PA2GX_HUMAN
ID PA2GX_HUMAN Reviewed; 165 AA.
AC O15496; Q14DU3; Q6NT23;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Group 10 secretory phospholipase A2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:12021277};
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9188469; DOI=10.1074/jbc.272.25.15745;
RA Cupillard L., Koumanov K., Mattei M.-G., Lazdunski M., Lambeau G.;
RT "Cloning, chromosomal mapping, and expression of a novel human secretory
RT phospholipase A2.";
RL J. Biol. Chem. 272:15745-15752(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12021277; DOI=10.1074/jbc.m202867200;
RA Hanasaki K., Yamada K., Yamamoto S., Ishimoto Y., Saiga A., Ono T.,
RA Ikeda M., Notoya M., Kamitani S., Arita H.;
RT "Potent modification of low density lipoprotein by group X secretory
RT phospholipase A2 is linked to macrophage foam cell formation.";
RL J. Biol. Chem. 277:29116-29124(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-88.
RX PubMed=16962371; DOI=10.1016/j.bbalip.2006.08.004;
RA Gora S., Lambeau G., Bollinger J.G., Gelb M., Ninio E., Karabina S.A.;
RT "The proinflammatory mediator Platelet Activating Factor is an effective
RT substrate for human group X secreted phospholipase A2.";
RL Biochim. Biophys. Acta 1761:1093-1099(2006).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-88.
RX PubMed=16146426; DOI=10.1042/bj20050781;
RA Mitsuishi M., Masuda S., Kudo I., Murakami M.;
RT "Group V and X secretory phospholipase A2 prevents adenoviral infection in
RT mammalian cells.";
RL Biochem. J. 393:97-106(2006).
RN [11]
RP TISSUE SPECIFICITY.
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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 43-165, DISULFIDE BONDS, ACTIVE
RP SITE, COFACTOR, AND CALCIUM-BINDING SITES.
RX PubMed=12161451; DOI=10.1074/jbc.m202531200;
RA Pan Y.H., Yu B.Z., Singer A.G., Ghomashchi F., Lambeau G., Gelb M.H.,
RA Jain M.K., Bahnson B.J.;
RT "Crystal structure of human group X secreted phospholipase A2.
RT Electrostatically neutral interfacial surface targets zwitterionic
RT membranes.";
RL J. Biol. Chem. 277:29086-29093(2002).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids (PubMed:9188469, PubMed:12021277).
CC Hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC position of phospholipids with preference for phosphatidylcholines and
CC phosphatidylglycerols over phosphatidylethanolamines. Preferentially
CC releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA)
CC chains over saturated fatty acyls (PubMed:12359733, PubMed:12021277).
CC Contributes to phospholipid remodeling of very low-density lipoprotein
CC (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein
CC (HDL) particles (PubMed:12021277). Hydrolyzes LDL phospholipids
CC releasing unsaturated fatty acids that regulate macrophage
CC differentiation toward foam cells (PubMed:12021277). Efficiently
CC hydrolyzes and inactivates platelet activating factor (PAF), a potent
CC lipid mediator present in oxidized LDL (PubMed:16962371). 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 (By similarity).
CC Secreted by gut epithelium, hydrolyzes dietary and biliary
CC phosphatidylcholines in the gastrointestinal lumen (By similarity).
CC Plays a stem cell regulator role in colon epithelium. Within
CC intracellular compartment, mediates Paneth-like cell differentiation
CC and its stem cell supporting functions by inhibiting the Wnt signaling
CC pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen
CC upon inflammation, acts in an autocrine way and promotes prostaglandin
CC E2 synthesis that stimulates Wnt signaling pathway in ISCs and tissue
CC regeneration (By similarity). May participate in hair follicle
CC morphogenesis by regulating phosphatidylethanolamines metabolism at the
CC outermost epithelial layer and facilitating melanin synthesis (By
CC similarity). By releasing lysophosphatidylcholines (LPCs) at sperm
CC acrosome, controls sperm cell capacitation, acrosome reaction and
CC overall fertility (By similarity). May promote neurite outgrowth in
CC neuron fibers involved in nociception (By similarity). Contributes to
CC lipid remodeling of cellular membranes and generation of lipid
CC mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl
CC chains of phosphatidylglycerols and phosphatidylethanolamines, which
CC are major components of membrane phospholipids in bacteria
CC (PubMed:12359733). Displays bactericidal activity against Gram-positive
CC bacteria by directly hydrolyzing phospholipids of the bacterial
CC membrane (PubMed:11694541). In pulmonary epithelium, may contribute to
CC host defense response against adenoviral infection. Prevents adenovirus
CC entry into host cells by hydrolyzing host cell plasma membrane,
CC releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and
CC viral infection. Likely prevents adenoviral entry into the endosomes of
CC host cells (PubMed:16146426). May play a role in maturation and
CC activation of innate immune cells including macrophages, group 2 innate
CC lymphoid cells and mast cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXX3, ECO:0000269|PubMed:11694541,
CC ECO:0000269|PubMed:12021277, ECO:0000269|PubMed:12359733,
CC ECO:0000269|PubMed:16146426, ECO:0000269|PubMed:16962371,
CC ECO:0000269|PubMed:9188469}.
