ID   E1BLF3_BOVIN            Unreviewed;       144 AA.
AC   E1BLF3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   11-DEC-2019, entry version 66.
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; 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=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       Note=Binds 1 Ca(2+) ion per subunit. {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}.
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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   eggNOG; ENOG411283D; LUCA.
DR   GeneTree; ENSGT00940000155096; -.
DR   InParanoid; E1BLF3; -.
DR   KO; K01047; -.
DR   OMA; CQCDKAA; -.
DR   OrthoDB; 1422829at2759; -.
DR   TreeFam; TF319283; -.
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:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR   GO; GO:0004623; F: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: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; -; 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|SAAS:SAAS00331946};
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, ECO:0000256|SAAS:SAAS00614840};
KW   Signal {ECO:0000256|RuleBase:RU361236}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361236"
FT   CHAIN           24..144
FT                   /note="Phospholipase A(2)"
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
//