ID   PA2_DABSI               Reviewed;          22 AA.
AC   P18999;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   23-FEB-2022, entry version 65.
DE   RecName: Full=Phospholipase A2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=343250;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Tu G.C., Ran Y.L., Zhang Y.S., Chen Y.-C., Liu K.F.;
RT   "The amino acid composition and the N-terminal partial sequence of the
RT   toxic phospholipase A of Vipera russelli siamensis venom (from Fujian
RT   province).";
RL   Dong Wu Xue Yan Jiu 2:9-12(1981).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC       neuromuscular transmission by blocking acetylcholine release from the
CC       nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC       2-acyl groups in 3-sn-phosphoglycerides.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC         ProRule:PRU10036};
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   -!- PTM: Seven disulfide bonds are present.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   PIR; JC0009; JC0009.
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; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Toxin.
FT   CHAIN           1..>22
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000161718"
FT   NON_TER         22
SQ   SEQUENCE   22 AA;  2659 MW;  781B6D471A400713 CRC64;
     NLFQFARMIN KKLGAFXFXN YI