ID   PA2_AUSSU               Reviewed;          17 AA.
AC   P59066;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Phospholipase A2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Austrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Austrelaps.
OX   NCBI_TaxID=29156;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=8362372; DOI=10.1016/0049-3848(93)90089-7;
RA   Yuan Y., Jackson S.P., Mitchell C.A., Salem H.H.;
RT   "Purification and characterisation of a snake venom phospholipase A2: a
RT   potent inhibitor of platelet aggregation.";
RL   Thromb. Res. 70:471-481(1993).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits collagen-,
CC       ADP-, thrombin-, ionophore-, adrenaline-, ristocetin-, and arachidonic
CC       acid-induced platelet aggregation. Inhibits serotonin release. PLA2
CC       catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC       sn-phosphoglycerides. {ECO:0000269|PubMed:8362372}.
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P59066; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hemostasis impairing toxin; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Platelet aggregation inhibiting toxin;
KW   Secreted; Toxin.
FT   CHAIN           1..>17
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000161609"
FT   NON_TER         17
SQ   SEQUENCE   17 AA;  1846 MW;  03FB7DD7B7D7D1CB CRC64;
     NLIQFANMIG CANHGSR