ID   E1BLF3_BOVIN            Unreviewed;       144 AA.
AC   E1BLF3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JUN-2015, entry version 35.
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).
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000017333}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333};
RG   Ensembl;
RL   Submitted (OCT-2011) to UniProtKB.
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   Ensembl; ENSBTAT00000017333; ENSBTAP00000017333; ENSBTAG00000013039.
DR   GeneID; 615045; -.
DR   KEGG; bta:615045; -.
DR   GeneTree; ENSGT00760000119160; -.
DR   InParanoid; E1BLF3; -.
DR   KO; K01047; -.
DR   OMA; MIKFTTG; -.
DR   OrthoDB; EOG7FZ00N; -.
DR   TreeFam; TF319283; -.
DR   Reactome; REACT_272771; Acyl chain remodelling of PE.
DR   Reactome; REACT_289244; Acyl chain remodelling of PS.
DR   Reactome; REACT_290641; Acyl chain remodelling of PC.
DR   Reactome; REACT_301543; Synthesis of PA.
DR   Reactome; REACT_315766; Acyl chain remodelling of PG.
DR   Reactome; REACT_325612; Acyl chain remodelling of PI.
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; IPR013090; PLipase_A2_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
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:SAAS00039002};
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:SAAS00039003};
KW   Signal {ECO:0000256|RuleBase:RU361236}.
FT   SIGNAL        1     23       {ECO:0000256|RuleBase:RU361236}.
FT   CHAIN        24    144       {ECO:0000256|RuleBase:RU361236}.
FT                                /FTId=PRO_5001390411.
SQ   SEQUENCE   144 AA;  16346 MW;  37B45626AFF667F5 CRC64;
     MKTLLLLAVI MAIGLLQVHG GLADFQKMIK FTTGKEPAIS YGFYGCHCGA GHRGTPKDAT
     DWCCRVHDCC YENLRKRGCR TSSQSYNFIF QRGQIVCGDQ DYCKRRLCQC DKRAADCLDK
     NLKTYNKNLQ YYNNLLCFGS TPKC
//