ID   PA2A_DABSI              Reviewed;          18 AA.
AC   P0DJP5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Acidic phospholipase A2 Drs-PLA2;
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, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=22091349;
RA   Khunsap S., Pakmanee N., Khow O., Chanhome L., Sitprija V., Suntravat M.,
RA   Lucena S.E., Perez J.C., Sanchez E.E.;
RT   "Purification of a phospholipase A(2) from Daboia russelii siamensis venom
RT   with anticancer effects.";
RL   J. Venom Res. 2:42-51(2011).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has several
CC       activities. It exhibits anticoagulant activities (by inhibiting
CC       activated coagulation factor X (F10)), it shows hemolytic and cytotoxic
CC       activities (cytotoxic concentration(50)=65.8 nM), and inhibits cell
CC       migration in human skin melanoma cells (IC(50)=25.6 nM). In addition,
CC       it reduces tumor lung colonization of B16F10 melanoma cells in BALB/c
CC       mice by 65%. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:22091349}.
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   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22091349}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13679; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22091349};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DJP5; -.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; Secreted;
KW   Toxin.
FT   CHAIN           1..>18
FT                   /note="Acidic phospholipase A2 Drs-PLA2"
FT                   /id="PRO_0000419064"
FT   NON_TER         18
SQ   SEQUENCE   18 AA;  2013 MW;  ED4F57131224B93B CRC64;
     NLFQFARMIN GKLGAFSV