ID PA2GX_MOUSE Reviewed; 151 AA. AC Q9QXX3; Q9EQK6; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 172. DE RecName: Full=Group 10 secretory phospholipase A2; DE EC=3.1.1.4 {ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:12359733}; DE AltName: Full=Group X secretory phospholipase A2; DE Short=GX sPLA2; DE Short=sPLA2-X; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 10; DE Flags: Precursor; GN Name=Pla2g10; 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], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=10531313; DOI=10.1074/jbc.274.44.31195; RA Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.; RT "On the diversity of secreted phospholipases A2. Cloning, tissue RT distribution, and functional expression of two novel mouse group II RT enzymes."; RL J. Biol. Chem. 274:31195-31202(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-30, CHARACTERIZATION, RP TISSUE SPECIFICITY, AND INTERACTION WITH PLA2R1. RC STRAIN=BALB/cJ; RX PubMed=11019817; DOI=10.1006/abbi.2000.1977; RA Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T., Nakano K., RA Fujii N., Ishizaki J., Arita H., Hanasaki K.; RT "Mouse group X secretory phospholipase A2 induces a potent release of RT arachidonic acid from spleen cells and acts as a ligand for the RT phospholipase A2 receptor."; RL Arch. Biochem. Biophys. 381:31-42(2000). RN [3] RP INTERACTION WITH PLA2R1, AND SUBCELLULAR LOCATION. RX PubMed=11741598; DOI=10.1016/s0014-5793(01)03173-8; RA Yokota Y., Notoya M., Higashino K., Ishimoto Y., Nakano K., Arita H., RA Hanasaki K.; RT "Clearance of group X secretory phospholipase A(2) via mouse phospholipase RT A(2) receptor."; RL FEBS Lett. 509:250-254(2001). RN [4] 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 [5] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12359733; DOI=10.1074/jbc.m205855200; RA Singer A.G., Ghomashchi F., Le Calvez C., Bollinger J., Bezzine S., RA Rouault M., Sadilek M., Nguyen E., Lazdunski M., Lambeau G., Gelb M.H.; RT "Interfacial kinetic and binding properties of the complete set of human RT and mouse groups I, II, V, X, and XII secreted phospholipases A2."; RL J. Biol. Chem. 277:48535-48549(2002). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RX PubMed=17403936; DOI=10.1084/jem.20070029; RA Henderson W.R. Jr., Chi E.Y., Bollinger J.G., Tien Y.T., Ye X., RA Castelli L., Rubtsov Y.P., Singer A.G., Chiang G.K., Nevalainen T., RA Rudensky A.Y., Gelb M.H.; RT "Importance of group X-secreted phospholipase A2 in allergen-induced airway RT inflammation and remodeling in a mouse asthma model."; RL J. Exp. Med. 204:865-877(2007). RN [7] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, RP AND MUTAGENESIS OF HIS-74. RX PubMed=20424324; DOI=10.1172/jci40494; RA Escoffier J., Jemel I., Tanemoto A., Taketomi Y., Payre C., Coatrieux C., RA Sato H., Yamamoto K., Masuda S., Pernet-Gallay K., Pierre V., Hara S., RA Murakami M., De Waard M., Lambeau G., Arnoult C.; RT "Group X phospholipase A2 is released during sperm acrosome reaction and RT controls fertility outcome in mice."; RL J. Clin. Invest. 120:1415-1428(2010). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP DISRUPTION PHENOTYPE. RX PubMed=21266583; DOI=10.1074/jbc.m110.206714; RA Yamamoto K., Taketomi Y., Isogai Y., Miki Y., Sato H., Masuda S., RA Nishito Y., Morioka K., Ishimoto Y., Suzuki N., Yokota Y., Hanasaki K., RA Ishikawa Y., Ishii T., Kobayashi T., Fukami K., Ikeda K., Nakanishi H., RA Taguchi R., Murakami M.; RT "Hair follicular expression and function of group X secreted phospholipase RT A2 in mouse skin."; RL J. Biol. Chem. 286:11616-11631(2011). RN [9] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=21266581; DOI=10.1074/jbc.m110.206755; RA Sato H., Isogai Y., Masuda S., Taketomi Y., Miki Y., Kamei D., Hara S., RA Kobayashi T., Ishikawa Y., Ishii T., Ikeda K., Taguchi R., Ishimoto Y., RA Suzuki N., Yokota Y., Hanasaki K., Suzuki-Yamamoto T., Yamamoto K., RA Murakami M.; RT "Physiological roles of group X-secreted phospholipase A2 in reproduction, RT gastrointestinal phospholipid digestion, and neuronal function."; RL J. Biol. Chem. 286:11632-11648(2011). RN [10] RP FUNCTION, AND TISSUE SPECIFICITY. 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). RN [11] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RX PubMed=29093264; DOI=10.1172/jci.insight.94929; RA Nolin J.D., Lai Y., Ogden H.L., Manicone A.M., Murphy R.C., An D., RA Frevert C.W., Ghomashchi F., Naika G.S., Gelb M.H., Gauvreau G.M., RA Piliponsky A.M., Altemeier W.A., Hallstrand T.S.; RT "Secreted PLA2 group X orchestrates innate and adaptive immune responses to RT inhaled allergen."; RL JCI Insight 2:0-0(2017). 