PA2G5_MOUSE
ID PA2G5_MOUSE Reviewed; 137 AA.
AC P97391; Q9QZU6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phospholipase A2 group V;
DE EC=3.1.1.4 {ECO:0000269|PubMed:14962950};
DE AltName: Full=PLA2-10;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 5;
DE Flags: Precursor;
GN Name=Pla2g5;
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 [MRNA].
RC STRAIN=129;
RX PubMed=8838795; DOI=10.1006/geno.1996.0126;
RA Tischfield J.A., Xia Y.R., Shih D.M., Klisak I., Chen J., Engle S.J.,
RA Siakotos A.N., Winstead M.V., Seilhamer J.J., Allamand V., Gyapay G.,
RA Lusis A.;
RT "Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked
RT and map to homologous chromosome regions in mouse and human.";
RL Genomics 32:328-333(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=10531350; DOI=10.1074/jbc.274.44.31476;
RA Bingham C.O. III, Fijneman R.J.A., Friend D.S., Goddeau R.P., Rogers R.A.,
RA Austen K.F., Arm J.P.;
RT "Low molecular weight group IIA and group V phospholipase A(2) enzymes have
RT different intracellular locations in mouse bone marrow-derived mast
RT cells.";
RL J. Biol. Chem. 274:31476-31484(1999).
RN [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14962950; DOI=10.1161/01.atv.0000122363.02961.c1;
RA Wooton-Kee C.R., Boyanovsky B.B., Nasser M.S., de Villiers W.J., Webb N.R.;
RT "Group V sPLA2 hydrolysis of low-density lipoprotein results in spontaneous
RT particle aggregation and promotes macrophage foam cell formation.";
RL Arterioscler. Thromb. Vasc. Biol. 24:762-767(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16407308; DOI=10.1074/jbc.m508314200;
RA Balestrieri B., Hsu V.W., Gilbert H., Leslie C.C., Han W.K.,
RA Bonventre J.V., Arm J.P.;
RT "Group V secretory phospholipase A2 translocates to the phagosome after
RT zymosan stimulation of mouse peritoneal macrophages and regulates
RT phagocytosis.";
RL J. Biol. Chem. 281:6691-6698(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19342668; DOI=10.4049/jimmunol.0803776;
RA Balestrieri B., Maekawa A., Xing W., Gelb M.H., Katz H.R., Arm J.P.;
RT "Group V secretory phospholipase A2 modulates phagosome maturation and
RT regulates the innate immune response against Candida albicans.";
RL J. Immunol. 182:4891-4898(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-67.
RX PubMed=20432503; DOI=10.1002/emmm.201000072;
RA Boilard E., Lai Y., Larabee K., Balestrieri B., Ghomashchi F., Fujioka D.,
RA Gobezie R., Coblyn J.S., Weinblatt M.E., Massarotti E.M., Thornhill T.S.,
RA Divangahi M., Remold H., Lambeau G., Gelb M.H., Arm J.P., Lee D.M.;
RT "A novel anti-inflammatory role for secretory phospholipase A2 in immune
RT complex-mediated arthritis.";
RL EMBO Mol. Med. 2:172-187(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20817863; DOI=10.4049/jimmunol.1001384;
RA Giannattasio G., Fujioka D., Xing W., Katz H.R., Boyce J.A.,
RA Balestrieri B.;
RT "Group V secretory phospholipase A2 reveals its role in house dust mite-
RT induced allergic pulmonary inflammation by regulation of dendritic cell
RT function.";
RL J. Immunol. 185:4430-4438(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP HIGH-FAT DIET.
RX PubMed=24910243; DOI=10.1016/j.cmet.2014.05.002;
RA Sato H., Taketomi Y., Ushida A., Isogai Y., Kojima T., Hirabayashi T.,
RA Miki Y., Yamamoto K., Nishito Y., Kobayashi T., Ikeda K., Taguchi R.,
RA Hara S., Ida S., Miyamoto Y., Watanabe M., Baba H., Miyata K., Oike Y.,
RA Gelb M.H., Murakami M.;
RT "The adipocyte-inducible secreted phospholipases PLA2G5 and PLA2G2E play
RT distinct roles in obesity.";
RL Cell Metab. 20:119-132(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29346348; DOI=10.1038/mi.2017.99;
RA Yamaguchi M., Samuchiwal S.K., Quehenberger O., Boyce J.A., Balestrieri B.;
RT "Macrophages regulate lung ILC2 activation via Pla2g5-dependent
RT mechanisms.";
RL Mucosal Immunol. 11:615-626(2018).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids. Hydrolyzes the ester bond of the
CC fatty acyl group attached at sn-2 position of phospholipids
CC (phospholipase A2 activity), preferentially releasing fatty acyl groups
CC with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl
CC (C18:2) groups (PubMed:14962950). Hydrolyzes low-density lipoprotein
CC (LDL) phospholipids releasing unsaturated fatty acids that drive
CC macrophage polarization toward an M2 phenotype (PubMed:14962950,
CC PubMed:24910243). May act in an autocrine and paracrine manner.
