ID S4R2K6_MOUSE Unreviewed; 77 AA. AC S4R2K6; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 13-SEP-2023, entry version 59. DE RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU361236}; DE EC=3.1.1.4 {ECO:0000256|RuleBase:RU361236}; GN Name=Pla2g1b {ECO:0000313|Ensembl:ENSMUSP00000138683.2, 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:ENSMUSP00000138683.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000138683.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000138683.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; 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:0000313|Ensembl:ENSMUSP00000138683.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000138683.2}; RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. 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|RuleBase:RU361236}; 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 ECO:0000256|RuleBase:RU361236}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. CC {ECO:0000256|ARBA:ARBA00007056, ECO:0000256|RuleBase:RU003654}. 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 AlphaFoldDB; S4R2K6; -. DR SMR; S4R2K6; -. DR ProteomicsDB; 326747; -. DR Antibodypedia; 31466; 355 antibodies from 39 providers. DR Ensembl; ENSMUST00000145785.8; ENSMUSP00000138683.2; ENSMUSG00000029522.13. DR AGR; MGI:101842; -. DR MGI; MGI:101842; Pla2g1b. DR VEuPathDB; HostDB:ENSMUSG00000029522; -. DR GeneTree; ENSGT00940000154885; -. DR HOGENOM; CLU_2757084_0_0_1; -. DR ChiTaRS; Pla2g1b; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000029522; Expressed in epithelium of stomach and 45 other tissues. DR ExpressionAtlas; S4R2K6; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR016090; PLipase_A2_dom. 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. PE 1: Evidence at protein level; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601211-2}; KW Hydrolase {ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601211-2}; KW Proteomics identification {ECO:0007829|MaxQB:S4R2K6}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361236}; KW Signal {ECO:0000256|RuleBase:RU361236}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|RuleBase:RU361236" FT CHAIN 17..77 FT /note="Phospholipase A2" FT /evidence="ECO:0000256|RuleBase:RU361236" FT /id="PRO_5001391206" FT DOMAIN 23..76 FT /note="Phospholipase A2" FT /evidence="ECO:0000259|SMART:SM00085" FT BINDING 50 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT BINDING 52 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" SQ SEQUENCE 77 AA; 8434 MW; 944A1A198C1CE820 CRC64; MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY CGLGGWGTPV DDLDSQKQQM RGLHLQL //