ID S4R2K6_MOUSE Unreviewed; 77 AA. AC S4R2K6; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 05-DEC-2018, entry version 39. DE RecName: Full=Phospholipase A(2) {ECO:0000256|RuleBase:RU361236}; DE EC=3.1.1.4 {ECO:0000256|RuleBase:RU361236}; GN Name=Pla2g1b {ECO:0000313|Ensembl:ENSMUSP00000138683, GN ECO:0000313|MGI:MGI:101842}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000138683, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000138683, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000138683, 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000138683} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000138683}; RG Ensembl; RL Submitted (JUL-2013) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1- CC acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); CC Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; CC EC=3.1.1.4; Evidence={ECO:0000256|RuleBase:RU361236}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361236}; CC Note=Binds 1 Ca(2+) ion per subunit. CC {ECO:0000256|RuleBase:RU361236}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361236, CC ECO:0000256|SAAS:SAAS00331951}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. CC {ECO:0000256|RuleBase:RU003654, ECO:0000256|SAAS:SAAS00587348}. 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; AC117735; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; S4R2K6; -. DR SMR; S4R2K6; -. DR PRIDE; S4R2K6; -. DR Ensembl; ENSMUST00000145785; ENSMUSP00000138683; ENSMUSG00000029522. DR MGI; MGI:101842; Pla2g1b. DR GeneTree; ENSGT00940000154885; -. DR ChiTaRS; Pla2g1b; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000029522; Expressed in 39 organ(s), highest expression level in stomach. 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:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC. DR GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); 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; -; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR016090; PLipase_A2_dom. DR InterPro; IPR036444; PLipase_A2_dom_sf. 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. PE 1: Evidence at protein level; KW Calcium {ECO:0000256|RuleBase:RU361236}; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00479786}; KW Hydrolase {ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Proteomics identification {ECO:0000213|MaxQB:S4R2K6}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Secreted {ECO:0000256|RuleBase:RU361236, KW ECO:0000256|SAAS:SAAS00479782}; KW Signal {ECO:0000256|RuleBase:RU361236}. FT SIGNAL 1 16 {ECO:0000256|RuleBase:RU361236}. FT CHAIN 17 77 Phospholipase A(2). FT {ECO:0000256|RuleBase:RU361236}. FT /FTId=PRO_5001391206. FT DOMAIN 23 76 PA2c. {ECO:0000259|SMART:SM00085}. SQ SEQUENCE 77 AA; 8434 MW; 944A1A198C1CE820 CRC64; MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY CGLGGWGTPV DDLDSQKQQM RGLHLQL //