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 with CC preference for phosphatidylcholines and phosphatidylglycerols over CC phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and CC omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty CC acyls (PubMed:12359733, PubMed:10531313). Contributes to phospholipid CC remodeling of very low-density lipoprotein (VLDL), low-density CC lipoprotein (LDL) and high-density lipoprotein (HDL) particles (By CC similarity). Hydrolyzes LDL phospholipids releasing unsaturated fatty CC acids that regulate macrophage differentiation toward foam cells (By CC similarity). Efficiently hydrolyzes and inactivates PAF, a potent lipid CC mediator present in oxidized LDL (By similarity). May act in an CC autocrine and paracrine manner. Secreted by lung epithelium, targets CC membrane phospholipids of infiltrating eosinophils, releasing CC arachidonate and boosting eicosanoid and cysteinyl leukotriene CC synthesis involved in airway inflammatory response (PubMed:29093264, CC PubMed:17403936). Secreted by gut epithelium, hydrolyzes dietary and CC biliary phosphatidylcholines in the gastrointestinal lumen, thereby CC regulating adipogenesis and body weight (PubMed:21266581). Plays a stem CC cell regulator role in colon epithelium. Within intracellular CC compartment, mediates Paneth-like cell differentiation and its stem CC cell supporting functions by inhibiting Wnt signaling pathway in CC intestinal stem cell (ISC). Secreted in the intestinal lumen upon CC inflammation, acts in an autocrine way and promotes prostaglandin E2 CC synthesis that stimulates the Wnt signaling pathway in ISCs and tissue CC regeneration (PubMed:27292189). May participate in hair follicle CC morphogenesis by regulating phosphatidylethanolamines metabolism at the CC outermost epithelial layer and facilitating melanin synthesis CC (PubMed:21266583). By generating lysophosphatidylcholines (LPCs) at CC sperm acrosome controls sperm cell capacitation, acrosome reaction and CC overall fertility (PubMed:20424324, PubMed:21266581). May promote CC neurite outgrowth in neuron fibers involved in nociception CC (PubMed:21266581). 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:12359733). Displays bactericidal CC activity against Gram-positive bacteria by directly hydrolyzing CC phospholipids of the bacterial membrane (PubMed:11694541). In pulmonary CC epithelium, may contribute to host defense response against adenoviral CC infection. Prevents adenovirus entry into host cells by hydrolyzing CC host cell plasma membrane, releasing C16:0 LPCs that inhibit virus- CC mediated membrane fusion and viral infection. Likely prevents CC adenoviral entry into the endosomes of host cells (By similarity). May CC play a role in maturation and activation of innate immune cells CC including macrophages, group 2 innate lymphoid cells and mast cells CC (PubMed:29093264). {ECO:0000250|UniProtKB:O15496, CC ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11694541, CC ECO:0000269|PubMed:12359733, ECO:0000269|PubMed:17403936, CC ECO:0000269|PubMed:20424324, ECO:0000269|PubMed:21266581, CC ECO:0000269|PubMed:21266583, ECO:0000269|PubMed:27292189, CC ECO:0000269|PubMed:29093264}. 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:10531313, CC ECO:0000269|PubMed:12359733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000305|PubMed:10531313, ECO:0000305|PubMed:12359733}; 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:O15496}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; CC Evidence={ECO:0000250|UniProtKB:O15496}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC octadecanoyl-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; CC Evidence={ECO:0000269|PubMed:12359733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; CC Evidence={ECO:0000305|PubMed:12359733}; 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:10531313, ECO:0000269|PubMed:12359733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; CC Evidence={ECO:0000305|PubMed:10531313, ECO:0000305|PubMed:12359733}; 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:12359733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525; CC Evidence={ECO:0000305|PubMed:12359733}; 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:10531313}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473; CC Evidence={ECO:0000305|PubMed:10531313}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L- CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020, CC ChEBI:CHEBI:75029; Evidence={ECO:0000269|PubMed:12359733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753; CC Evidence={ECO:0000305|PubMed:12359733}; 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:12359733, ECO:0000269|PubMed:21266583}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; CC