ID   PA2A4_TRIST             Reviewed;          24 AA.
AC   P82895;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Acidic phospholipase A2 4;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=PLA2-IV;
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.
RC   TISSUE=Venom;
RA   Li S.-Y., Guo Z.-X., Yang Y.-Y., Wang W.-Y., Xiong Y.-L.;
RT   "Isolation and sequencing of five variants of phospholipase A2 from venom
RT   of snake Trimeresurus stejnegeri.";
RL   J. Hubei Univ. 25:63-68(2003).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides.
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   -!- MISCELLANEOUS: Hemolytic and neurotoxic activities are not detected
CC       (Ref.1).
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P82895; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Secreted.
FT   CHAIN           1..>24
FT                   /note="Acidic phospholipase A2 4"
FT                   /id="PRO_0000161710"
FT   NON_TER         24
SQ   SEQUENCE   24 AA;  2834 MW;  AD892238D95A861D CRC64;
     NLMQFELLIM KVAGRSGIVW YSDY