PA21B_PIG
ID PA21B_PIG Reviewed; 146 AA.
AC P00592;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Phospholipase A2, major isoenzyme;
DE EC=3.1.1.4 {ECO:0000269|PubMed:17603006};
DE AltName: Full=Group IB phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE Flags: Precursor;
GN Name=PLA2G1B;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=3295782; DOI=10.1093/nar/15.9.3743;
RA de Geus P., van den Bergh C.J., Kuipers O., Verheij H.M., Hoekstra W.P.M.,
RA de Haas G.H.;
RT "Expression of porcine pancreatic phospholipase A2. Generation of active
RT enzyme by sequence-specific cleavage of a hybrid protein from Escherichia
RT coli.";
RL Nucleic Acids Res. 15:3743-3759(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=3028739; DOI=10.1089/dna.1.1986.5.519;
RA Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K.;
RT "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from
RT porcine pancreas and human lung.";
RL DNA 5:519-527(1986).
RN [3]
RP PROTEIN SEQUENCE OF 16-146, AND PYROGLUTAMATE FORMATION AT GLN-16.
RX PubMed=5528841; DOI=10.1016/0005-2795(70)90195-9;
RA de Haas G.H., Slotboom A.J., Bonsen P.P.M., van Deenen L.L.M., Maroux S.,
RA Puigserver A., Desnuelle P.;
RT "Studies on phospholipase A and its zymogen from porcine pancreas. I. The
RT complete amino acid sequence.";
RL Biochim. Biophys. Acta 221:31-53(1970).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=884127; DOI=10.1016/0005-2795(77)90076-9;
RA Puijk W.C., Verheij H.M., de Haas G.H.;
RT "The primary structure of phospholipase A2 from porcine pancreas. A
RT reinvestigation.";
RL Biochim. Biophys. Acta 492:254-259(1977).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=4919729; DOI=10.1016/0005-2795(70)90196-0;
RA de Haas G.H., Slotboom A.J., Bonsen P.P.M., Nieuwenhuizen W.,
RA van Deenen L.L.M., Maroux S., Dlouha V., Desnuelle P.;
RT "Studies on phospholipase A and its zymogen from porcine pancreas. II. The
RT assignment of the position of the six disulfide bridges.";
RL Biochim. Biophys. Acta 221:54-61(1970).
RN [6]
RP PALMITOYLATION AT LYS-78.
RC TISSUE=Pancreas;
RX PubMed=2498336; DOI=10.1016/s0021-9258(18)81764-1;
RA Tomasselli A.G., Hui J., Fisher J., Zuercher-Neely H., Reardon H.M.,
RA Oriaku E., Kezdy F.J., Heinrikson R.L.;
RT "Dimerization and activation of porcine pancreatic phospholipase A2 via
RT substrate level acylation of lysine 56.";
RL J. Biol. Chem. 264:10041-10047(1989).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP 62-GLU--CYS-66.
RX PubMed=17603006; DOI=10.1016/j.bbamem.2007.05.019;
RA Yu B.Z., Apitz-Castro R.J., Jain M.K., Berg O.G.;
RT "Role of 57-72 loop in the allosteric action of bile salts on pancreatic IB
RT phospholipase A(2): regulation of fat and cholesterol homeostasis.";
RL Biochim. Biophys. Acta 1768:2478-2490(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), ACTIVE SITE, AND BINDING SITES.
