ID   PA2_PSEPP               Reviewed;          34 AA.
AC   Q7LZG3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Phospholipase A2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragments;
OS   Pseudechis papuanus (Papuan black snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX   NCBI_TaxID=61265;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=7632717; DOI=10.1016/0167-4838(95)00081-5;
RA   Laing G.D., Kamiguti A.S., Wilkinson M.C., Lowe G.M., Theakston R.D.G.;
RT   "Characterisation of a purified phospholipase A2 from the venom of the
RT   Papuan black snake (Pseudechis papuanus).";
RL   Biochim. Biophys. Acta 1250:137-143(1995).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that strongly inhibits
CC       platelet aggregation and has a strong anticoagulant activity. PLA2
CC       catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC       sn-phosphoglycerides. {ECO:0000269|PubMed:7632717}.
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   -!- 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 {ECO:0000269|PubMed:7632717}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:7632717}.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- TOXIC DOSE: LD(50) is 722 ug/kg by intravenous injection into mice.
CC       {ECO:0000269|PubMed:7632717}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   PIR; S57282; S57282.
DR   AlphaFoldDB; Q7LZG3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..>34
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000408517"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_CONS        20..21
FT                   /evidence="ECO:0000305"
FT   NON_TER         34
SQ   SEQUENCE   34 AA;  4020 MW;  F768E3AA18E759AC CRC64;
     NLIQFSNMIQ LDRCCETHDN EAEKKGCYPK LTLY