Evidence={ECO:0000305|PubMed:12359733, ECO:0000305|PubMed:21266583}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CC H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphate + CC H(+); Xref=Rhea:RHEA:63996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839; CC Evidence={ECO:0000250|UniProtKB:O15496}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63997; CC Evidence={ECO:0000250|UniProtKB:O15496}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; CC Evidence={ECO:0000250|UniProtKB:O15496}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; CC Evidence={ECO:0000250|UniProtKB:O15496}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:O15496}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O15496}; CC -!- SUBUNIT: Interacts with PLA2R1; this interaction mediates PLA2G10 CC clearance and inactivation. {ECO:0000269|PubMed:11019817, CC ECO:0000269|PubMed:11741598}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10531313, CC ECO:0000269|PubMed:11741598, ECO:0000269|PubMed:20424324}. Lysosome CC {ECO:0000269|PubMed:11741598}. Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000269|PubMed:20424324}. CC -!- TISSUE SPECIFICITY: Expressed at high levels in testis and the CC gastrointestinal tract including stomach and colon. Expressed at lower CC levels in other tissues including small intestine, uterus, oviduct, CC lung, thymus, spleen and brain (PubMed:11019817, PubMed:21266581). CC Expressed in Paneth-like secretory epithelial cells of the colon CC (PubMed:27292189). Expressed in gastric and ileac epithelial cells and CC in glandular epithelium of intestinal mucosa (at protein level) CC (PubMed:21266581). Expressed in late spermatogenic cells, spermatocytes CC and spermatids, but not spermatogonia in seminiferous tubules (at CC protein level) (PubMed:20424324). Expressed mainly in the apical side CC of endometrial epithelial cells and in the interstitium beneath the CC epithelium of uterus (at protein level) (PubMed:21266581). Expressed in CC resident spleen macrophages (at protein level) (PubMed:11019817). CC Expressed at outermost layer of hair follicles (PubMed:21266583). CC Expressed in dorsal root ganglia in both NEFH-positive A-fibers and CC PRPH-positive C-fibers (at protein level) (PubMed:21266581). CC {ECO:0000269|PubMed:11019817, ECO:0000269|PubMed:20424324, CC ECO:0000269|PubMed:21266581, ECO:0000269|PubMed:21266583, CC ECO:0000269|PubMed:27292189}. CC -!- DEVELOPMENTAL STAGE: During hair follicle growth cycle, it is detected CC at low levels at 17.5 dpc (hair folliculogenesis stage), increases to a CC maximum expression level by P10 (anagen), declines to the basal level CC at P15-20 (catagen to telogen), and again increases at P25 (re-entry CC into the next anagen). {ECO:0000269|PubMed:21266583}. CC -!- INDUCTION: Up-regulated in alveolar macrophages upon allergen-induced CC airway inflammation (PubMed:17403936). Up-regulated in bronchoalveolar CC lavage fluid (BALF) in response to house dust mite proteolytic CC allergens (PubMed:29093264). {ECO:0000269|PubMed:17403936, CC ECO:0000269|PubMed:29093264}. CC -!- DISRUPTION PHENOTYPE: Mutant male mice have reduced fertility due to CC deficient acrosome reaction (PubMed:20424324). Mutant mice are lean and CC protected from age-related adiposity and fatty liver (PubMed:21266581). CC Mutant mice show resistance to allergen-induced asthma, with marked CC reduction of inflammatory cell recruitment in the lungs, reduced goblet CC cell metaplasia, smooth muscle cell layer thickening and subepithelial CC fibrosis and impaired mucus hypersecretion. This resistance to CC allergen-induced inflammation is associated with deficient T helper CC type 2 immune response and decreased eicosanoid synthesis CC (PubMed:17403936). Mutant mice are protected against airway allergic CC inflammation induced by house dust mite allergens (PubMed:29093264). CC Mutant mice show hair shaft abnormalities including hypoplastic outer CC root sheath and reduced number of melanin granules (PubMed:21266583). CC {ECO:0000269|PubMed:17403936, ECO:0000269|PubMed:20424324, CC ECO:0000269|PubMed:21266581, ECO:0000269|PubMed:21266583, CC ECO:0000269|PubMed:29093264}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF166097; AAF04498.2; -; mRNA. DR EMBL; AF210429; AAG43522.1; -; mRNA. DR CCDS; CCDS27967.1; -. DR RefSeq; NP_036117.1; NM_011987.4. DR AlphaFoldDB; Q9QXX3; -. DR SMR; Q9QXX3; -. DR STRING; 10090.ENSMUSP00000023364; -. DR BindingDB; Q9QXX3; -. DR ChEMBL; CHEMBL4200; -. DR PaxDb; 10090-ENSMUSP00000023364; -. DR ProteomicsDB; 295452; -. DR Antibodypedia; 24881; 104 antibodies from 16 providers. DR DNASU; 26565; -. DR Ensembl; ENSMUST00000023364.7; ENSMUSP00000023364.7; ENSMUSG00000022683.14. DR GeneID; 26565; -. DR KEGG; mmu:26565; -. DR UCSC; uc007ygh.2; mouse. DR AGR; MGI:1347522; -. DR CTD; 8399; -. DR MGI; MGI:1347522; Pla2g10. DR VEuPathDB; HostDB:ENSMUSG00000022683; -. DR eggNOG; KOG4087; Eukaryota. DR GeneTree; ENSGT00940000157803; -. DR HOGENOM; CLU_090683_3_1_1; -. DR InParanoid; Q9QXX3; -. DR OMA; WECEDNA; -. DR OrthoDB; 638584at2759; -. DR PhylomeDB; Q9QXX3; -. DR TreeFam; TF319283; -. 