RX PubMed=6876174; DOI=10.1016/s0022-2836(83)80328-3;
RA Dijkstra B.W., Renetseder R., Kalk K.H., Hol W.G.J., Drenth J.;
RT "Structure of porcine pancreatic phospholipase A2 at 2.6-A resolution and
RT comparison with bovine phospholipase A2.";
RL J. Mol. Biol. 168:163-179(1983).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=2254938; DOI=10.1016/s0022-2836(05)80332-8;
RA Thunnissen M.M.G.M., Kalk K.H., Drenth J., Dijkstra B.W.;
RT "Structure of an engineered porcine phospholipase A2 with enhanced activity
RT at 2.1-A resolution. Comparison with the wild-type porcine and Crotalus
RT atrox phospholipase A2.";
RL J. Mol. Biol. 216:425-439(1990).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=2215698; DOI=10.1038/347689a0;
RA Thunnissen M.M.G.M., Ab E., Kalk K.H., Drenth J., Dijkstra B.W.,
RA Kuipers O.P., Dijkman R., de Haas G.H., Verheij H.M.;
RT "X-ray structure of phospholipase A2 complexed with a substrate-derived
RT inhibitor.";
RL Nature 347:689-691(1990).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=2007145; DOI=10.1021/bi00226a022;
RA Dekker N., Peters A.R., Slotboom A.J., Boelens R., Kaptein R.,
RA de Haas G.H.;
RT "Porcine pancreatic phospholipase A2: sequence-specific 1H and 15N NMR
RT assignments and secondary structure.";
RL Biochemistry 30:3135-3147(1991).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=7664098; DOI=10.1038/nsb0595-402;
RA van den Berg B., Tessari M., Boelens R., Dijkman R., de Haas G.H.,
RA Kaptein R., Verheij H.M.;
RT "NMR structures of phospholipase A2 reveal conformational changes during
RT interfacial activation.";
RL Nat. Struct. Biol. 2:402-406(1995).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=7556053;
RA van den Berg B., Tessari M., de Haas G.H., Verheij H.M., Boelens R.,
RA Kaptein R.;
RT "Solution structure of porcine pancreatic phospholipase A2.";
RL EMBO J. 14:4123-4131(1995).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=7703697; DOI=10.1007/bf00208802;
RA van den Berg B., Tessari M., Boelens R., Dijkman R., Kaptein R.,
RA de Haas G.H., Verheij H.M.;
RT "Solution structure of porcine pancreatic phospholipase A2 complexed with
RT micelles and a competitive inhibitor.";
RL J. Biomol. NMR 5:110-121(1995).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets dietary phospholipids in the intestinal tract
CC (PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group
CC attached at sn-2 position of phospholipids (phospholipase A2 activity)
CC with preference for phosphatidylethanolamines and phosphatidylglycerols
CC over phosphatidylcholines (By similarity). May play a role in the
CC biosynthesis of N-acyl ethanolamines that regulate energy metabolism
CC and inflammation in the intestinal tract. Hydrolyzes N-acyl
CC phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines,
CC which are further cleaved by a lysophospholipase D to release N-acyl
CC ethanolamines (By similarity). May act in an autocrine and paracrine
CC manner (By similarity). Has anti-helminth activity in a process
CC regulated by gut microbiota. Upon helminth infection of intestinal
CC epithelia, directly affects phosphatidylethanolamine contents in the
CC membrane of helminth larvae, likely controlling an array of
CC phospholipid-mediated cellular processes such as membrane fusion and
CC cell division while providing for better immune recognition, ultimately
CC reducing larvae integrity and infectivity (By similarity).
CC {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055,
CC ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:17603006}.
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:17603006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:131738;
CC Evidence={ECO:0000269|PubMed:17603006};
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:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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:0000250|UniProtKB:P04054};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P04054};
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:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:P04054};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:P04054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) +
CC N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00593};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
CC -!- ACTIVITY REGULATION: Regulated by bile acid salts. Up-regulated by
CC cholate and down-regulated by taurochenodeoxycholate.
CC {ECO:0000269|PubMed:17603006}.
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:2498336}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}.
CC Note=Secreted from pancreatic acinar cells in its inactive form.
CC {ECO:0000250|UniProtKB:P04054}.
CC -!- PTM: Acylation causes dimerization. {ECO:0000269|PubMed:2498336}.
CC -!- PTM: Activated by trypsin cleavage in the duodenum. Can also be
CC activated by thrombin or autocatalytically.
