PA2GX_MOUSE
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 03-AUG-2022, entry version 164.
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-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: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; Q9QXX3; -.
DR PRIDE; Q9QXX3; -.
DR ProteomicsDB; 295452; -.
DR Antibodypedia; 24881; 84 antibodies from 16 providers.
DR DNASU; 26565; -.
DR Ensembl; ENSMUST00000023364; ENSMUSP00000023364; ENSMUSG00000022683.
DR GeneID; 26565; -.
DR KEGG; mmu:26565; -.
DR UCSC; uc007ygh.2; mouse.
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; CERDSPK; -.
DR OrthoDB; 1422829at2759; -.
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; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9QXX3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9QXX3; protein.
DR Bgee; ENSMUSG00000022683; Expressed in epithelium of stomach and 59 other tissues.
DR ExpressionAtlas; Q9QXX3; baseline and differential.
DR Genevisible; Q9QXX3; MM.
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; -; 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; 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
