PA2GE_HUMAN
ID PA2GE_HUMAN Reviewed; 142 AA.
AC Q9NZK7; Q5VXJ8;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Group IIE secretory phospholipase A2;
DE Short=GIIE sPLA2;
DE Short=sPLA2-IIE;
DE EC=3.1.1.4 {ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:28883454};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2E;
DE Flags: Precursor;
GN Name=PLA2G2E;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10681567; DOI=10.1074/jbc.275.8.5785;
RA Suzuki N., Ishizaki J., Yokota Y., Higashino K., Ono T., Ikeda M.,
RA Fujii N., Kawamoto K., Hanasaki K.;
RT "Structures, enzymatic properties, and expression of novel human and mouse
RT secretory phospholipase A(2)s.";
RL J. Biol. Chem. 275:5785-5793(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION BY IL1B.
RX PubMed=11922621; DOI=10.1006/bbrc.2002.6716;
RA Murakami M., Yoshihara K., Shimbara S., Lambeau G., Singer A., Gelb M.H.,
RA Sawada M., Inagaki N., Nagai H., Kudo I.;
RT "Arachidonate release and eicosanoid generation by group IIE phospholipase
RT A(2).";
RL Biochem. Biophys. Res. Commun. 292:689-696(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 20-142 IN COMPLEX WITH INDOLE
RP ANALOGS, COFACTOR, DISULFIDE BOND, FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ASN-40; ASP-41; HIS-65; ASP-66 AND ASN-132.
RX PubMed=28883454; DOI=10.1038/s41598-017-11219-8;
RA Hou S., Xu T., Xu J., Qu L., Xu Y., Chen L., Liu J.;
RT "Structural basis for functional selectivity and ligand recognition
RT revealed by crystal structures of human secreted phospholipase A2 group
RT IIE.";
RL Sci. Rep. 7:10815-10815(2017).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids (PubMed:10681567, PubMed:11922621,
CC PubMed:28883454). Hydrolyzes the ester bond of the fatty acyl group
CC attached at sn-2 position of phospholipids (phospholipase A2 activity),
CC releasing various unsaturated fatty acids including oleoate,
CC linoleoate, arachidonate, docosahexaenoate and
CC lysophosphatidylethanolamines in preference to lysophosphatidylcholines
CC (PubMed:10681567, PubMed:28883454). In response to high-fat diet,
CC hydrolyzes minor lipoprotein phospholipids including
CC phosphatidylserines, phosphatidylinositols and phosphatidylglycerols,
CC altering lipoprotein composition and fat storage in adipose tissue and
CC liver (By similarity). May act in an autocrine and paracrine manner
CC (PubMed:11922621). Contributes to lipid remodeling of cellular
CC membranes and generation of lipid mediators involved in pathogen
CC clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and
CC phosphatidylethanolamines, which are major components of membrane
CC phospholipids in bacteria (PubMed:11922621). Acts as a hair follicle
CC phospholipase A2. Selectively releases lysophosphatidylethanolamines
CC (LPE) and various unsaturated fatty acids in skin to regulate hair
CC follicle homeostasis (By similarity). May regulate the inflammatory
CC response by releasing arachidonate, a precursor of prostaglandins and
CC leukotrienes (PubMed:11922621). Upon allergen exposure, may participate
CC in allergic inflammatory response by enhancing leukotriene C4 synthesis
CC and degranulation in mast cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9QUL3, ECO:0000269|PubMed:10681567,
CC ECO:0000269|PubMed:11922621, ECO:0000269|PubMed:28883454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-
CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:11922621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O
CC = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC ChEBI:CHEBI:84475; Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000305|PubMed:10681567};
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:0000255|PROSITE-ProRule:PRU10035,
CC ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:28883454};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:10681567, ECO:0000305|PubMed:28883454};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:10681567};
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:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:41231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:77016;
CC Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:28883454};
CC Note=Binds 2 Ca(2+) ions per subunit. One ion binds at a conserved
CC binding site (GCXCG), whereas the second ion binds at a flexible site
CC and may act as a supplemental electrophile as well as a backup.
CC {ECO:0000269|PubMed:28883454};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:10681567};
CC -!- INTERACTION:
CC Q9NZK7; Q13021: MALL; NbExp=3; IntAct=EBI-13380620, EBI-750078;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10681567,
CC ECO:0000269|PubMed:11922621}. Cytoplasm {ECO:0000269|PubMed:11922621}.
CC Note=Through binding to heparan sulfate proteoglycan, may be localized
CC to cytoplasmic compartments enriched in anionic phospholipids.
CC {ECO:0000269|PubMed:11922621}.
CC -!- TISSUE SPECIFICITY: Restricted to the brain, heart, lung, and placenta.
CC {ECO:0000269|PubMed:10681567}.
CC -!- INDUCTION: Up-regulated by inflammatory cytokine IL1B.
CC {ECO:0000269|PubMed:11922621}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF189279; AAF36541.1; -; mRNA.
DR EMBL; AL358253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS200.1; -.
DR RefSeq; NP_055404.1; NM_014589.2.
DR PDB; 5WZM; X-ray; 2.00 A; A=22-142.
DR PDB; 5WZO; X-ray; 1.90 A; A=20-142.
DR PDB; 5WZS; X-ray; 2.30 A; A=20-142.
DR PDB; 5WZT; X-ray; 2.40 A; A=20-142.
DR PDB; 5WZU; X-ray; 2.20 A; A=20-142.
DR PDB; 5WZV; X-ray; 2.20 A; A=20-142.
DR PDB; 5WZW; X-ray; 1.95 A; A=20-142.
DR PDB; 5Y5E; X-ray; 1.80 A; A=20-142.
DR PDB; 6KQU; X-ray; 2.00 A; A=20-142.
