ID E1BLF3_BOVIN Unreviewed; 144 AA. AC E1BLF3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 12-SEP-2018, entry version 57. DE RecName: Full=Phospholipase A(2) {ECO:0000256|RuleBase:RU361236}; DE EC=3.1.1.4 {ECO:0000256|RuleBase:RU361236}; GN Name=LOC615045 {ECO:0000313|Ensembl:ENSBTAP00000017333}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017333, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017333, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000017333} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333}; RG Ensembl; RL Submitted (MAR-2016) 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 ECO:0000256|SAAS:SAAS00614830}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. CC {ECO:0000256|RuleBase:RU003654, ECO:0000256|SAAS:SAAS00534670}. 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; DAAA02006512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002685775.1; XM_002685729.2. DR RefSeq; XP_871834.1; XM_866741.3. DR UniGene; Bt.87224; -. DR STRING; 9913.ENSBTAP00000017333; -. DR PaxDb; E1BLF3; -. DR Ensembl; ENSBTAT00000017333; ENSBTAP00000017333; ENSBTAG00000013039. DR GeneID; 615045; -. DR KEGG; bta:615045; -. DR eggNOG; KOG4087; Eukaryota. DR eggNOG; ENOG411283D; LUCA. DR GeneTree; ENSGT00760000119160; -. DR InParanoid; E1BLF3; -. DR KO; K01047; -. DR OMA; MIKFTTG; -. DR OrthoDB; EOG091G0UZ3; -. DR TreeFam; TF319283; -. DR Reactome; R-BTA-1482788; Acyl chain remodelling of PC. DR Reactome; R-BTA-1482801; Acyl chain remodelling of PS. DR Reactome; R-BTA-1482839; Acyl chain remodelling of PE. DR Reactome; R-BTA-1482922; Acyl chain remodelling of PI. DR Reactome; R-BTA-1482925; Acyl chain remodelling of PG. DR Reactome; R-BTA-1483166; Synthesis of PA. DR Reactome; R-BTA-6803157; Antimicrobial peptides. DR Proteomes; UP000009136; Chromosome 2. DR Bgee; ENSBTAG00000013039; Expressed in 1 organ(s), highest expression level in colon. 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 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 3: Inferred from homology; KW Calcium {ECO:0000256|RuleBase:RU361236}; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00479786}; KW Hydrolase {ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Secreted {ECO:0000256|RuleBase:RU361236, KW ECO:0000256|SAAS:SAAS00614840}; KW Signal {ECO:0000256|RuleBase:RU361236}. FT SIGNAL 1 23 {ECO:0000256|RuleBase:RU361236}. FT CHAIN 24 144 Phospholipase A(2). FT {ECO:0000256|RuleBase:RU361236}. FT /FTId=PRO_5001390411. FT DOMAIN 21 138 PA2c. {ECO:0000259|SMART:SM00085}. SQ SEQUENCE 144 AA; 16346 MW; 37B45626AFF667F5 CRC64; MKTLLLLAVI MAIGLLQVHG GLADFQKMIK FTTGKEPAIS YGFYGCHCGA GHRGTPKDAT DWCCRVHDCC YENLRKRGCR TSSQSYNFIF QRGQIVCGDQ DYCKRRLCQC DKRAADCLDK NLKTYNKNLQ YYNNLLCFGS TPKC //