDLIISFDF
SARPSDSSPP FKEILLAEKW AKMNKLPFPK IDPYVFDREG LKECYVFKPK NPDVEKDCPT
IIHFVLANIN FRDYKAPGIP RETQEEKDFA DFDIFDDPES PFSTFNFQYP NQAFKRLHDL
MHFNTMNNID VIKNAIFESI EYRRQNPSRC SVSLSNIEAR RFFNKDSLSK PSA
//
