ID   PA22_BUNCE              Reviewed;         147 AA.
AC   Q8QFW3;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-NOV-2008, entry version 40.
DE   RecName: Full=Phospholipase A2, beta bungarotoxin A2 chain;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Bungarus caeruleus (Indian krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=132961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Paramasivam M., Srinivasan A., Singh T.P.;
RT   "Bungarus caeruleus mRNA for phospholipase A2, beta bungarotoxin A2
RT   chain complete coding region.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. Inhibits neuromuscular
CC       transmission by blocking acetylcholine release from the nerve
CC       termini. Acts presynaptically (By similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
CC       subfamily.
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DR   EMBL; AY081147; AAL87004.1; -; mRNA.
DR   HSSP; P00617; 1BUN.
DR   SMR; Q8QFW3; 28-147.
DR   HOVERGEN; Q8QFW3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   GO; GO:0007268; P:synaptic transmission; IEA:UniProtKB-KW.
DR   InterPro; IPR016090; Phospholipase_A2.
DR   InterPro; IPR013090; Phospholipase_A2_AS.
DR   InterPro; IPR001211; Phospholipase_A2_euk.
DR   Gene3D; G3DSA:1.20.90.10; Phospholipase_A2; 1.
DR   PANTHER; PTHR11716; Phospholipase_A2; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   ProDom; PD000303; PhospholipaseA2; 1.
DR   SMART; SM00085; PA2c; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Lipid degradation; Metal-binding; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     27       By similarity.
FT                                /FTId=PRO_0000022825.
FT   CHAIN        28    147       Phospholipase A2, beta bungarotoxin A2
FT                                chain.
FT                                /FTId=PRO_0000022826.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    121    121       By similarity.
FT   METAL        55     55       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        57     57       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        59     59       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        76     76       Calcium (By similarity).
FT   DISULFID     42     42       Interchain (with a B chain) (By
FT                                similarity).
FT   DISULFID     54    146       By similarity.
FT   DISULFID     56     72       By similarity.
FT   DISULFID     71    127       By similarity.
FT   DISULFID     78    120       By similarity.
FT   DISULFID     88    113       By similarity.
FT   DISULFID    106    118       By similarity.
SQ   SEQUENCE   147 AA;  16120 MW;  3B72A0EEE323EADF CRC64;
     MYPAHLLVLS AVCVSLLGAA NIPPYPLNLI NFMEMIRYTI PCDKTWGHYA DYGCYCGAGG
     SGTPVDALDR CCYVHDNCYG VAENKHKCNP KTQSCSYKLT KRTIICYGAA GTCGRIVCDC
     DRTAALCFGD SEYIGAHKNI DTKRHCQ
//