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 BioGRID-ORCS; 26565; 3 hits in 79 CRISPR screens. DR PRO; PR:Q9QXX3; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q9QXX3; Protein. DR Bgee; ENSMUSG00000022683; Expressed in epithelium of stomach and 61 other cell types or tissues. DR ExpressionAtlas; Q9QXX3; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0004623; F:phospholipase A2 activity; ISO:MGI. DR GO; GO:0004620; F:phospholipase activity; IMP:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0007411; P:axon guidance; ISO:MGI. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL. DR GO; GO:0051607; P:defense response to virus; ISO:MGI. DR GO; GO:0043249; P:erythrocyte maturation; IMP:MGI. DR GO; GO:0009566; P:fertilization; IMP:MGI. DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB. DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:UniProtKB. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:MGI. DR GO; GO:0051977; P:lysophospholipid transport; ISO:MGI. DR GO; GO:0042116; P:macrophage activation; IDA:MGI. DR GO; GO:0090370; P:negative regulation of cholesterol efflux; IDA:BHF-UCL. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:MGI. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL. DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI. DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:UniProtKB. DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISO:MGI. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB. DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IDA:UniProtKB. DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IDA:UniProtKB. DR GO; GO:0006658; P:phosphatidylserine metabolic process; IDA:UniProtKB. DR GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI. DR GO; GO:0062234; P:platelet activating factor catabolic process; ISS:UniProtKB. DR GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:UniProtKB. DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:BHF-UCL. DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:MGI. DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:MGI. DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI. DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IDA:MGI. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB. DR GO; GO:0043030; P:regulation of macrophage activation; ISO: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:SF4; GROUP 10 SECRETORY PHOSPHOLIPASE A2; 1. DR PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 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. DR Genevisible; Q9QXX3; MM. PE 1: Evidence at protein level; KW Calcium; Cleavage on pair of basic residues; Cytoplasmic vesicle; KW Direct protein sequencing; Disulfide bond; Hydrolase; Lipid metabolism; KW Lysosome; Metal-binding; Phospholipid metabolism; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000269|PubMed:11019817" FT PROPEP 18..28 FT /evidence="ECO:0000269|PubMed:11019817" FT /id="PRO_0000022766" FT CHAIN 29..151 FT /note="Group 10 secretory phospholipase A2" FT /id="PRO_0000022767" FT ACT_SITE 74 FT /evidence="ECO:0000250|UniProtKB:O15496" FT ACT_SITE 119 FT /evidence="ECO:0000250|UniProtKB:O15496" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O15496" FT BINDING 58 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O15496" FT BINDING 75 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 39..97 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 53..143 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 55..71 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 70..125 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 76..150 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 77..118 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 86..111 FT /evidence="ECO:0000250|UniProtKB:O15496" FT DISULFID 104..116 FT /evidence="ECO:0000250|UniProtKB:O15496" FT MUTAGEN 74 FT /note="H->Q: Impaired acrosome reaction." FT /evidence="ECO:0000269|PubMed:20424324" FT CONFLICT 151 FT /note="N -> D (in Ref. 2; AAG43522)" FT /evidence="ECO:0000305" SQ SEQUENCE 151 AA; 17005 MW; 05D15E70BC2C9294 CRC64; MLLLLLLLLL GPGPGFSEAT RRSHVYKRGL LELAGTLDCV GPRSPMAYMN YGCYCGLGGH GEPRDAIDWC CYHHDCCYSR AQDAGCSPKL DRYPWKCMDH HILCGPAENK CQELLCRCDE ELAYCLAGTE YHLKYLFFPS ILCEKDSPKC N //