ID E1BLF3_BOVIN Unreviewed; 144 AA. AC E1BLF3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 86. 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:ENSBTAP00000017333.5}; 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:ENSBTAP00000017333.5, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017333.5, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333.5, 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:ENSBTAP00000017333.5} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333.5}; RG Ensembl; RL Submitted (NOV-2023) 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; ENSBTAT00000017333.6; ENSBTAP00000017333.5; ENSBTAG00000013039.6. 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|PIRSR:PIRSR601211-2, ECO:0000256|RuleBase:RU361236}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR601211-3}; KW Hydrolase {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}. 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="Phospholipase A2" FT /evidence="ECO:0000259|SMART:SM00085" FT ACT_SITE 67 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-1" FT ACT_SITE 111 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-1" FT BINDING 49 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT BINDING 51 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT BINDING 68 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT DISULFID 46..137 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" FT DISULFID 48..64 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" FT DISULFID 63..117 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" FT DISULFID 69..144 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" FT DISULFID 70..110 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" FT DISULFID 79..103 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" FT DISULFID 97..108 FT /evidence="ECO:0000256|PIRSR:PIRSR601211-3" SQ SEQUENCE 144 AA; 16346 MW; 37B45626AFF667F5 CRC64; MKTLLLLAVI MAIGLLQVHG GLADFQKMIK FTTGKEPAIS YGFYGCHCGA GHRGTPKDAT DWCCRVHDCC YENLRKRGCR TSSQSYNFIF QRGQIVCGDQ DYCKRRLCQC DKRAADCLDK NLKTYNKNLQ YYNNLLCFGS TPKC //