PA2B5_BUNMU
ID PA2B5_BUNMU Reviewed; 137 AA.
AC P59018;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Basic phospholipase A2 beta-bungarotoxin A5 chain;
DE Short=Beta-BuTX A5 chain;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor; Fragment;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=8619855; DOI=10.1006/bbrc.1996.0595;
RA Chang L.-S., Wu P.-F., Chang C.-C.;
RT "cDNA sequence analysis and expression of the a chain of beta-bungarotoxin
RT from Bungarus multicinctus (Taiwan banded krait).";
RL Biochem. Biophys. Res. Commun. 221:328-332(1996).
RN [2]
RP MUTAGENESIS OF TYR-28; CYS-32 AND LEU-89.
RX PubMed=9008300; DOI=10.1007/bf01887150;
RA Chang L.-S., Wu P.-F., Chang C.-C.;
RT "cDNA sequence analysis and mutagenesis studies on the A chain of beta-
RT bungarotoxin from Taiwan banded krait.";
RL J. Protein Chem. 15:755-761(1996).
RN [3]
RP REVIEW.
RX PubMed=10936627; DOI=10.1016/s0041-0101(00)00159-8;
RA Rowan E.G.;
RT "What does beta-bungarotoxin do at the neuromuscular junction?";
RL Toxicon 39:107-118(2001).
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z54225; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JC4710; JC4710.
DR AlphaFoldDB; P59018; -.
DR SMR; P59018; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL <1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..137
FT /note="Basic phospholipase A2 beta-bungarotoxin A5 chain"
FT /id="PRO_0000022843"
FT ACT_SITE 65
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 32
FT /note="Interchain (with a B chain)"
FT /evidence="ECO:0000250"
FT DISULFID 44..136
FT /evidence="ECO:0000250"
FT DISULFID 46..62
FT /evidence="ECO:0000250"
FT DISULFID 61..117
FT /evidence="ECO:0000250"
FT DISULFID 68..110
FT /evidence="ECO:0000250"
FT DISULFID 78..103
FT /evidence="ECO:0000250"
FT DISULFID 96..108
FT /evidence="ECO:0000250"
FT MUTAGEN 28
FT /note="Y->C: Alterations of folding pathway and structure."
FT /evidence="ECO:0000269|PubMed:9008300"
FT MUTAGEN 32
FT /note="C->S: Alterations of folding pathway and structure."
FT /evidence="ECO:0000269|PubMed:9008300"
FT MUTAGEN 89
FT /note="L->C: Alterations of folding pathway and structure."
FT /evidence="ECO:0000269|PubMed:9008300"
FT NON_TER 1
SQ SEQUENCE 137 AA; 15265 MW; 11E25066A18E7293 CRC64;
AVCVSLLGAA NIPPQHLNLY QFKEMIRYTI PCEKTWGEYA DYGCYCGAGG SGRPIDALDR
CCYVHDNCYG DAEKKHKCNP KTQSYSYKLT KRTIICYGAA GTCGRIVCDC DRTTALCFGN
SEYIEGHKNI DTARFCQ
