PA2GA_MOUSE
ID PA2GA_MOUSE Reviewed; 146 AA.
AC P31482; Q60871;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phospholipase A2, membrane associated;
DE EC=3.1.1.4 {ECO:0000269|PubMed:8425615};
DE AltName: Full=Enhancing factor;
DE Short=EF;
DE AltName: Full=GIIC sPLA2;
DE AltName: Full=Group IIA phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2A;
DE Flags: Precursor;
GN Name=Pla2g2a;
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.
RC STRAIN=BALB/cJ;
RA Mulherkar R.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM.
RC STRAIN=BALB/cJ, and CD-1; TISSUE=Intestine;
RX PubMed=7673223; DOI=10.1074/jbc.270.38.22378;
RA Kennedy B.P., Payette P., Mudgett J., Vadas P., Pruzanski W., Ywan M.,
RA Tang C., Rancourt D.E., Cromlish W.;
RT "A natural disruption of the secretory group II phospholipase A2 gene in
RT inbred mouse strains.";
RL J. Biol. Chem. 270:22378-22385(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RX PubMed=7781071; DOI=10.1016/0092-8674(95)90015-2;
RA MacPhee M., Chepenik K.P., Liddell R.A., Nelson K.K., Siracusa L.D.,
RA Buchberg A.M.;
RT "The secretory phospholipase A2 gene is a candidate for the Mom1 locus, a
RT major modifier of ApcMin-induced intestinal neoplasia.";
RL Cell 81:957-966(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-146, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Small intestine;
RX PubMed=8267767; DOI=10.1006/bbrc.1993.2179;
RA Mulherkar R., Rao R.S., Wagle A.S., Patki V., Deo M.G.;
RT "Enhancing factor, a Paneth cell specific protein from mouse small
RT intestines: predicted amino acid sequence from RT-PCR amplified cDNA and
RT its expression.";
RL Biochem. Biophys. Res. Commun. 195:1254-1263(1993).
RN [6]
RP ERRATUM OF PUBMED:8267767.
RX PubMed=8250944; DOI=10.1006/bbrc.1993.2485;
RA Mulherkar R., Rao R.S., Wagle A.S., Patki V., Deo M.G.;
RL Biochem. Biophys. Res. Commun. 197:351-352(1993).
RN [7]
RP PRELIMINARY PROTEIN SEQUENCE OF 22-41, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Small intestine;
RX PubMed=8425615; DOI=10.1016/0014-5793(93)81289-c;
RA Mulherkar R., Rao R., Rao L., Patki V., Chauhan V.S., Deo M.G.;
RT "Enhancing factor protein from mouse small intestines belongs to the
RT phospholipase A2 family.";
RL FEBS Lett. 317:263-266(1993).
RN [8]
RP FUNCTION.
RX PubMed=10358193;
RA Laine V.J., Grass D.S., Nevalainen T.J.;
RT "Protection by group II phospholipase A2 against Staphylococcus aureus.";
RL J. Immunol. 162:7402-7408(1999).
RN [9]
RP FUNCTION.
RX PubMed=11694541; DOI=10.1074/jbc.m109699200;
RA Koduri R.S., Groenroos J.O., Laine V.J., Le Calvez C., Lambeau G.,
RA Nevalainen T.J., Gelb M.H.;
RT "Bactericidal properties of human and murine groups I, II, V, X, and XII
RT secreted phospholipases A(2).";
RL J. Biol. Chem. 277:5849-5857(2002).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27292189; DOI=10.1016/j.stem.2016.05.023;
RA Schewe M., Franken P.F., Sacchetti A., Schmitt M., Joosten R.,
RA Boettcher R., van Royen M.E., Jeammet L., Payre C., Scott P.M., Webb N.R.,
RA Gelb M., Cormier R.T., Lambeau G., Fodde R.;
RT "Secreted Phospholipases A2 Are Intestinal Stem Cell Niche Factors with
RT Distinct Roles in Homeostasis, Inflammation, and Cancer.";
RL Cell Stem Cell 19:38-51(2016).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids with implications in host
CC antimicrobial defense, inflammatory response and tissue regeneration
CC (PubMed:8425615, PubMed:10358193, PubMed:11694541). Hydrolyzes the
CC ester bond of the fatty acyl group attached at sn-2 position of
CC phospholipids (phospholipase A2 activity) with preference for
CC phosphatidylethanolamines and phosphatidylglycerols over
CC phosphatidylcholines. Contributes to lipid remodeling of cellular
CC membranes and generation of lipid mediators involved in pathogen
CC clearance. Displays bactericidal activity against Gram-positive
CC bacteria by directly hydrolyzing phospholipids of the bacterial
CC membrane (PubMed:11694541). Upon sterile inflammation, targets membrane
CC phospholipids of extracellular mitochondria released from activated
CC platelets, generating free unsaturated fatty acids such as arachidonate
CC that is used by neighboring leukocytes to synthesize inflammatory
CC eicosanoids such as leukotrienes. Simultaneously, by compromising
CC mitochondrial membrane integrity, promotes the release in circulation
CC of potent damage-associated molecular pattern molecules that activate
CC the innate immune response (By similarity). Plays a stem cell regulator
CC role in the intestinal crypt. Within intracellular compartment mediates
CC Paneth cell differentiation and its stem cell supporting functions by
CC inhibiting Wnt signaling pathway in intestinal stem cell (ICS).