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:12021277};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:12021277};
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:12359733,
CC ECO:0000269|PubMed:16962371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:12359733, ECO:0000305|PubMed:16962371};
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:12359733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={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:0000250|UniProtKB:Q9QXX3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000250|UniProtKB:Q9QXX3};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:12359733};
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:0000269|PubMed:12359733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63997;
CC Evidence={ECO:0000305|PubMed:12359733};
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:0000269|PubMed:16962371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000305|PubMed:16962371};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12161451, ECO:0000269|PubMed:9188469};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12161451};
CC -!- ACTIVITY REGULATION: Inhibited by methyl indoxam.
CC {ECO:0000269|PubMed:12359733}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:9188469};
CC -!- SUBUNIT: Interacts with PLA2R1; this interaction mediates PLA2G10
CC clearance and inactivation. {ECO:0000250|UniProtKB:Q9QXX3}.
CC -!- INTERACTION:
CC O15496; P21549: AGXT; NbExp=3; IntAct=EBI-726466, EBI-727098;
CC O15496; P29972: AQP1; NbExp=3; IntAct=EBI-726466, EBI-745213;
CC O15496; Q03989: ARID5A; NbExp=3; IntAct=EBI-726466, EBI-948603;
CC O15496; P54253: ATXN1; NbExp=3; IntAct=EBI-726466, EBI-930964;
CC O15496; O95817: BAG3; NbExp=3; IntAct=EBI-726466, EBI-747185;
CC O15496; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-726466, EBI-745073;
CC O15496; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-726466, EBI-946029;
CC O15496; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-726466, EBI-744545;
CC O15496; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-726466, EBI-744556;
CC O15496; Q02930-3: CREB5; NbExp=3; IntAct=EBI-726466, EBI-10192698;
CC O15496; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-726466, EBI-3867333;
CC O15496; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-726466, EBI-2807642;
CC O15496; O75593: FOXH1; NbExp=3; IntAct=EBI-726466, EBI-1759806;
CC O15496; Q9BWX5: GATA5; NbExp=3; IntAct=EBI-726466, EBI-12132270;
CC O15496; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-726466, EBI-11975289;
CC O15496; O14964: HGS; NbExp=3; IntAct=EBI-726466, EBI-740220;
CC O15496; P31273: HOXC8; NbExp=3; IntAct=EBI-726466, EBI-1752118;
CC O15496; O43593: HR; NbExp=3; IntAct=EBI-726466, EBI-2880706;
CC O15496; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-726466, EBI-12056251;
CC O15496; Q0VD86: INCA1; NbExp=3; IntAct=EBI-726466, EBI-6509505;
CC O15496; Q5T749: KPRP; NbExp=3; IntAct=EBI-726466, EBI-10981970;
CC O15496; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-726466, EBI-1052037;
CC O15496; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-726466, EBI-3957672;
CC O15496; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-726466, EBI-11962058;
CC O15496; Q5T751: LCE1C; NbExp=3; IntAct=EBI-726466, EBI-12224199;
CC O15496; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-726466, EBI-10246607;
CC O15496; O14633: LCE2B; NbExp=4; IntAct=EBI-726466, EBI-11478468;
CC O15496; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-726466, EBI-10246750;
CC O15496; P21145: MAL; NbExp=3; IntAct=EBI-726466, EBI-3932027;
CC O15496; O60336: MAPKBP1; NbExp=3; IntAct=EBI-726466, EBI-947402;
CC O15496; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-726466, EBI-12025760;
CC O15496; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-726466, EBI-741158;
CC O15496; P32242: OTX1; NbExp=3; IntAct=EBI-726466, EBI-740446;
CC O15496; P78337: PITX1; NbExp=3; IntAct=EBI-726466, EBI-748265;
CC O15496; Q15319: POU4F3; NbExp=3; IntAct=EBI-726466, EBI-12033574;
CC O15496; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-726466, EBI-12000762;
CC O15496; Q01974: ROR2; NbExp=3; IntAct=EBI-726466, EBI-6422642;
CC O15496; P09234: SNRPC; NbExp=3; IntAct=EBI-726466, EBI-766589;
CC O15496; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-726466, EBI-11959123;
CC O15496; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-726466, EBI-5235340;
CC O15496; O75716: STK16; NbExp=3; IntAct=EBI-726466, EBI-749295;
CC O15496; O95947: TBX6; NbExp=3; IntAct=EBI-726466, EBI-2824328;
CC O15496; Q92734: TFG; NbExp=3; IntAct=EBI-726466, EBI-357061;
CC O15496; O43711: TLX3; NbExp=3; IntAct=EBI-726466, EBI-3939165;
CC O15496; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-726466, EBI-11957216;
CC O15496; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-726466, EBI-2559305;
CC O15496; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-726466, EBI-742550;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9188469}. Lysosome
CC {ECO:0000250|UniProtKB:Q9QXX3}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q9QXX3}.
