ID PA24E_HUMAN Reviewed; 868 AA. AC Q3MJ16; B7WPN2; Q6ZSC0; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 4. DT 27-MAR-2024, entry version 139. 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:0000250|UniProtKB:Q50L42}; DE AltName: Full=Calcium-dependent N-acyltransferase {ECO:0000303|PubMed:29447909}; DE AltName: Full=Phospholipase A2 group IVE; GN Name=PLA2G4E {ECO:0000312|HGNC:HGNC:24791}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-868. RC TISSUE=Heart, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. 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, BIOPHYSICOCHEMICAL PROPERTIES, AND RP ACTIVITY REGULATION. 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). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION, AND MUTAGENESIS RP OF SER-412. RX PubMed=30517655; DOI=10.1093/jb/mvy104; RA Binte Mustafiz S.S., Uyama T., Hussain Z., Kawai K., Tsuboi K., Araki N., RA Ueda N.; RT "The role of intracellular anionic phospholipids in the production of N- RT acyl-phosphatidylethanolamines by cytosolic phospholipase A2 epsilon."; RL J. Biochem. 165:343-352(2019). CC -!- FUNCTION: Calcium-dependent N-acyltransferase involved in the CC biosynthesis of N-acyl ethanolamines (NAEs) in the brain CC (PubMed:29447909). 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:29447909, CC PubMed:30517655). Has weak phospholipase A2 and lysophospholipase CC activities (By similarity). Regulates intracellular membrane CC trafficking that requires modulation of membrane curvature as it occurs CC by enrichment in lysophospholipids. Promotes tubule formation involved CC in clathrin-independent endocytotic trafficking and cargo recycling (By CC similarity). {ECO:0000250|UniProtKB:Q50L42, CC ECO:0000269|PubMed:29447909, ECO:0000269|PubMed:30517655}. 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:29447909, ECO:0000269|PubMed:30517655}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45189; CC Evidence={ECO:0000305|PubMed:29447909, ECO:0000305|PubMed:30517655}; 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:0000250|UniProtKB:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55253; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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:0000250|UniProtKB:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55249; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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:29447909, ECO:0000269|PubMed:30517655}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45173; CC Evidence={ECO:0000305|PubMed:29447909, ECO:0000305|PubMed:30517655}; 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:0000250|UniProtKB:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55257; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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:0000250|UniProtKB:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55261; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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-O-(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:0000250|UniProtKB:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63593; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; 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:Q50L42}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; CC Evidence={ECO:0000250|UniProtKB:Q50L42}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041, ECO:0000269|PubMed:29447909}; CC -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+). Stimulated by CC anionic phospholipids such as phosphatidylserines, phosphatidates and CC phosphatidylinositols. {ECO:0000269|PubMed:29447909, CC ECO:0000269|PubMed:30517655}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:29447909}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q50L42}. Early endosome membrane CC {ECO:0000250|UniProtKB:Q50L42}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q50L42}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q50L42}. Lysosome membrane CC {ECO:0000250|UniProtKB:Q50L42}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q50L42}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q50L42}. Cell membrane CC {ECO:0000250|UniProtKB:Q50L42}; Peripheral membrane protein; CC Cytoplasmic side {ECO:0000250|UniProtKB:Q50L42}. Note=Targeted to CC clathrin-independent endocytotic vesicles through binding to CC phosphoinositides, especially phosphatidylinositol 4,5-bisphosphates. CC {ECO:0000250|UniProtKB:Q50L42}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3MJ16-3; Sequence=Displayed; CC Name=2; CC IsoId=Q3MJ16-2; Sequence=VSP_019883; 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}. 