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   24-JAN-2024, entry version 162.
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-
CC         phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC         glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:44524,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:84472, ChEBI:CHEBI:84475;
CC         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.ENSMUSP00000099571; -.
DR   BindingDB; P97391; -.
DR   ChEMBL; CHEMBL4167; -.
DR   PaxDb; 10090-ENSMUSP00000099569; -.
DR   ProteomicsDB; 294318; -.
DR   DNASU; 18784; -.
DR   GeneID; 18784; -.
DR   KEGG; mmu:18784; -.
DR   AGR; MGI:101899; -.
DR   CTD; 5322; -.
DR   MGI; MGI:101899; Pla2g5.
DR   eggNOG; KOG4087; Eukaryota.
DR   InParanoid; P97391; -.
DR   OrthoDB; 638584at2759; -.
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; 2 hits in 79 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; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
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:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
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:0043030; P:regulation of macrophage activation; IMP:MGI.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 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; PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11716:SF10; PHOSPHOLIPASE A2 GROUP V; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 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
//