CC -!- TISSUE SPECIFICITY: Found in spleen, thymus, peripheral blood
CC leukocytes, pancreas, lung, and colon (PubMed:9188469). Expressed in
CC neuronal fibers in dorsal root ganglia and in peripheral tissues
CC including stomach, white adipose tissue and prostate (at protein level)
CC (PubMed:21266581). {ECO:0000269|PubMed:21266581,
CC ECO:0000269|PubMed:9188469}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; U95301; AAB64410.1; -; mRNA.
DR EMBL; CR456885; CAG33166.1; -; mRNA.
DR EMBL; AC009167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85104.1; -; Genomic_DNA.
DR EMBL; BC069539; AAH69539.1; -; mRNA.
DR EMBL; BC106731; AAI06732.1; -; mRNA.
DR EMBL; BC106732; AAI06733.1; -; mRNA.
DR EMBL; BC111804; AAI11805.1; -; mRNA.
DR CCDS; CCDS10555.1; -.
DR RefSeq; NP_003552.1; NM_003561.2.
DR PDB; 1LE6; X-ray; 1.97 A; A/B/C=43-165.
DR PDB; 1LE7; X-ray; 2.09 A; A/B=43-165.
DR PDB; 4UY1; X-ray; 2.20 A; A/B=43-165.
DR PDB; 5G3M; X-ray; 1.85 A; A/B=43-165.
DR PDB; 5OW8; X-ray; 1.90 A; A/B=43-165.
DR PDB; 5OWC; X-ray; 1.75 A; A/B=43-164.
DR PDB; 6G5J; X-ray; 1.85 A; A/B=1-165.
DR PDBsum; 1LE6; -.
DR PDBsum; 1LE7; -.
DR PDBsum; 4UY1; -.
DR PDBsum; 5G3M; -.
DR PDBsum; 5OW8; -.
DR PDBsum; 5OWC; -.
DR PDBsum; 6G5J; -.
DR AlphaFoldDB; O15496; -.
DR SMR; O15496; -.
DR BioGRID; 113987; 151.
DR IntAct; O15496; 99.
DR STRING; 9606.ENSP00000393847; -.
DR BindingDB; O15496; -.
DR ChEMBL; CHEMBL4342; -.
DR DrugBank; DB13894; Agkistrodon piscivorus antivenin.
DR DrugBank; DB13893; Crotalus adamanteus antivenin.
DR DrugBank; DB13892; Crotalus atrox antivenin.
DR DrugBank; DB05737; Varespladib methyl.
DR GuidetoPHARMACOLOGY; 1422; -.
DR SwissLipids; SLP:000001084; -.
DR GlyGen; O15496; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O15496; -.
DR BioMuta; PLA2G10; -.
DR jPOST; O15496; -.
DR MassIVE; O15496; -.
DR PaxDb; O15496; -.
DR PeptideAtlas; O15496; -.
DR PRIDE; O15496; -.
DR ProteomicsDB; 48696; -.
DR Antibodypedia; 24881; 84 antibodies from 16 providers.
DR DNASU; 8399; -.
DR Ensembl; ENST00000438167.8; ENSP00000393847.4; ENSG00000069764.10.
