PA2BA_BUNCA
ID PA2BA_BUNCA Reviewed; 14 AA.
AC P84475;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 23-FEB-2022, entry version 39.
DE RecName: Full=Basic phospholipase A2 T1-1 A chain;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase T1-1 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 0.26 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 T1-1 A chain"
FT /id="PRO_0000161630"
FT NON_TER 14
FT /evidence="ECO:0000303|PubMed:14769867"
SQ SEQUENCE 14 AA; 1816 MW; 6E91DBA06720A09B CRC64;
NLYQFKEMIR YTIP