DR PDBsum; 5WZM; -.
DR PDBsum; 5WZO; -.
DR PDBsum; 5WZS; -.
DR PDBsum; 5WZT; -.
DR PDBsum; 5WZU; -.
DR PDBsum; 5WZV; -.
DR PDBsum; 5WZW; -.
DR PDBsum; 5Y5E; -.
DR PDBsum; 6KQU; -.
DR AlphaFoldDB; Q9NZK7; -.
DR SMR; Q9NZK7; -.
DR BioGRID; 119038; 15.
DR IntAct; Q9NZK7; 1.
DR STRING; 9606.ENSP00000364257; -.
DR BindingDB; Q9NZK7; -.
DR ChEMBL; CHEMBL2154; -.
DR DrugBank; DB07958; (2-CARBAMOYLMETHYL-5-PROPYL-OCTAHYDRO-INDOL-7-YL)ACETIC ACID.
DR DrugBank; DB07500; (2E)-1-[2-hydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one.
DR DrugBank; DB06987; (R)-Atenolol.
DR DrugBank; DB01955; 1,4-Butanediol.
DR DrugBank; DB08447; 3-{3-[(DIMETHYLAMINO)METHYL]-1H-INDOL-7-YL}PROPAN-1-OL.
DR DrugBank; DB02636; 9-Hydroxy-8-Methoxy-6-Nitro-Phenanthrol[3,4-D][1,3]Dioxole-5-Carboxylic Acid.
DR DrugBank; DB00233; Aminosalicylic acid.
DR DrugBank; DB09462; Glycerin.
DR DrugBank; DB07950; Indoleacetic acid.
DR DrugBank; DB02758; Indolepropionic acid.
DR DrugBank; DB04725; Licofelone.
DR DrugBank; DB02448; N-Tridecanoic Acid.
DR DrugBank; DB04743; Nimesulide.
DR DrugBank; DB03585; Oxyphenbutazone.
DR DrugBank; DB02795; P-Anisic Acid.
DR GuidetoPHARMACOLOGY; 1419; -.
DR SwissLipids; SLP:000001082; -.
DR iPTMnet; Q9NZK7; -.
DR PhosphoSitePlus; Q9NZK7; -.
DR BioMuta; PLA2G2E; -.
DR DMDM; 20139240; -.
DR PaxDb; Q9NZK7; -.
DR PeptideAtlas; Q9NZK7; -.
DR PRIDE; Q9NZK7; -.
DR ProteomicsDB; 83426; -.
DR Antibodypedia; 29744; 35 antibodies from 12 providers.
DR DNASU; 30814; -.
DR Ensembl; ENST00000375116.3; ENSP00000364257.3; ENSG00000188784.4.
DR GeneID; 30814; -.
DR KEGG; hsa:30814; -.
DR MANE-Select; ENST00000375116.3; ENSP00000364257.3; NM_014589.3; NP_055404.1.
DR UCSC; uc001bct.2; human.
DR CTD; 30814; -.
DR DisGeNET; 30814; -.
DR GeneCards; PLA2G2E; -.
DR HGNC; HGNC:13414; PLA2G2E.
DR HPA; ENSG00000188784; Tissue enriched (lymphoid).
DR MIM; 618320; gene.
DR neXtProt; NX_Q9NZK7; -.
DR OpenTargets; ENSG00000188784; -.
DR PharmGKB; PA134889019; -.
DR VEuPathDB; HostDB:ENSG00000188784; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000161504; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; Q9NZK7; -.
DR OMA; IGGSHWP; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9NZK7; -.
DR TreeFam; TF319283; -.
DR PathwayCommons; Q9NZK7; -.
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-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q9NZK7; -.
DR BioGRID-ORCS; 30814; 11 hits in 1068 CRISPR screens.
DR GenomeRNAi; 30814; -.
DR Pharos; Q9NZK7; Tchem.
DR PRO; PR:Q9NZK7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NZK7; protein.
DR Bgee; ENSG00000188784; Expressed in tonsil and 17 other tissues.
DR Genevisible; Q9NZK7; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; TAS:ProtInc.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Disulfide bond; Hydrolase;
KW Inflammatory response; Lipid metabolism; Metal-binding;
KW Phospholipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..142
FT /note="Group IIE secretory phospholipase A2"
FT /id="PRO_0000022757"
FT ACT_SITE 65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 44..135
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 46..62
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 61..115
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 67..142
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 68..108
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 77..101
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT DISULFID 95..106
FT /evidence="ECO:0000269|PubMed:28883454,
FT ECO:0007744|PDB:5WZM"
FT MUTAGEN 40
FT /note="N->G,M,W: Significantly decreases the catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:28883454"
FT MUTAGEN 41
FT /note="D->A,K: Significantly decreases the catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:28883454"
FT MUTAGEN 65
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28883454"
FT MUTAGEN 66
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28883454"
FT MUTAGEN 132
FT /note="N->A,K: Significantly decreases the catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:28883454"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:5Y5E"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5Y5E"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5Y5E"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5Y5E"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5Y5E"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:5Y5E"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5Y5E"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5Y5E"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5Y5E"
FT HELIX 100..118
FT /evidence="ECO:0007829|PDB:5Y5E"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5Y5E"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5Y5E"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5Y5E"
SQ SEQUENCE 142 AA; 15989 MW; 3C360EA710E141FB CRC64;
MKSPHVLVFL CLLVALVTGN LVQFGVMIEK MTGKSALQYN DYGCYCGIGG SHWPVDQTDW
CCHAHDCCYG RLEKLGCEPK LEKYLFSVSE RGIFCAGRTT CQRLTCECDK RAALCFRRNL
GTYNRKYAHY PNKLCTGPTP PC
