ID   PA2AB_TRIST             Reviewed;          23 AA.
AC   P0DJP6;
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 Ts-A2;
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=Taiwan; 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: Exhibits moderate hydrolytic activities and prefers the
CC       anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles
CC       (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent
CC       hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {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=13779; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12959640};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: According to PubMed:12959640, T.stejnegeri was formerly named
CC       T.gramineus, implying that this protein is the same as PLA-II from
CC       T.gramineus. They have been kept separated, because T.gramineus and
CC       T.stejnegeri are considered to be two different species (see
CC       http://reptile-database.org). {ECO:0000305}.
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DR   AlphaFoldDB; P0DJP6; -.
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; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Toxin.
FT   CHAIN           1..>23
FT                   /note="Acidic phospholipase A2 Ts-A2"
FT                   /id="PRO_0000419066"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2770 MW;  31E4D8D95EA4CE8B CRC64;
     NLLQFENMIR NVAGRSGIWW YSD