ID E1BLF3_BOVIN Unreviewed; 117 AA. AC E1BLF3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 2. DT 29-MAY-2024, entry version 87. 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:ENSBTAP00000017333.6}; 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:ENSBTAP00000017333.6, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017333.6, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333.6, 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. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000017333.6} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333.6}; RG Ensembl; RL Submitted (FEB-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O CC = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) + CC hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829, CC ChEBI:CHEBI:75158; Evidence={ECO:0000256|ARBA:ARBA00036461}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473; CC Evidence={ECO:0000256|ARBA:ARBA00036461}; 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-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- CC glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)- CC docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:41231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:77016; CC Evidence={ECO:0000256|ARBA:ARBA00036719}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232; CC Evidence={ECO:0000256|ARBA:ARBA00036719}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; CC Evidence={ECO:0000256|ARBA:ARBA00036113}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; CC Evidence={ECO:0000256|ARBA:ARBA00036113}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn- CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; CC Evidence={ECO:0000256|ARBA:ARBA00023408}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; CC Evidence={ECO:0000256|ARBA:ARBA00023408}; 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=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn- CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; CC Evidence={ECO:0000256|ARBA:ARBA00023391}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; CC Evidence={ECO:0000256|ARBA:ARBA00023391}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn- CC glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:44524, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; CC Evidence={ECO:0000256|ARBA:ARBA00043731}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525; CC Evidence={ECO:0000256|ARBA:ARBA00043731}; 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 -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1- CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; CC Evidence={ECO:0000256|ARBA:ARBA00036775}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605; CC Evidence={ECO:0000256|ARBA:ARBA00036775}; 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: Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004450}. Secreted CC {ECO:0000256|ARBA:ARBA00004613, 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 AlphaFoldDB; E1BLF3; -. DR SMR; E1BLF3; -. DR STRING; 9913.ENSBTAP00000017333; -. DR PaxDb; 9913-ENSBTAP00000017333; -. DR Ensembl; ENSBTAT00000017333.7; ENSBTAP00000017333.6; ENSBTAG00000013039.7. DR GeneID; 615045; -. DR KEGG; bta:615045; -. DR VEuPathDB; HostDB:ENSBTAG00000013039; -. DR eggNOG; KOG4087; Eukaryota. DR GeneTree; ENSGT00940000155096; -. DR HOGENOM; CLU_090683_3_0_1; -. DR InParanoid; E1BLF3; -. DR OMA; GDQDYCK; -. DR OrthoDB; 638584at2759; -. DR TreeFam; TF319283; -. DR Proteomes; UP000009136; Chromosome 2. DR Bgee; ENSBTAG00000013039; Expressed in ascending colon and 39 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; 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:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central. DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central. DR CDD; cd00125; PLA2c; 1. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 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; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR PANTHER; PTHR11716:SF9; PHOSPHOLIPASE A2, MEMBRANE ASSOCIATED; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. DR PROSITE; PS00119; PA2_ASP; 1. DR PROSITE; PS00118; PA2_HIS; 1. PE 3: Inferred from homology; KW Antimicrobial {ECO:0000256|ARBA:ARBA00022638}; KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601211-2}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR601211-3}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601211-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361236}; KW Signal {ECO:0000256|RuleBase:RU361236}. SQ SEQUENCE 117 AA; 13469 MW; 976435A47D310F38 CRC64; MIKFTTGKEP AISYGFYGCH CGAGHRGTPK DATDWCCRVH DCCYENLRKR GCRTSSQSYN FIFQRGQIVC GDQDYCKRRL CQCDKRAADC LDKNLKTYNK NLQYYNNLLC FGSTPKC //