PA24E_MOUSE
ID PA24E_MOUSE Reviewed; 875 AA.
AC Q50L42; Q8BX44;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytosolic phospholipase A2 epsilon {ECO:0000303|PubMed:24413173};
DE Short=cPLA2-epsilon {ECO:0000303|PubMed:24413173};
DE EC=3.1.1.4 {ECO:0000269|PubMed:15866882};
DE AltName: Full=Calcium-dependent N-acyltransferase {ECO:0000303|PubMed:29447909};
DE AltName: Full=Phospholipase A2 group IVE;
GN Name=Pla2g4e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15866882; DOI=10.1074/jbc.m413711200;
RA Ohto T., Uozumi N., Hirabayashi T., Shimizu T.;
RT "Identification of novel cytosolic phospholipase A(2)s, murine
RT cPLA(2)delta, epsilon, and zeta, which form a gene cluster with
RT cPLA(2)beta.";
RL J. Biol. Chem. 280:24576-24583(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, REGION, AND MUTAGENESIS OF SER-420.
RX PubMed=24413173; DOI=10.1242/jcs.136598;
RA Capestrano M., Mariggio S., Perinetti G., Egorova A.V., Iacobacci S.,
RA Santoro M., Di Pentima A., Iurisci C., Egorov M.V., Di Tullio G.,
RA Buccione R., Luini A., Polishchuk R.S.;
RT "Cytosolic phospholipase A(2)epsilon drives recycling through the clathrin-
RT independent endocytic route.";
RL J. Cell Sci. 127:977-993(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF SER-420.
RX PubMed=27399000; DOI=10.1038/nchembio.2127;
RA Ogura Y., Parsons W.H., Kamat S.S., Cravatt B.F.;
RT "A calcium-dependent acyltransferase that produces N-acyl
RT phosphatidylethanolamines.";
RL Nat. Chem. Biol. 12:669-671(2016).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=29447909; DOI=10.1016/j.bbalip.2018.02.002;
RA Hussain Z., Uyama T., Kawai K., Binte Mustafiz S.S., Tsuboi K., Araki N.,
RA Ueda N.;
RT "Phosphatidylserine-stimulated production of N-acyl-
RT phosphatidylethanolamines by Ca2+-dependent N-acyltransferase.";
RL Biochim. Biophys. Acta 1863:493-502(2018).
CC -!- FUNCTION: Calcium-dependent N-acyltransferase involved in the
CC biosynthesis of N-acyl ethanolamines (NAEs) in the brain
CC (PubMed:27399000). Transfers the sn-1 fatty acyl chain of
CC phosphatidylcholine (fatty acyl donor) to the amine group of
CC phosphatidylethanolamine (fatty acyl acceptor) to generate N-acyl
CC phosphatidylethanolamine (NAPE). Similarly can use
CC plasmenylethanolamine as a fatty acyl acceptor to form N-acyl
CC plasmenylethanolamine (N-Acyl-PlsEt). Both NAPE and N-Acyl-PlsEt can
CC serve as precursors of bioactive NAEs like N-arachidonoyl
CC phosphatidylethanolamine also called anandamide (PubMed:27399000,
CC PubMed:29447909). Has weak phospholipase A2 and lysophospholipase
CC activities (PubMed:27399000, PubMed:15866882). Regulates intracellular
CC membrane trafficking that requires modulation of membrane curvature as
CC it occurs by enrichment in lysophospholipids. Promotes tubule formation
CC involved in clathrin-independent endocytotic trafficking and cargo
CC recycling (PubMed:24413173). {ECO:0000269|PubMed:15866882,
CC ECO:0000269|PubMed:24413173, ECO:0000269|PubMed:27399000,
CC ECO:0000269|PubMed:29447909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine = a 2-acyl-sn-glycero-3-phosphocholine
CC + H(+) + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45188, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:57875, ChEBI:CHEBI:62537, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:27399000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45189;
CC Evidence={ECO:0000305|PubMed:27399000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1-
CC hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine = 2-
CC octadecanoyl-sn-glycero-3-phosphocholine + H(+) + N-hexadecanoyl-1,2-
CC di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:55252, ChEBI:CHEBI:15378, ChEBI:CHEBI:73000,
CC ChEBI:CHEBI:74986, ChEBI:CHEBI:76076, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000269|PubMed:27399000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55253;
CC Evidence={ECO:0000305|PubMed:27399000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1-
CC octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine = 2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + N-octadecanoyl-1,2-
CC di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:55248, ChEBI:CHEBI:15378, ChEBI:CHEBI:74986,
CC ChEBI:CHEBI:75026, ChEBI:CHEBI:76078, ChEBI:CHEBI:85292;
CC Evidence={ECO:0000269|PubMed:27399000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55249;