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; AK127558; BAC87034.1; -; mRNA. DR EMBL; AC039056; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC101584; AAI01585.2; -; mRNA. DR EMBL; BC101612; AAI01613.2; -; mRNA. DR CCDS; CCDS55962.1; -. [Q3MJ16-3] DR RefSeq; NP_001193599.1; NM_001206670.1. [Q3MJ16-3] DR RefSeq; XP_011519540.1; XM_011521238.1. [Q3MJ16-2] DR AlphaFoldDB; Q3MJ16; -. DR SMR; Q3MJ16; -. DR BioGRID; 125832; 32. DR IntAct; Q3MJ16; 3. DR STRING; 9606.ENSP00000382434; -. DR ChEMBL; CHEMBL3831242; -. DR PhosphoSitePlus; Q3MJ16; -. DR BioMuta; PLA2G4E; -. DR DMDM; 325511387; -. DR EPD; Q3MJ16; -. DR jPOST; Q3MJ16; -. DR MassIVE; Q3MJ16; -. DR PaxDb; 9606-ENSP00000382434; -. DR PeptideAtlas; Q3MJ16; -. DR ProteomicsDB; 61802; -. [Q3MJ16-2] DR ProteomicsDB; 6312; -. DR Antibodypedia; 42114; 102 antibodies from 22 providers. DR DNASU; 123745; -. DR Ensembl; ENST00000399518.3; ENSP00000382434.3; ENSG00000188089.14. [Q3MJ16-3] DR GeneID; 123745; -. DR KEGG; hsa:123745; -. DR UCSC; uc021sjp.2; human. DR AGR; HGNC:24791; -. DR CTD; 123745; -. DR DisGeNET; 123745; -. DR GeneCards; PLA2G4E; -. DR HGNC; HGNC:24791; PLA2G4E. DR HPA; ENSG00000188089; Tissue enriched (skin). DR MIM; 620649; gene. DR neXtProt; NX_Q3MJ16; -. DR OpenTargets; ENSG00000188089; -. DR VEuPathDB; HostDB:ENSG00000188089; -. DR eggNOG; KOG1028; Eukaryota. DR eggNOG; KOG1325; Eukaryota. DR GeneTree; ENSGT01030000234606; -. DR InParanoid; Q3MJ16; -. DR OMA; SFENTQR; -. DR OrthoDB; 4250045at2759; -. DR PhylomeDB; Q3MJ16; -. DR TreeFam; TF325228; -. DR PathwayCommons; Q3MJ16; -. DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC. DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS. DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE. DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI. DR Reactome; R-HSA-1483115; Hydrolysis of LPC. DR SignaLink; Q3MJ16; -. DR BioGRID-ORCS; 123745; 19 hits in 1145 CRISPR screens. DR GenomeRNAi; 123745; -. DR Pharos; Q3MJ16; Tbio. DR PRO; PR:Q3MJ16; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q3MJ16; Protein. DR Bgee; ENSG00000188089; Expressed in skin of leg and 46 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate 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:0008970; F:phospholipase A1 activity; TAS:Reactome. 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:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome. DR GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:UniProtKB. DR CDD; cd04036; C2_cPLA2; 1. DR CDD; cd07201; cPLA2_Grp-IVB-IVD-IVE-IVF; 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; IPR040723; cPLA2_C2. DR InterPro; IPR002642; LysoPLipase_cat_dom. DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1. DR PANTHER; PTHR10728:SF24; CYTOSOLIC PHOSPHOLIPASE A2 EPSILON; 1. 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; 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 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..868 FT /note="Cytosolic phospholipase A2 epsilon" FT /id="PRO_0000247025" FT DOMAIN 46..170 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 324..856 FT /note="PLA2c" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 857..868 FT /note="Required for localization at membrane structures" FT /evidence="ECO:0000269|PubMed:30517655" FT ACT_SITE 412 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 700 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 84 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 140 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 140 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 142 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 142 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 148 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT MOD_RES 800 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q50L42" FT VAR_SEQ 1..376 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_019883" FT VARIANT 400 FT /note="N -> S (in dbSNP:rs4924595)" FT /id="VAR_027052" FT VARIANT 693 FT /note="A -> T (in dbSNP:rs8030775)" FT /id="VAR_027053" FT MUTAGEN 412 FT /note="S->A: Impairs localization at membrane structures FT and N-acyl transferase activity." FT /evidence="ECO:0000269|PubMed:30517655" FT CONFLICT 389 FT /note="M -> V (in Ref. 1; BAC87034)" FT /evidence="ECO:0000305" FT CONFLICT 502 FT /note="A -> P (in Ref. 1; BAC87034)" FT /evidence="ECO:0000305" FT CONFLICT 690 FT /note="T -> A (in Ref. 1; BAC87034)" FT /evidence="ECO:0000305" FT CONFLICT 765 FT /note="C -> Y (in Ref. 1; BAC87034)" FT /evidence="ECO:0000305" SQ SEQUENCE 868 AA; 99190 MW; F9A6F33880A5409F CRC64; MSLQASEGCP GLGTNVFVPQ SPQTDEEGSR SGRSFSEFED TQDLDTPGLP PFCPMAPWGS EEGLSPCHLL TVRVIRMKNV RQADMLSQTD CFVSLWLPTA SQKKLRTRTI SNCPNPEWNE SFNFQIQSRV KNVLELSVCD EDTVTPDDHL LTVLYDLTKL CFRKKTHVKF PLNPQGMEEL EVEFLLEESP SPPETLVTNG VLVSRQVSCL EVHAQSRRRR KREKMKDLLV MVNESFENTQ RVRPCLEPCC PTSACFQTAA CFHYPKYFQS QVHVEVPKSH WSCGLCCRSR KKGPISQPLD CLSDGQVMTL PVGESYELHM KSTPCPETLD VRLGFSLCPA ELEFLQKRKV VVAKALKQVL QLEEDLQEDE VPLIAIMATG GGTRSMTSMY GHLLGLQKLN LLDCASYITG LSGATWTMAT LYRDPDWSSK NLEPAIFEAR RHVVKDKLPS LFPDQLRKFQ EELRQRSQEG YRVTFTDFWG LLIETCLGDE RNECKLSDQR AALSCGQNPL PIYLTINVKD DVSNQDFREW FEFSPYEVGL QKYGAFIPSE LFGSEFFMGR LVKRIPESRI CYMLGLWSSI FSLNLLDAWN LSHTSEEFFH RWTREKVQDI EDEPILPEIP KCDANILETT VVIPGSWLSN SFREILTHRS FVSEFHNFLS GLQLHTNYLQ NGQFSRWKDT VLDGFPNQLT ESANHLCLLD TAFFVNSSYP PLLRPERKAD LIIHLNYCAG SQTKPLKQTC EYCTVQNIPF PKYELPDENE NLKECYLMEN PQEPDAPIVT FFPLINDTFR KYKAPGVERS PEELEQGQVD IYGPKTPYAT KELTYTEATF DKLVKLSEYN ILNNKDTLLQ ALRLAVEKKK RLKGQCPS //