PA21B_MOUSE
ID PA21B_MOUSE Reviewed; 146 AA.
AC Q9Z0Y2; A6H6K5; Q9D7E2; Q9D884;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055};
DE AltName: Full=Group IB phospholipase A2;
DE AltName: Full=PLA2-Ib;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE Flags: Precursor;
GN Name=Pla2g1b; Synonyms=Pla2;
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.
RC STRAIN=129/SvJ;
RA Mandal A.K., Zhang Z., Mukherjee A.B.;
RT "Isolation, characterization and chromosomal localization of mouse sPLA2-Ib
RT gene.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PLA2R1, AND TISSUE
RP SPECIFICITY.
RX PubMed=10066760; DOI=10.1074/jbc.274.11.7043;
RA Cupillard L., Mulherkar R., Gomez N., Kadam S., Valentin E., Lazdunski M.,
RA Lambeau G.;
RT "Both group IB and group IIA secreted phospholipases A2 are natural ligands
RT of the mouse 180-kDa M-type receptor.";
RL J. Biol. Chem. 274:7043-7051(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10689188; DOI=10.1016/s0378-1119(00)00006-8;
RA Richmond B.L., Hui D.Y.;
RT "Molecular structure and tissue-specific expression of the mouse pancreatic
RT phospholipase A2 gene.";
RL Gene 244:65-72(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvJ; TISSUE=Pancreas;
RA Mandal A.K., Zhang Z., Popescu N., Mukherjee A.B.;
RT "Role of sPLA2-I in colorectal tumorigenesis.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, Small intestine, Stomach, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=21908646; DOI=10.1194/jlr.m019463;
RA Hollie N.I., Hui D.Y.;
RT "Group 1B phospholipase A(2) deficiency protects against diet-induced
RT hyperlipidemia in mice.";
RL J. Lipid Res. 52:2005-2011(2011).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY IL4
RP AND IL13.
RX PubMed=29024642; DOI=10.1016/j.chom.2017.09.006;
RA Entwistle L.J., Pelly V.S., Coomes S.M., Kannan Y., Perez-Lloret J.,
RA Czieso S., Silva Dos Santos M., MacRae J.I., Collinson L., Sesay A.,
RA Nikolov N., Metidji A., Helmby H., Hui D.Y., Wilson M.S.;
RT "Epithelial-Cell-Derived Phospholipase A2 Group 1B Is an Endogenous
RT Anthelmintic.";
RL Cell Host Microbe 22:484-493(2017).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets dietary phospholipids in the intestinal tract (By similarity).
CC Hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC position of phospholipids (phospholipase A2 activity) with preference
CC for phosphatidylethanolamines and phosphatidylglycerols over
CC phosphatidylcholines (By similarity). May play a role in the
CC biosynthesis of N-acyl ethanolamines that regulate energy metabolism
CC and inflammation in the intestinal tract. Hydrolyzes N-acyl
CC phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines,
CC which are further cleaved by a lysophospholipase D to release N-acyl
CC ethanolamines (By similarity). May act in an autocrine and paracrine
CC manner (PubMed:10066760). Upon binding to the PLA2R1 receptor can
CC regulate podocyte survival and glomerular homeostasis (By similarity).
CC Has anti-helminth activity in a process regulated by gut microbiota
CC (PubMed:29024642). Upon helminth infection of intestinal epithelia,
CC directly affects phosphatidylethanolamine contents in the membrane of
CC helminth larvae, likely controlling an array of phospholipid-mediated
CC cellular processes such as membrane fusion and cell division while
CC providing for better immune recognition, ultimately reducing larvae
CC integrity and infectivity (PubMed:29024642).
CC {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055,
CC ECO:0000269|PubMed:10066760, ECO:0000269|PubMed:29024642}.
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:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055,
CC ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:P04054,
CC ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489;
CC Evidence={ECO:0000250|UniProtKB:P04054};
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:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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:P04054,
CC ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P04054,
CC ECO:0000250|UniProtKB:P04055};
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:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:P04054,
CC ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:P04054,
CC ECO:0000250|UniProtKB:P04055};
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:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) +
CC N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00593};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
CC -!- SUBUNIT: Monomer or homodimer (By similarity). Interacts with PLA2R1;
CC this interaction mediates intracellular signaling as well as clearance
CC of extracellular PLA2G1B via endocytotic pathway (PubMed:10066760).
CC {ECO:0000250|UniProtKB:P00592, ECO:0000269|PubMed:10066760}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}.
CC Note=Secreted from pancreatic acinar cells in its inactive form.
CC {ECO:0000250|UniProtKB:P04054}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, liver, lung and spleen
CC (PubMed:10066760). Expressed in EPCAM-positive intestinal epithelial
CC cell (at protein level) (PubMed:29024642).
CC {ECO:0000269|PubMed:10066760, ECO:0000269|PubMed:29024642}.
CC -!- INDUCTION: Up-regulated in EPCAM-positive intestinal epithelial cell
CC upon helminth infection (PubMed:29024642). Up-regulated in intestinal
CC epithelial organoids in response to stimulation with T-helper type 2
CC cytokines IL4 and IL13 (PubMed:29024642).