CC {ECO:0000250|UniProtKB:P04054}.
CC -!- MISCELLANEOUS: Loss of activity upon alkylation of His-70 with p-bromo
CC phenacyl bromide; Ca(2+) and Ba(2+) protect against inactivation.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; Y00146; CAA68341.1; -; mRNA.
DR EMBL; M21055; AAA31101.1; -; mRNA.
DR PIR; B25793; PSPGA.
DR RefSeq; NP_001004037.1; NM_001004037.1.
DR PDB; 1FX9; X-ray; 2.00 A; A/B=23-146.
DR PDB; 1FXF; X-ray; 1.85 A; A/B=23-146.
DR PDB; 1HN4; X-ray; 1.50 A; A/B=16-146.
DR PDB; 1L8S; X-ray; 1.55 A; A/B=23-146.
DR PDB; 1P2P; X-ray; 2.60 A; A=23-146.
DR PDB; 1PIR; NMR; -; A=23-146.
DR PDB; 1PIS; NMR; -; A=23-146.
DR PDB; 1SFV; NMR; -; A=23-146.
DR PDB; 1SFW; NMR; -; A=23-146.
DR PDB; 1Y6O; X-ray; 2.00 A; A/B=23-146.
DR PDB; 1Y6P; X-ray; 2.25 A; A/B=23-146.
DR PDB; 2AZY; X-ray; 1.90 A; A=23-146.
DR PDB; 2AZZ; X-ray; 2.20 A; A=23-146.
DR PDB; 2B00; X-ray; 1.85 A; A=23-146.
DR PDB; 2B01; X-ray; 2.20 A; A=23-146.
DR PDB; 2B03; X-ray; 2.30 A; A=23-146.
DR PDB; 2B04; X-ray; 2.50 A; A=23-146.
DR PDB; 2PHI; X-ray; 2.20 A; A/B=23-146.
DR PDB; 3FVI; X-ray; 2.70 A; A/B/C/D=23-146.
DR PDB; 3FVJ; X-ray; 2.30 A; A=23-146.
DR PDB; 3HSW; X-ray; 2.50 A; A=23-146.
DR PDB; 3L30; X-ray; 2.40 A; A=23-146.
DR PDB; 3O4M; X-ray; 2.50 A; A=23-146.
DR PDB; 3P2P; X-ray; 2.10 A; A/B=23-146.
DR PDB; 3QLM; X-ray; 2.50 A; A=23-146.
DR PDB; 4DBK; X-ray; 2.30 A; A=23-146.
DR PDB; 4G5I; X-ray; 2.40 A; A=23-146.
DR PDB; 4O1Y; X-ray; 2.50 A; A=23-146.
DR PDB; 4P2P; X-ray; 2.40 A; A=23-146.
DR PDB; 5P2P; X-ray; 2.40 A; A/B=23-146.
DR PDBsum; 1FX9; -.
DR PDBsum; 1FXF; -.
DR PDBsum; 1HN4; -.
DR PDBsum; 1L8S; -.
DR PDBsum; 1P2P; -.
DR PDBsum; 1PIR; -.
DR PDBsum; 1PIS; -.
DR PDBsum; 1SFV; -.
DR PDBsum; 1SFW; -.
DR PDBsum; 1Y6O; -.
DR PDBsum; 1Y6P; -.
DR PDBsum; 2AZY; -.
DR PDBsum; 2AZZ; -.
DR PDBsum; 2B00; -.
DR PDBsum; 2B01; -.
DR PDBsum; 2B03; -.
DR PDBsum; 2B04; -.
DR PDBsum; 2PHI; -.
DR PDBsum; 3FVI; -.
DR PDBsum; 3FVJ; -.
DR PDBsum; 3HSW; -.
DR PDBsum; 3L30; -.
DR PDBsum; 3O4M; -.
DR PDBsum; 3P2P; -.
DR PDBsum; 3QLM; -.
DR PDBsum; 4DBK; -.
