ID   E1BLF3_BOVIN            Unreviewed;       144 AA.
AC   E1BLF3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   16-MAR-2016, entry version 41.
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).
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   -!- SIMILARITY: Belongs to the phospholipase A2 family.
CC       {ECO:0000256|RuleBase:RU003654}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSBTAP00000017333}.
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DR   EMBL; DAAA02006512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002685775.1; XM_002685729.1.
DR   RefSeq; XP_871834.1; XM_866741.2.
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; EOG7FZ00N; -.
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   NextBio; 20899419; -.
DR   Proteomes; UP000009136; Chromosome 2.
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:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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; 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:SAAS00435610};
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:SAAS00524324};
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
//