ID   PA2BU_BUNCA             Reviewed;          14 AA.
AC   P84474;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   23-FEB-2022, entry version 40.
DE   RecName: Full=Basic phospholipase A2 T2 A chain;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase T2 A;
DE   Flags: Fragment;
OS   Bungarus candidus (Malayan krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=92438;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND TOXIC DOSE.
RC   TISSUE=Venom {ECO:0000269|PubMed:14769867};
RX   PubMed=14769867; DOI=10.1093/jb/mvg187;
RA   Khow O., Chanhome L., Omori-Satoh T., Ogawa Y., Yanoshita R., Samejima Y.,
RA   Kuch U., Mebs D., Sitprija V.;
RT   "Isolation, toxicity and amino terminal sequences of three major
RT   neurotoxins in the venom of Malayan krait (Bungarus candidus) from
RT   Thailand.";
RL   J. Biochem. 134:799-804(2003).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC       neuromuscular transmission by blocking acetylcholine release from the
CC       nerve termini and exhibits indirect hemolytic activity against human
CC       erythrocytes. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:14769867}.
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:0000250|UniProtKB:P00617, ECO:0000255|PROSITE-
CC         ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P00617};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P00617};
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. The A chains have phospholipase
CC       A2 activity and the B chains show homology with the basic protease
CC       inhibitors. {ECO:0000269|PubMed:14769867}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14769867}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:14769867}.
CC   -!- TOXIC DOSE: LD(50) is 0.84 mg/kg by intravenous injection in mice.
CC       {ECO:0000269|PubMed:14769867}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000255}.
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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: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; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Toxin.
FT   CHAIN           1..>14
FT                   /note="Basic phospholipase A2 T2 A chain"
FT                   /id="PRO_0000161632"
FT   NON_TER         14
FT                   /evidence="ECO:0000303|PubMed:14769867"
SQ   SEQUENCE   14 AA;  1755 MW;  690FC3173720A09B CRC64;
     NLINFMEMIR YTIP