ID E1BLF3_BOVIN Unreviewed; 144 AA. AC E1BLF3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-APR-2021, entry version 72. DE RecName: Full=Phospholipase A2 {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; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017333, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017333} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. RN [2] {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}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; 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:ARBA00001479}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; CC Evidence={ECO:0000256|ARBA:ARBA00001479}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1- CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + 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:ARBA00001804}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; CC Evidence={ECO:0000256|ARBA:ARBA00001804}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'- CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero- CC 3-phospho-(1'-sn-glycerol) + 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:ARBA00001855}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; CC Evidence={ECO:0000256|ARBA:ARBA00001855}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- CC phosphocholine + 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:ARBA00001126}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; CC Evidence={ECO:0000256|ARBA:ARBA00001126}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1- CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; 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:ARBA00001129}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; CC Evidence={ECO:0000256|ARBA:ARBA00001129}; 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|RuleBase:RU361236}; 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 RefSeq; XP_002685775.1; XM_002685729.2. DR RefSeq; XP_871834.1; XM_866741.3. DR SMR; E1BLF3; -. DR STRING; 9913.ENSBTAP00000017333; -. DR PaxDb; E1BLF3; -. DR Ensembl; ENSBTAT00000017333; ENSBTAP00000017333; ENSBTAG00000013039. DR GeneID; 615045; -. DR KEGG; bta:615045; -. DR eggNOG; KOG4087; Eukaryota. DR GeneTree; ENSGT00940000155096; -. DR HOGENOM; CLU_090683_3_0_1; -. DR InParanoid; E1BLF3; -. DR OMA; CQCDKAA; -. DR OrthoDB; 1422829at2759; -. DR TreeFam; TF319283; -. DR Proteomes; UP000009136; Chromosome 2. DR Bgee; ENSBTAG00000013039; Expressed in colon and 1 other tissue. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central. 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:0005543; F:phospholipid binding; IBA:GO_Central. 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; IBA:GO_Central. 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361236}; KW Signal {ECO:0000256|RuleBase:RU361236}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|RuleBase:RU361236" FT CHAIN 24..144 FT /note="Phospholipase A2" FT /evidence="ECO:0000256|RuleBase:RU361236" FT /id="PRO_5001390411" FT DOMAIN 21..138 FT /note="PA2c" FT /evidence="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 //