ID   PA2AG_TRIST             Reviewed;          23 AA.
AC   P0DJP8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Acidic phospholipase A2 CTs-A1;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS   stejnegeri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=39682;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   STRAIN=Chinese; TISSUE=Venom;
RX   PubMed=12959640; DOI=10.1042/bj20030818;
RA   Tsai I.-H., Wang Y.-M., Chen Y.-H., Tsai T.-S., Tu M.-C.;
RT   "Venom phospholipases A2 of bamboo viper (Trimeresurus stejnegeri):
RT   molecular characterization, geographic variations and evidence of multiple
RT   ancestries.";
RL   Biochem. J. 377:215-223(2004).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows a moderate
CC       inhibition of ADP-induced human platelet aggregation when tested on
CC       platelet rich plasma. Exhibits moderate hydrolytic activities and
CC       prefers the anionic micelles (dPPC with deoxycholate) to the
CC       zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the
CC       calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC       phosphoglycerides. {ECO:0000269|PubMed:12959640}.
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: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13774; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12959640};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DJP8; -.
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 CTs-A1"
FT                   /id="PRO_0000419071"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2509 MW;  63F1B8DF86ED0850 CRC64;
     SLIQFETLIM KVAGQSGMFS YSA