DR PDBsum; 4G5I; -.
DR PDBsum; 4O1Y; -.
DR PDBsum; 4P2P; -.
DR PDBsum; 5P2P; -.
DR AlphaFoldDB; P00592; -.
DR BMRB; P00592; -.
DR SMR; P00592; -.
DR STRING; 9823.ENSSSCP00000028002; -.
DR BindingDB; P00592; -.
DR ChEMBL; CHEMBL4715; -.
DR DrugCentral; P00592; -.
DR SwissLipids; SLP:000001435; -.
DR PaxDb; P00592; -.
DR Ensembl; ENSSSCT00035052384; ENSSSCP00035021070; ENSSSCG00035039434.
DR Ensembl; ENSSSCT00045058963; ENSSSCP00045041273; ENSSSCG00045034381.
DR Ensembl; ENSSSCT00055029475; ENSSSCP00055023471; ENSSSCG00055014901.
DR GeneID; 445525; -.
DR KEGG; ssc:445525; -.
DR CTD; 5319; -.
DR eggNOG; KOG4087; Eukaryota.
DR InParanoid; P00592; -.
DR OrthoDB; 1422829at2759; -.
DR BRENDA; 3.1.1.4; 6170.
DR EvolutionaryTrace; P00592; -.
DR PRO; PR:P00592; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032052; F:bile acid binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IDA:BHF-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:BHF-UCL.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:BHF-UCL.
DR GO; GO:0002446; P:neutrophil mediated immunity; IDA:BHF-UCL.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
DR GO; GO:0050778; P:positive regulation of immune response; IDA:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0046324; P:regulation of glucose import; IDA:BHF-UCL.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
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; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid metabolism; Lipoprotein; Metal-binding;
KW Palmitate; Phospholipid metabolism; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:5528841"
FT PROPEP 16..22
FT /note="Activation peptide"
FT /id="PRO_0000022743"
FT CHAIN 23..146
FT /note="Phospholipase A2, major isoenzyme"
FT /id="PRO_0000022744"
FT ACT_SITE 70
FT /evidence="ECO:0000269|PubMed:6876174"
FT ACT_SITE 121
FT /evidence="ECO:0000269|PubMed:6876174"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT MOD_RES 16
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5528841"
FT LIPID 78
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000269|PubMed:2498336"
FT DISULFID 33..99
FT /evidence="ECO:0000269|PubMed:4919729"
FT DISULFID 49..146
FT /evidence="ECO:0000269|PubMed:4919729"
FT DISULFID 51..67
FT /evidence="ECO:0000269|PubMed:4919729"
FT DISULFID 66..127
FT /evidence="ECO:0000269|PubMed:4919729"
FT DISULFID 73..120
FT /evidence="ECO:0000269|PubMed:4919729"
FT DISULFID 83..113
FT /evidence="ECO:0000269|PubMed:4919729"
FT DISULFID 106..118
FT /evidence="ECO:0000269|PubMed:4919729"
FT MUTAGEN 62..66
FT /note="Missing: Impairs the hydrolysis rate-lowering effect
FT of taurochenodeoxycholate."
FT /evidence="ECO:0000269|PubMed:17603006"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:1HN4"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3O4M"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1HN4"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1FXF"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1HN4"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1HN4"
FT HELIX 62..78
FT /evidence="ECO:0007829|PDB:1HN4"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1HN4"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1HN4"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1HN4"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1HN4"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1P2P"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:1HN4"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1HN4"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1HN4"
SQ SEQUENCE 146 AA; 16279 MW; DE87674C9476FA36 CRC64;
MKFLVLAVLL TVGAAQEGIS SRALWQFRSM IKCAIPGSHP LMDFNNYGCY CGLGGSGTPV
DELDRCCETH DNCYRDAKNL DSCKFLVDNP YTESYSYSCS NTEITCNSKN NACEAFICNC
DRNAAICFSK APYNKEHKNL DTKKYC
