PA24E_HUMAN
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 03-AUG-2022, entry version 130.
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-(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;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC 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}.
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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; 30.
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 PeptideAtlas; Q3MJ16; -.
DR PRIDE; Q3MJ16; -.
DR ProteomicsDB; 61802; -. [Q3MJ16-2]
DR ProteomicsDB; 6312; -.
DR Antibodypedia; 42114; 81 antibodies from 22 providers.
DR DNASU; 123745; -.
DR Ensembl; ENST00000399518.3; ENSP00000382434.3; ENSG00000188089.13. [Q3MJ16-3]
DR GeneID; 123745; -.
DR KEGG; hsa:123745; -.
DR UCSC; uc021sjp.2; human.
DR CTD; 123745; -.
DR DisGeNET; 123745; -.
DR GeneCards; PLA2G4E; -.
DR HGNC; HGNC:24791; PLA2G4E.
DR HPA; ENSG00000188089; Tissue enriched (skin).
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; YELHMKS; -.
DR OrthoDB; 302848at2759; -.
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 1067 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 45 other 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:0004623; F:phospholipase A2 activity; IBA:GO_Central.
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 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..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
