ID   PA2A_OVOMO              Reviewed;          29 AA.
AC   P0DJJ7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Acidic phospholipase A2 Omo-E6;
DE            Short=svPLA2 {ECO:0000303|PubMed:22115990};
DE            EC=3.1.1.4 {ECO:0000269|PubMed:22115990};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Ovophis monticola (Chinese mountain pitviper) (Trimeresurus monticola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Ovophis.
OX   NCBI_TaxID=103941;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND CATALYTIC ACTIVITY.
RC   TISSUE=Venom;
RX   PubMed=22115990; DOI=10.1016/j.toxicon.2011.10.016;
RA   Tsai I.-H., Tsai T.-S., Wang Y.-M., Tu M.-C., Chang H.-C.;
RT   "Cloning and characterization of Trimeresurus gracilis venom phospholipases
RT   A(2): comparison with Ovophis okinavensis venom and the systematic
RT   implications.";
RL   Toxicon 59:151-157(2012).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the
CC       ADP- and collagen-induced human platelet aggregation (By similarity).
CC       Exhibits strong hydrolytic activities and prefers the anionic micelles
CC       (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton
CC       X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000250,
CC       ECO:0000269|PubMed:22115990}.
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:0000269|PubMed:22115990};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:22115990};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=13801; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22115990};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DJJ7; -.
DR   SMR; P0DJJ7; -.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0043655; C:host extracellular space; TAS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..>29
FT                   /note="Acidic phospholipase A2 Omo-E6"
FT                   /id="PRO_0000419053"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         29
SQ   SEQUENCE   29 AA;  3263 MW;  245269EEA0ED2F43 CRC64;
     DLMQFETLIM KIAGRSGVWI YGSYGCYCG