CC Contributes to lipid remodeling of cellular membranes at different
CC subcellular locations and generation of lipid mediators involved in
CC pathogen clearance. Cleaves sn-2 fatty acyl chains of cardiolipin, a
CC major component of the inner membrane of mitochondria and bacterial
CC membranes (By similarity). Promotes phagocytosis of bacteria in
CC macrophages through production of lysophosphatidylethanolamines (By
CC similarity). Displays bactericidal activity against Gram-positive
CC bacteria by directly hydrolyzing the phospholipids of the bacterial
CC membrane (PubMed:11694541, PubMed:16407308). Promotes phagocytosis and
CC killing of ingested fungi likely through controlling phagosome-lysosome
CC fusion and phagosome maturation (PubMed:19342668). Plays a role in
CC biosynthesis of cysteinyl leukotrienes (CysLTs) in myeloid cells (By
CC similarity). In eosinophils, triggers perinuclear arachidonate release
CC and LTC4 synthesis in a PLA2G4A-independent way (By similarity). In
CC neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A (By
CC similarity). Promotes immune complex clearance in macrophages via
CC stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger
CC phagocytosis (PubMed:20432503). May regulate antigen processing in
CC antigen-presenting cells (PubMed:20817863). In pulmonary macrophages
CC regulates IL33 production required for activation of group 2 innate
CC lymphoid cells (PubMed:29346348). May play a role in the biosynthesis
CC of N-acyl ethanolamines that regulate energy metabolism. Hydrolyzes N-
CC acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines,
CC which are further cleaved by a lysophospholipase D to release N-acyl
CC ethanolamines (By similarity). {ECO:0000250|UniProtKB:P39877,
CC ECO:0000269|PubMed:11694541, ECO:0000269|PubMed:14962950,
CC ECO:0000269|PubMed:16407308, ECO:0000269|PubMed:19342668,
CC ECO:0000269|PubMed:20432503, ECO:0000269|PubMed:20817863,
CC ECO:0000269|PubMed:24910243, ECO:0000269|PubMed:29346348}.
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:14962950};
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:14962950};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:14962950};
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:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P39877};
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:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P39877};
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:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + 1-octadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+);
CC Xref=Rhea:RHEA:41215, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:74243, ChEBI:CHEBI:133606;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41216;
CC Evidence={ECO:0000250|UniProtKB:P39877};
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:14962950};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000305|PubMed:14962950};
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:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-
CC octadecenoate + 1',3'-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H(+); Xref=Rhea:RHEA:40467, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77256,
CC ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40468;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H2O = (9Z)-octadecenoate + 1'-[1,2-di-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H(+); Xref=Rhea:RHEA:40463, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77253,
CC ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40464;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:P39877}.
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC {ECO:0000250|UniProtKB:P39877}.
CC -!- PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis.
CC {ECO:0000250|UniProtKB:P39877}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10531350}. Cell
CC membrane {ECO:0000269|PubMed:10531350}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:16407308}. Recycling endosome
CC {ECO:0000269|PubMed:16407308}. Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:16407308}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:16407308}.
CC -!- TISSUE SPECIFICITY: Expressed in peritoneal macrophages (at protein
CC level) (PubMed:16407308). Expressed in heart, skeletal muscle and white
CC adipose tissue (PubMed:24910243). {ECO:0000269|PubMed:16407308,
CC ECO:0000269|PubMed:24910243}.
CC -!- INDUCTION: Up-regulated in white adipocytes upon high-fat diet.
CC {ECO:0000269|PubMed:24910243}.