CC {ECO:0000269|PubMed:29024642}.
CC -!- PTM: Activated by trypsin cleavage in the duodenum. Can also be
CC activated by thrombin or autocatalytically.
CC {ECO:0000250|UniProtKB:P04054}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are susceptible to H. polygyrus and
CC N. brasiliensis infection, failing to expel larvae and retaining a
CC sustained infection (PubMed:29024642). In response to high fat diet,
CC mutant mice are resistant to hyperlipidemia associated with reduced
CC hepatic very low density lipoprotein production and increased
CC triglyceride-rich lipoprotein clearance (PubMed:21908646).
CC {ECO:0000269|PubMed:21908646, ECO:0000269|PubMed:29024642}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF094611; AAF02298.1; -; Genomic_DNA.
DR EMBL; AF097637; AAD19896.1; -; mRNA.
DR EMBL; AF162712; AAD45806.1; -; mRNA.
DR EMBL; AF187852; AAF44297.1; -; mRNA.
DR EMBL; AF094610; AAG27064.1; -; mRNA.
DR EMBL; AK028104; BAC25749.1; -; mRNA.
DR EMBL; AK028134; BAC25763.1; -; mRNA.
DR EMBL; AK008936; BAB25978.1; -; mRNA.
DR EMBL; AK007730; BAB25218.1; -; mRNA.
DR EMBL; AK007797; BAB25263.1; -; mRNA.
DR EMBL; AK008664; BAB25819.1; -; mRNA.
DR EMBL; AK008668; BAB25822.1; -; mRNA.
DR EMBL; AK008841; BAB25922.1; -; mRNA.
DR EMBL; AK008934; BAB25976.1; -; mRNA.
DR EMBL; AK008331; BAB25608.1; -; mRNA.
DR EMBL; AK009314; BAB26212.1; -; mRNA.
DR EMBL; BC145908; AAI45909.1; -; mRNA.
DR EMBL; BC145910; AAI45911.1; -; mRNA.
DR CCDS; CCDS19592.1; -.
DR RefSeq; NP_035237.1; NM_011107.1.
DR AlphaFoldDB; Q9Z0Y2; -.
DR SMR; Q9Z0Y2; -.
DR STRING; 10090.ENSMUSP00000031495; -.
DR BindingDB; Q9Z0Y2; -.
DR ChEMBL; CHEMBL4378; -.
DR MaxQB; Q9Z0Y2; -.
DR PaxDb; Q9Z0Y2; -.
DR PRIDE; Q9Z0Y2; -.
DR ProteomicsDB; 293995; -.
DR Antibodypedia; 31466; 335 antibodies from 39 providers.
DR DNASU; 18778; -.
DR Ensembl; ENSMUST00000031495; ENSMUSP00000031495; ENSMUSG00000029522.
DR GeneID; 18778; -.
DR KEGG; mmu:18778; -.
DR UCSC; uc008zdx.1; mouse.
DR CTD; 5319; -.
DR MGI; MGI:101842; Pla2g1b.
DR VEuPathDB; HostDB:ENSMUSG00000029522; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000154885; -.
DR HOGENOM; CLU_090683_1_1_1; -.
DR InParanoid; Q9Z0Y2; -.
DR OMA; ELDTCCQ; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9Z0Y2; -.
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; 18778; 7 hits in 76 CRISPR screens.
DR ChiTaRS; Pla2g1b; mouse.
DR PRO; PR:Q9Z0Y2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z0Y2; protein.
DR Bgee; ENSMUSG00000029522; Expressed in epithelium of stomach and 45 other tissues.
DR ExpressionAtlas; Q9Z0Y2; baseline and differential.
DR Genevisible; Q9Z0Y2; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; ISO:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:MGI.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; TAS:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISS:UniProtKB.
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 Autocatalytic cleavage; Calcium; Disulfide bond; Hydrolase;
KW Lipid metabolism; Metal-binding; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000250"
FT PROPEP 16..22
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000022741"
FT CHAIN 23..146
FT /note="Phospholipase A2"
FT /id="PRO_0000022742"
FT ACT_SITE 70
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT ACT_SITE 121
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 33..99
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 49..146
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 51..67
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 66..127
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 73..120
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 83..113
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 106..118
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT CONFLICT 52
FT /note="G -> S (in Ref. 6; BAB26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="T -> P (in Ref. 6; BAB26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..79
FT /note="KK -> EN (in Ref. 6; BAB26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="I -> R (in Ref. 6; BAB26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Y -> F (in Ref. 6; BAB26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> G (in Ref. 6; BAB26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="R -> S (in Ref. 6; BAB25608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16290 MW; 59500C68845B7C81 CRC64;
MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY CGLGGWGTPV
DDLDRCCQTH DHCYSQAKKL ESCKFLIDNP YTNTYSYSCS GSEITCSAKN NKCEDFICNC
DREAAICFSK VPYNKEYKNL DTGKFC
