ID   PA2BD_BUNFA             Reviewed;          31 AA.
AC   Q7LZQ6;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Basic phospholipase A2 13;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Cytotoxin XIII;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=Phospholipase A2 XIII;
DE   Flags: Fragment;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Zhang Y.S., Wu S.L., Chen Y.C., Chen S.Q.;
RT   "The amino acid composition and partial sequence of cytotoxin XIII from
RT   Canton Bungarus fasciatus venom.";
RL   Dong Wu Xue Yan Jiu 2:27-32(1981).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC       neuromuscular transmission by blocking acetylcholine release from the
CC       nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC       2-acyl groups in 3-sn-phosphoglycerides (By similarity). {ECO:0000250}.
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   -!- 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   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000305}.
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DR   PIR; JC0008; JC0008.
DR   AlphaFoldDB; Q7LZQ6; -.
DR   SMR; Q7LZQ6; -.
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   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>31
FT                   /note="Basic phospholipase A2 13"
FT                   /id="PRO_0000161633"
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  3704 MW;  8BF975AB20C9F729 CRC64;
     NLYQFKNMIE CAGTRTWIAY VKYGAYTYAY T