CC Evidence={ECO:0000305|PubMed:27399000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = 2-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+) + N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45172,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:74986,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000269|PubMed:27399000, ECO:0000269|PubMed:29447909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45173;
CC Evidence={ECO:0000305|PubMed:27399000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphocholine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phosphocholine + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:55256, ChEBI:CHEBI:15378, ChEBI:CHEBI:60657,
CC ChEBI:CHEBI:74986, ChEBI:CHEBI:76079, ChEBI:CHEBI:85277;
CC Evidence={ECO:0000269|PubMed:27399000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55257;
CC Evidence={ECO:0000305|PubMed:27399000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine =
CC 2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H(+) + N,1,2-
CC tri-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:55260, ChEBI:CHEBI:15378, ChEBI:CHEBI:74986,
CC ChEBI:CHEBI:76088, ChEBI:CHEBI:85291;
CC Evidence={ECO:0000269|PubMed:27399000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55261;
CC Evidence={ECO:0000305|PubMed:27399000};
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:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 1-(1Z-
CC octadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine =
CC 1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-
CC hexadecanoyl-ethanolamine + 2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:63592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:76078, ChEBI:CHEBI:78340,
CC ChEBI:CHEBI:138663; Evidence={ECO:0000269|PubMed:29447909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63593;
CC Evidence={ECO:0000305|PubMed:29447909};
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:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:15866882};
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:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:27399000, ECO:0000269|PubMed:29447909};
CC -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+) (PubMed:27399000,
CC PubMed:29447909). Stimulated by anionic phospholipids such as
CC phosphatidylserine (PubMed:29447909). {ECO:0000269|PubMed:27399000,
CC ECO:0000269|PubMed:29447909}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:29447909};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}.
CC Early endosome membrane {ECO:0000269|PubMed:24413173,
CC ECO:0000269|PubMed:29447909}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305|PubMed:24413173}. Lysosome
CC membrane {ECO:0000269|PubMed:15866882, ECO:0000269|PubMed:24413173,
CC ECO:0000269|PubMed:29447909}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305|PubMed:24413173}. Cell
CC membrane {ECO:0000269|PubMed:24413173, ECO:0000269|PubMed:29447909};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305|PubMed:24413173}. Note=Targeted to clathrin-independent
CC endocytotic vesicles through binding to phosphoinositides, especially
CC phosphatidylinositol 4,5-bisphosphates. {ECO:0000269|PubMed:24413173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q50L42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q50L42-2; Sequence=VSP_019884, VSP_019885, VSP_019886;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain, heart, skeletal
CC muscle, testis and thyroid (PubMed:15866882, PubMed:27399000).
CC Expressed in neurons but not astrocytes or microglia (PubMed:27399000).
CC Expressed at lower level in stomach (PubMed:15866882).
CC {ECO:0000269|PubMed:15866882, ECO:0000269|PubMed:27399000}.
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 Ca(2+) (By
CC similarity). {ECO:0000250}.
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DR EMBL; AB195277; BAD98153.1; -; mRNA.
DR EMBL; AK049063; BAC33531.1; -; mRNA.
DR CCDS; CCDS16616.1; -. [Q50L42-1]
DR RefSeq; NP_808513.2; NM_177845.4. [Q50L42-1]
DR AlphaFoldDB; Q50L42; -.
DR SMR; Q50L42; -.
DR STRING; 10090.ENSMUSP00000087525; -.
DR SwissLipids; SLP:000001822; -.
DR iPTMnet; Q50L42; -.
DR PhosphoSitePlus; Q50L42; -.
DR SwissPalm; Q50L42; -.
DR PaxDb; Q50L42; -.
DR PRIDE; Q50L42; -.
DR ProteomicsDB; 294371; -. [Q50L42-1]
DR ProteomicsDB; 294372; -. [Q50L42-2]
DR Antibodypedia; 42114; 81 antibodies from 22 providers.
DR DNASU; 329502; -.
