ID   D3YWH2_MOUSE            Unreviewed;       124 AA.
AC   D3YWH2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|ARBA:ARBA00021721};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
DE   AltName: Full=Group IB phospholipase A2 {ECO:0000256|ARBA:ARBA00042411};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B {ECO:0000256|ARBA:ARBA00041854};
DE   Flags: Fragment;
GN   Name=Pla2g1b {ECO:0000313|Ensembl:ENSMUSP00000120743.2,
GN   ECO:0000313|MGI:MGI:101842};
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 {ECO:0000313|Ensembl:ENSMUSP00000120743.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000120743.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000120743.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0000313|Ensembl:ENSMUSP00000120743.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000120743.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000120743.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000120743.2};
RG   Ensembl;
RL   Submitted (JUL-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H(+);
CC         Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000256|ARBA:ARBA00048227};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000256|ARBA:ARBA00048227};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         tetradecanoyl-sn-glycero-3-phosphocholine + tetradecanoate + H(+);
CC         Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489;
CC         Evidence={ECO:0000256|ARBA:ARBA00048029};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine +
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:40427,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC         Evidence={ECO:0000256|ARBA:ARBA00048373};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000256|ARBA:ARBA00048373};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3-
CC         phosphoethanolamine + (9Z,12Z)-octadecadienoate + 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:0000256|ARBA:ARBA00049039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000256|ARBA:ARBA00049039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC         sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-
CC         glycerol) + (9Z)-octadecenoate + 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:0000256|ARBA:ARBA00048015};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC         Evidence={ECO:0000256|ARBA:ARBA00048015};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + (9Z)-
CC         octadecenoate + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73001; Evidence={ECO:0000256|ARBA:ARBA00048699};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000256|ARBA:ARBA00048699};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = N,1-dihexadecanoyl-sn-glycero-3-
CC         phosphoethanolamine + (9Z,12Z)-octadecadienoate + H(+);
CC         Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335;
CC         Evidence={ECO:0000256|ARBA:ARBA00047535};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425;
CC         Evidence={ECO:0000256|ARBA:ARBA00047535};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-
CC         glycero-3-phosphoethanolamine + (9Z)-octadecenoate + H(+);
CC         Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC         Evidence={ECO:0000256|ARBA:ARBA00048221};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC         Evidence={ECO:0000256|ARBA:ARBA00048221};
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:0000256|PROSITE-ProRule:PRU10035};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601211-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR601211-2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
CC       {ECO:0000256|ARBA:ARBA00007056, ECO:0000256|RuleBase:RU003654}.
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DR   SMR; D3YWH2; -.
DR   ProteomicsDB; 316866; -.
DR   Ensembl; ENSMUST00000125568.2; ENSMUSP00000120743.2; ENSMUSG00000029522.14.
DR   VEuPathDB; HostDB:ENSMUSG00000029522; -.
DR   AGR; MGI:101842; -.
DR   MGI; MGI:101842; Pla2g1b.
DR   GeneTree; ENSGT00940000154885; -.
DR   HOGENOM; CLU_090683_4_0_1; -.
DR   Bgee; ENSMUSG00000029522; Expressed in epithelium of stomach and 47 other cell types or tissues.
DR   ExpressionAtlas; D3YWH2; baseline and differential.
DR   CDD; cd00125; PLA2c; 1.
DR   FunFam; 1.20.90.10:FF:000011; Phospholipase A(2); 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR   InterPro; IPR001211; PLA2.
DR   InterPro; IPR016090; PLA2-like_dom.
DR   InterPro; IPR033113; PLA2_histidine.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PANTHER; PTHR11716:SF94; 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; PS00118; PA2_HIS; 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:A2-type glycerophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Antibodypedia; 31466; 350 antibodies from 40 providers.
DR   AlphaFoldDB; D3YWH2; -.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601211-2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601211-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601211-2};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:D3YWH2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..124
FT                   /note="Phospholipase A2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012994388"
FT   DOMAIN          22..124
FT                   /note="Phospholipase A2-like central"
FT                   /evidence="ECO:0000259|SMART:SM00085"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10035"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-1"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        72..119
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        82..112
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        105..117
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   NON_TER         124
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000120743.2"
SQ   SEQUENCE   124 AA;  13739 MW;  108A443AB84C6AD2 CRC64;
     MKLLLLAALL TGAAAHSISP RAVWQFRNMI KCTIPGSDPL KDYNNYGCYC GLGGWGTPVD
     DLDRCCQTHD HCYSQAKKLE SCKFLIDNPY TNTYSYSCSG SEITCSAKNN KCEDFICNCD
     REAA
//