ID   PA2B_BOTJR              Reviewed;          21 AA.
AC   P0CAR8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Basic phospholipase A2 BjIV;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Bothrops jararacussu (Jararacussu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8726;
RN   [1]
RP   PROTEIN SEQUENCE, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=11565904; DOI=10.1023/a:1010956126585;
RA   Bonfim V.L., Toyama M.H., Novello J.C., Hyslop S., Oliveira C.R.B.,
RA   Rodrigues-Simioni L., Marangoni S.;
RT   "Isolation and enzymatic characterization of a basic phospholipase A2 from
RT   Bothrops jararacussu snake venom.";
RL   J. Protein Chem. 20:239-245(2001).
CC   -!- FUNCTION: Snake venom phospholipase A2 has a high enzymatic activity
CC       and produces moderate myonecrosis in skeletal muscle, but shows no
CC       neuromuscular activity in mouse phrenic nerve-diaphragm preparations.
CC       PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC       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;
CC         Evidence={ECO:0000269|PubMed:11565904};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11565904};
CC   -!- ACTIVITY REGULATION: Inhibited by crotapotin.
CC       {ECO:0000269|PubMed:11565904}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.7 mM for 4-nitro-3-(octanoyloxy)benzoic acid
CC         {ECO:0000269|PubMed:11565904};
CC         Vmax=7.2 nmol/min/mg enzyme {ECO:0000269|PubMed:11565904};
CC       pH dependence:
CC         Optimum pH is 8.2. {ECO:0000269|PubMed:11565904};
CC       Temperature dependence:
CC         Optimum temperature is 35-45 degrees Celsius.
CC         {ECO:0000269|PubMed:11565904};
CC   -!- SUBUNIT: Can form dimers, trimers and tetramers.
CC       {ECO:0000269|PubMed:11565904}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains seven disulfide bonds.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0CAR8; -.
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; Myotoxin; Secreted;
KW   Toxin.
FT   CHAIN           1..>21
FT                   /note="Basic phospholipase A2 BjIV"
FT                   /id="PRO_0000377502"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2490 MW;  E2C8D86A0124DA25 CRC64;
     DLWSWGQMIQ ETGLLPSYTT Y