ID S4R2K6_MOUSE Unreviewed; 77 AA. AC S4R2K6; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 27-MAY-2015, entry version 15. 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; Sciurognathi; 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: Phosphatidylcholine + H(2)O = 1- CC acylglycerophosphocholine + a carboxylate. CC {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 -!- SIMILARITY: Belongs to the phospholipase A2 family. CC {ECO:0000256|RuleBase:RU003654}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMUSP00000138683}. 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; 19-64. DR Ensembl; ENSMUST00000145785; ENSMUSP00000138683; ENSMUSG00000029522. DR MGI; MGI:101842; Pla2g1b. DR GeneTree; ENSGT00760000119160; -. DR ChiTaRS; Pla2g1b; mouse. DR Proteomes; UP000000589; Chromosome 5. DR ExpressionAtlas; S4R2K6; baseline and differential. 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:0005509; F:calcium ion binding; ISO:MGI. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISO:MGI. DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI. DR GO; GO:0005102; F:receptor binding; IDA:MGI. DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI. 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:0044240; P:multicellular organismal lipid catabolic process; ISO:MGI. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:MGI. DR GO; GO:0009395; P:phospholipid catabolic process; TAS:MGI. DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI. DR Gene3D; 1.20.90.10; -; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR016090; PLipase_A2_dom. 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:SAAS00122668}; 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:SAAS00122677}; KW Signal {ECO:0000256|RuleBase:RU361236}. FT SIGNAL 1 16 {ECO:0000256|RuleBase:RU361236}. FT CHAIN 17 77 {ECO:0000256|RuleBase:RU361236}. FT /FTId=PRO_5001391206. SQ SEQUENCE 77 AA; 8434 MW; 944A1A198C1CE820 CRC64; MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY CGLGGWGTPV DDLDSQKQQM RGLHLQL //