DR Ensembl; ENST00000621727.2; ENSP00000479397.1; ENSG00000276870.2.
DR GeneID; 8399; -.
DR KEGG; hsa:8399; -.
DR MANE-Select; ENST00000438167.8; ENSP00000393847.4; NM_003561.3; NP_003552.1.
DR UCSC; uc002dcq.4; human.
DR CTD; 8399; -.
DR DisGeNET; 8399; -.
DR GeneCards; PLA2G10; -.
DR HGNC; HGNC:9029; PLA2G10.
DR HPA; ENSG00000069764; Group enriched (intestine, pancreas, stomach).
DR MIM; 603603; gene.
DR neXtProt; NX_O15496; -.
DR OpenTargets; ENSG00000069764; -.
DR PharmGKB; PA33360; -.
DR VEuPathDB; HostDB:ENSG00000069764; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000157803; -.
DR HOGENOM; CLU_090683_3_1_1; -.
DR InParanoid; O15496; -.
DR OMA; CERDSPK; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; O15496; -.
DR TreeFam; TF319283; -.
DR BRENDA; 3.1.1.4; 2681.
DR PathwayCommons; O15496; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; O15496; -.
DR BioGRID-ORCS; 8399; 463 hits in 1067 CRISPR screens.
DR ChiTaRS; PLA2G10; human.
DR EvolutionaryTrace; O15496; -.
DR GeneWiki; PLA2G10; -.
DR GenomeRNAi; 8399; -.
DR Pharos; O15496; Tchem.
DR PRO; PR:O15496; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O15496; protein.
DR Bgee; ENSG00000069764; Expressed in mucosa of transverse colon and 90 other tissues.
DR ExpressionAtlas; O15496; baseline and differential.
DR Genevisible; O15496; HS.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA: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; TAS:ProtInc.
DR GO; GO:0004620; F:phospholipase activity; ISS:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; NAS:BHF-UCL.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0051977; P:lysophospholipid transport; IDA:MGI.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0090370; P:negative regulation of cholesterol efflux; ISS:BHF-UCL.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0062234; P:platelet activating factor catabolic process; IDA:UniProtKB.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:UniProtKB.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; ISS:BHF-UCL.
DR GO; GO:0010884; P:positive regulation of lipid storage; IMP:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:BHF-UCL.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:BHF-UCL.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:Ensembl.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP:BHF-UCL.
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 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid metabolism; Lysosome; Metal-binding; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..42
FT /evidence="ECO:0000255"
FT /id="PRO_0000022764"
FT CHAIN 43..165
FT /note="Group 10 secretory phospholipase A2"
FT /id="PRO_0000022765"
FT ACT_SITE 88
FT /evidence="ECO:0000269|PubMed:12161451"
FT ACT_SITE 133
FT /evidence="ECO:0000269|PubMed:12161451"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12161451,
FT ECO:0007744|PDB:1LE6, ECO:0007744|PDB:1LE7"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12161451,
FT ECO:0007744|PDB:1LE6, ECO:0007744|PDB:1LE7"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12161451,
FT ECO:0007744|PDB:1LE6, ECO:0007744|PDB:1LE7"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12161451,
FT ECO:0007744|PDB:1LE6, ECO:0007744|PDB:1LE7"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..111
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 67..157
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 69..85
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 84..139
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 90..164
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 91..132
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 100..125
FT /evidence="ECO:0000269|PubMed:12161451"
FT DISULFID 118..130
FT /evidence="ECO:0000269|PubMed:12161451"
FT MUTAGEN 88
FT /note="H->Q: Loss of PLA2 activity toward PAF. Impairs
FT anti-adenoviral activity."
FT /evidence="ECO:0000269|PubMed:16146426,
FT ECO:0000269|PubMed:16962371"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:5OWC"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5OWC"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:5OWC"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5OWC"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5OWC"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5OWC"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:5OWC"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:5OWC"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:5OWC"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5OWC"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:5OWC"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5OWC"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:5OWC"
SQ SEQUENCE 165 AA; 18153 MW; AD197A164319F102 CRC64;
MGPLPVCLPI MLLLLLPSLL LLLLLPGPGS GEASRILRVH RRGILELAGT VGCVGPRTPI
AYMKYGCFCG LGGHGQPRDA IDWCCHGHDC CYTRAEEAGC SPKTERYSWQ CVNQSVLCGP
AENKCQELLC KCDQEIANCL AQTEYNLKYL FYPQFLCEPD SPKCD
