PA2AE_TRIST
ID PA2AE_TRIST Reviewed; 23 AA.
AC P0DJP7;
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-A5;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=CTs-A5;
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, and 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: 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 high hydrolytic activities and prefers
CC the anionic micelles (dPPC with deoxycholate) to the zwitterionic
CC micelles (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=13711; 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, supposing that this protein is the same as PLA-III from
CC T.gramineus. They have been kept separated, because T.gramineus and
CC T.stejnegeri are considered as being two different species (see
CC http://reptile-database.org). {ECO:0000305}.
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DR AlphaFoldDB; P0DJP7; -.
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-A5"
FT /id="PRO_0000419069"
FT NON_TER 23
SQ SEQUENCE 23 AA; 2651 MW; 554378D17B248D8A CRC64;
NLMQFETLIM KVAGRSGVWY YGS
