ID   PA2B2_AGKBI             Reviewed;          39 AA.
AC   Q9PSF9;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Basic phospholipase A2 2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=Phospholipase A2 II;
DE            Short=PLA2-II;
DE   Flags: Fragment;
OS   Agkistrodon bilineatus (Cantil) (Tropical moccasin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8718;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND ACTIVITY REGULATION.
RC   TISSUE=Venom;
RX   PubMed=8138046; DOI=10.1016/0020-711x(94)90193-7;
RA   Nikai T., Komori Y., Ohara A., Yagihashi S., Ohizumi Y., Sugihara H.;
RT   "Characterization and amino-terminal sequence of phospholipase A2-II from
RT   the venom of Agkistrodon bilineatus (common cantil).";
RL   Int. J. Biochem. 26:43-48(1994).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits ADP-induced
CC       platelet aggregation. PLA2 catalyzes the calcium-dependent hydrolysis
CC       of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:8138046}.
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   -!- ACTIVITY REGULATION: Inhibited by ethylenediamine tetraacetic acid,
CC       ethyleneglycol (beta-aminoethyl) N,N,N',N'-tetraacetic acid, p-
CC       bromophenacyl bromide or N-bromosuccinimide, but not by iodoacetic acid
CC       or diisopropyl fluorophosphate. {ECO:0000269|PubMed:8138046}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; Q9PSF9; -.
DR   SMR; Q9PSF9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hemostasis impairing toxin; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Platelet aggregation inhibiting toxin;
KW   Secreted; Toxin.
FT   CHAIN           1..>39
FT                   /note="Basic phospholipase A2 2"
FT                   /id="PRO_0000161593"
FT   NON_TER         39
SQ   SEQUENCE   39 AA;  4212 MW;  52B299698AC43CD2 CRC64;
     SLLELGKMIL QETGKIAITS YGSYGCNCGW GHRGRPKDA