ID   PA22A_BUNCA             Reviewed;          14 AA.
AC   P84472;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Phospholipase A2, neurotoxin T1-2 A chain;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase T1-2 A;
DE   Flags: Fragment;
OS   Bungarus candidus (Malayan krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=92438;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND LETHAL DOSE.
RC   TISSUE=Venom;
RX   PubMed=14769867; DOI=10.1093/jb/mvg187;
RA   Khow O., Chanhome L., Omori-Satoh T., Ogawa Y., Yanoshita R.,
RA   Samejima Y., 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: Neurotoxin T1-2 is a presynaptic neurotoxin of the venom
CC       that exhibits indirect hemolytic activity against human
CC       erythrocytes. PA2 catalyzes the calcium-dependent hydrolysis of
CC       the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits
CC       neuromuscular transmission by blocking acetylcholine release from
CC       the nerve termini.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Binds 1 calcium ion (By similarity).
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. The A chains have
CC       phospholipase A2 activity and the B chains show homology with the
CC       basic protease inhibitors.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- TOXIC DOSE: LD(50) is 0.22 mg/kg by intravenous injection in mice.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
CC       subfamily.
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DR   HOVERGEN; P84472; -.
DR   BRENDA; 3.1.1.4; 291622.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; IEA:UniProtKB-KW.
DR   InterPro; IPR013090; Phospholipase_A2_AS.
DR   PROSITE; PS00119; PA2_ASP; PARTIAL.
DR   PROSITE; PS00118; PA2_HIS; PARTIAL.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Neurotoxin; Presynaptic neurotoxin; Secreted;
KW   Toxin.
FT   CHAIN         1    >14       Phospholipase A2, neurotoxin T1-2 A
FT                                chain.
FT                                /FTId=PRO_0000161631.
FT   NON_TER      14     14
SQ   SEQUENCE   14 AA;  1816 MW;  6E91DBA06720A09B CRC64;
     NLYQFKEMIR YTIP
//