ID   PA2AC_CROVV             Reviewed;          23 AA.
AC   P0DJM5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Acidic phospholipase A2 Cvv-E6c;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Crotalus viridis viridis (Prairie rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8742;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND MASS SPECTROMETRY.
RC   STRAIN=Colorado, South Dakota, Texas, Western Oklahoma, and Wyoming;
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12623078; DOI=10.1016/s0003-9861(02)00747-6;
RA   Tsai I.-H., Wang Y.-M., Chen Y.-H., Tu A.T.;
RT   "Geographic variations, cloning, and functional analyses of the venom
RT   acidic phospholipases A2 of Crotalus viridis viridis.";
RL   Arch. Biochem. Biophys. 411:289-296(2003).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that significantly
CC       inhibits ADP-induced platelet aggregation in platelet-rich plasma of
CC       human, rabbit and guinea pig. PLA2 catalyzes the calcium-dependent
CC       hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:12623078}.
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;
CC         Evidence={ECO:0000269|PubMed:12623078};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13817; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12623078};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DJM5; -.
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   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..>23
FT                   /note="Acidic phospholipase A2 Cvv-E6c"
FT                   /id="PRO_0000418555"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2581 MW;  5E5D04DF9E607D8A CRC64;
     NLVQFELLIM KVAKRSGLLS YSA