DR Ensembl; ENSMUST00000090071; ENSMUSP00000087525; ENSMUSG00000050211. [Q50L42-1]
DR GeneID; 329502; -.
DR KEGG; mmu:329502; -.
DR UCSC; uc008lve.1; mouse. [Q50L42-1]
DR UCSC; uc008lvg.1; mouse. [Q50L42-2]
DR CTD; 123745; -.
DR MGI; MGI:1919144; Pla2g4e.
DR VEuPathDB; HostDB:ENSMUSG00000050211; -.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_0_0_1; -.
DR InParanoid; Q50L42; -.
DR OMA; YELHMKS; -.
DR OrthoDB; 302848at2759; -.
DR PhylomeDB; Q50L42; -.
DR TreeFam; TF325228; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR BioGRID-ORCS; 329502; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Pla2g4e; mouse.
DR PRO; PR:Q50L42; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q50L42; protein.
DR Bgee; ENSMUSG00000050211; Expressed in lip and 135 other tissues.
DR Genevisible; Q50L42; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA:UniProtKB.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IMP: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; IPR040723; cPLA2_C2.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF18695; cPLA2_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 Alternative splicing; Calcium; Cell membrane; Cytoplasm; Endosome;
KW Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..875
FT /note="Cytosolic phospholipase A2 epsilon"
FT /id="PRO_0000247026"
FT DOMAIN 60..183
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 332..875
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 16..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..875
FT /note="Required for localization at membrane structures"
FT /evidence="ECO:0000269|PubMed:24413173"
FT COMPBIAS 51..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 708
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019884"
FT VAR_SEQ 584..599
FT /note="LWSSIFSLNLLDAWNL -> DSLRYSAPERARPAFD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019885"
FT VAR_SEQ 600..875
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019886"
FT MUTAGEN 420
FT /note="S->A: Impairs calcium-dependent biosynthesis of
FT NAPEs and NAEs. Reduces tubule growth and cargo transport
FT from clathrin-independent endosomes."
FT /evidence="ECO:0000269|PubMed:24413173,
FT ECO:0000269|PubMed:27399000"
FT CONFLICT 513
FT /note="R -> K (in Ref. 2; BAC33531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 875 AA; 100157 MW; 74A628C1E1A2CDEA CRC64;
MQSIPHSDEA DVAGMTHASE GHHGLGTSML VPKNPQGEED SKLGRNCSGF EDAQDPQTAV
PSSPLLSMAS CSSQEGSSPC HLLTVRIIGM KNVRQADILS QTDCFVTLWL PTASQKKLKT
RTISNCLHPE WDESFTFQIQ TQVKNVLELS VCDEDTLTQN DHLLTVLYDL SKLCLRNKTH
VKFPLNPEGM EELEVEFLLE ENFSSSETLI TNGVLVSRQV SCLEVHAESR RPRKRKKNKD
LLVMVTDSFE NTQRVPPCQE PCYPNSACFH YPKYSQPQLY AEAPKSHCNF RLCCCGTHRN
DPVCQPLNCL SDGQVTTLPV GENYELHMKS SPCSDTLDVR LGFSLCQEEV EFVQKRKMVV
AKTLSQMLQL EEGLHEDEVP IIAIMATGGG TRSMVSLYGH LLGLQKLNFL DASTYITGLS
GATWTMATLY SDPEWSSKNL ETVVFEARRH VVKDKMPALF PDQLYKWRED LQKHSQEGYK
TTFTDFWGKL IEYSLGDKKN ECKLSDQRAA LCRGQNPLPI YLTINVKDDV SNQDFREWFE
FSPYEVGMQK YGAFIPSELF GSEFFMGRLM KRIPEPEMCY MLGLWSSIFS LNLLDAWNLS
HTSEEFFYRW TRERLHDIED DPILPEIPRC DDNPLETTVV IPTTWLSNTF REILTRRPFV
SEFHNFLYGM QLHTDYLQNR QFSMWKDTVL DTFPNQLTQF AKHLNLLDTA FFVNSSYAPL
LRPERKVDLI IHLNYCAGSQ TKPLKQTCEY CTEQKIPFPS FSILEDDNSL KECYVMENPQ
EPDAPIVAYF PLISDTFQKY KAPGVERSPD ELELGQLNIY GPKSPYATKE LTYTEAAFDK
LVKLSEYNIL NNRDKLIQAL RLAMEKKRMR SQCPS