CC Secreted in the intestinal lumen upon inflammation, acts in an
CC autocrine way and promotes prostaglandin E2 synthesis that stimulates
CC Wnt signaling pathway in ICS cells and tissue regeneration
CC (PubMed:27292189). May play a role in the biosynthesis of N-acyl
CC ethanolamines that regulate energy metabolism and inflammation.
CC Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines (By similarity).
CC Independent of its catalytic activity, acts as a ligand for integrins.
CC Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and
CC ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the
CC classical ligand-binding site (site 1) and induces integrin
CC conformational changes and enhanced ligand binding to site 1. Induces
CC cell proliferation in an integrin-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P14555, ECO:0000269|PubMed:10358193,
CC ECO:0000269|PubMed:11694541, ECO:0000269|PubMed:27292189,
CC ECO:0000269|PubMed:8425615}.
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:8425615};
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:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14555};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P14555}. Cell
CC membrane {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14555}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14555}.
CC -!- TISSUE SPECIFICITY: Mainly in the Paneth cells adjacent to the stem
CC population in the small intestines. {ECO:0000269|PubMed:27292189,
CC ECO:0000269|PubMed:8267767}.
CC -!- INDUCTION: Up-regulated upon dextran sodium sulfate-induced
CC inflammation in gastrointestinal tract. {ECO:0000269|PubMed:27292189}.
CC -!- POLYMORPHISM: In strains 129/Sv, B10.RIII and C57BL/6, a polymorphism
CC causes a frameshift and premature truncation of the protein, rendering
CC it inactive. Strains BALB/c, C3H/He, DBA/1, DBA/2, MRL and NZB/B1N
CC contain the normal protein while strain CD-1 is heterozygous for the
CC mutation. {ECO:0000269|PubMed:7673223}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB06315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X74266; CAA52325.1; -; mRNA.
DR EMBL; U32358; AAC52252.1; -; Genomic_DNA.
DR EMBL; U28244; AAB06315.1; ALT_INIT; mRNA.
DR EMBL; BC045156; AAH45156.1; -; mRNA.
DR PIR; I48342; I48342.
DR PIR; S29495; S29495.
DR RefSeq; NP_001076000.1; NM_001082531.1.
DR AlphaFoldDB; P31482; -.
DR SMR; P31482; -.
DR BioGRID; 202219; 4.
DR BindingDB; P31482; -.
DR ChEMBL; CHEMBL5761; -.
DR PhosphoSitePlus; P31482; -.
DR PRIDE; P31482; -.
DR DNASU; 18780; -.
DR GeneID; 18780; -.
DR KEGG; mmu:18780; -.
DR UCSC; uc008vlk.1; mouse.
DR CTD; 5320; -.
DR MGI; MGI:104642; Pla2g2a.
DR InParanoid; P31482; -.
DR PhylomeDB; P31482; -.
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-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 18780; 2 hits in 23 CRISPR screens.
DR PRO; PR:P31482; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P31482; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; IGI:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:1902563; P:regulation of neutrophil activation; ISS:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
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 Antimicrobial; Bacteriolytic enzyme; Calcium; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Growth regulation; Hydrolase;
KW Inflammatory response; Lipid degradation; Lipid metabolism; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Phospholipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..146
FT /note="Phospholipase A2, membrane associated"
FT /id="PRO_0000022751"
FT ACT_SITE 68
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT SITE 122
FT /note="Important for integrin binding"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 47..139
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 49..65
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 64..119
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 70..146
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 71..112
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 80..105
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 98..110
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT CONFLICT 19
FT /note="V -> D (in Ref. 1; CAA52325)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="K -> T (in Ref. 1; CAA52325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16145 MW; AB904F6B3B1BA5C7 CRC64;
MKVLLLLAAS IMAFGSIQVQ GNIAQFGEMI RLKTGKRAEL SYAFYGCHCG LGGKGSPKDA
TDRCCVTHDC CYKSLEKSGC GTKLLKYKYS HQGGQITCSA NQNSCQKRLC QCDKAAAECF
ARNKKTYSLK YQFYPNMFCK GKKPKC
