ID   PA2B2_BOTPA             Reviewed;          35 AA.
AC   P0DM52;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Basic phospholipase A2 BnpTX-2;
DE            Short=BnPTx-II;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=1042543;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, BIOASSAY, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=15302537; DOI=10.1016/j.toxicon.2004.06.008;
RA   Rodrigues V.M., Marcussi S., Cambraia R.S., de Araujo A.L.,
RA   Malta-Neto N.R., Hamaguchi A., Ferro E.A., Homsi-Brandeburgo M.I.,
RA   Giglio J.R., Soares A.M.;
RT   "Bactericidal and neurotoxic activities of two myotoxic phospholipases A2
RT   from Bothrops neuwiedi pauloensis snake venom.";
RL   Toxicon 44:305-314(2004).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2). In vitro, shows
CC       anticoagulant activity and induces cytotoxicity when tested on C2C12
CC       myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity
CC       (intramuscular injection), edema (injection in the subplantar region)
CC       and lethality. The catalytic and anticoagulant activities of BnpTX-II
CC       are lower than those of BnpTX-I. PLA2 catalyzes the calcium-dependent
CC       hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:15302537}.
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:0000269|PubMed:15302537};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:15302537}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 7 disulfide bonds.
CC   -!- MISCELLANEOUS: Has a pI of approximately 7.8 and about 121 amino acids.
CC       {ECO:0000305|PubMed:15302537}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DM52; -.
DR   SMR; P0DM52; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR001211; PLipase_A2.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
KW   Secreted; Toxin.
FT   CHAIN           1..>35
FT                   /note="Basic phospholipase A2 BnpTX-2"
FT                   /id="PRO_0000423033"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         35
SQ   SEQUENCE   35 AA;  4051 MW;  202C3CE166CB5C5F CRC64;
     SLWEFAQMIL EETKRLPFPY YGAYGCYCGW GGQGQ