CC -!- PTM: This enzyme lacks one of the seven disulfide bonds found in
CC similar PA2 proteins.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show increased high-fat diet induced
CC obesity, increased visceral fat depositions and exacerbated INS
CC resistance (PubMed:24910243). In a model of systemic candidiasis,
CC mutant mice are deficient in clearing C. albicans in kidney, liver and
CC spleen, resulting in increased mortality (PubMed:19342668). In K/BxN
CC serum transfer arthritis model, a well-described mouse model of
CC inflammatory arthritis, mutant mice develop severe autoantibody-driven
CC arthritic response characterized by increased leukocytic tissue
CC infiltration, pannus formation and bone and cartilage destruction
CC (PubMed:20432503). In a model of allergic pulmonary inflammation
CC induced by dust mite D. farinae, mutant mice show impaired T helper
CC type 2 immune response associated with markedly decreased granulocyte
CC infiltration in bronchoalveolar fluid and decreased goblet cell
CC metaplasia (PubMed:20817863). In a model of antigen-induced asthma
CC following repetitive A. Alternata inhalation, mutant mice display
CC impaired pulmonary eosinophil infiltration and overall impaired
CC allergen-induced inflammation (PubMed:29346348).
CC {ECO:0000269|PubMed:19342668, ECO:0000269|PubMed:20432503,
CC ECO:0000269|PubMed:20817863, ECO:0000269|PubMed:24910243,
CC ECO:0000269|PubMed:29346348}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; U66873; AAC53038.1; -; mRNA.
DR EMBL; AF162713; AAD45807.1; -; mRNA.
DR CCDS; CCDS18834.1; -.
DR RefSeq; NP_001116426.1; NM_001122954.1.
DR RefSeq; NP_035240.3; NM_011110.4.
DR RefSeq; XP_006538721.2; XM_006538658.3.
DR RefSeq; XP_011248510.1; XM_011250208.2.
DR RefSeq; XP_017175532.1; XM_017320043.1.
DR RefSeq; XP_017175533.1; XM_017320044.1.
DR AlphaFoldDB; P97391; -.
DR SMR; P97391; -.
DR STRING; 10090.ENSMUSP00000099569; -.
DR BindingDB; P97391; -.
DR ChEMBL; CHEMBL4167; -.
DR PaxDb; P97391; -.
DR PRIDE; P97391; -.
DR ProteomicsDB; 294318; -.
DR DNASU; 18784; -.
DR GeneID; 18784; -.
DR KEGG; mmu:18784; -.
DR CTD; 5322; -.
DR MGI; MGI:101899; Pla2g5.
DR eggNOG; KOG4087; Eukaryota.
DR InParanoid; P97391; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P97391; -.
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 UniPathway; UPA00085; -.
DR UniPathway; UPA00878; -.
DR UniPathway; UPA00879; -.
DR BioGRID-ORCS; 18784; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pla2g5; mouse.
DR PRO; PR:P97391; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97391; protein.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032010; C:phagolysosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISO:MGI.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IDA:UniProtKB.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; ISO:MGI.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0090265; P:positive regulation of immune complex clearance by monocytes and macrophages; IMP:UniProtKB.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IMP:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:1905164; P:positive regulation of phagosome maturation; IMP:UniProtKB.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:MGI.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP: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 Calcium; Cell membrane; Cytoplasmic vesicle; Disulfide bond; Endosome;
KW Fatty acid metabolism; Golgi apparatus; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Phagocytosis;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..137
FT /note="Phospholipase A2 group V"
FT /id="PRO_0000022762"
FT ACT_SITE 67
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 46..137
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000250"
FT DISULFID 63..117
FT /evidence="ECO:0000250"
FT DISULFID 70..110
FT /evidence="ECO:0000250"
FT DISULFID 79..103
FT /evidence="ECO:0000250"
FT DISULFID 97..108
FT /evidence="ECO:0000250"
FT MUTAGEN 67
FT /note="H->Q: Impairs cysteinyl leukotrienes synthesis and
FT phagocytosis of IgG immune complexes by synovial fluid
FT monocyte/macrophage cells."
FT /evidence="ECO:0000269|PubMed:20432503"
FT CONFLICT 34
FT /note="G -> R (in Ref. 1; AAC53038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15859 MW; F08920E1FD1D912A CRC64;
MKGLLTLAWF LACSVPAVPG GLLELKSMIE KVTGKNAFKN YGFYGCYCGW GGRGTPKDGT
DWCCQMHDRC YGQLEEKDCA IRTQSYDYRY TNGLVICEHD SFCPMRLCAC DRKLVYCLRR
NLWTYNPLYQ YYPNFLC
