PA2BA_BUNMU
ID PA2BA_BUNMU Reviewed; 138 AA.
AC Q9PTA1; Q9PRH4; Q9PSR3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Basic phospholipase A2 beta-bungarotoxin A-AL1 chain;
DE Short=Beta-BuTX A-AL1 chain;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=SP III-A;
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=10903499; DOI=10.1046/j.1432-1327.2000.01518.x;
RA Wu P.-F., Chang L.-S.;
RT "Genetic organization of A chain and B chain of beta-bungarotoxin from
RT Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain
RT genes do not share a common origin.";
RL Eur. J. Biochem. 267:4668-4675(2000).
RN [2]
RP PROTEIN SEQUENCE OF 19-52.
RC TISSUE=Venom;
RX PubMed=7945237; DOI=10.1042/bj3030171;
RA Chu C.C., Chu S.T., Chen S.W., Chen Y.H.;
RT "The non-phospholipase A2 subunit of beta-bungarotoxin plays an important
RT role in the phospholipase A2-independent neurotoxic effect:
RT characterization of three isotoxins with a common phospholipase A2
RT subunit.";
RL Biochem. J. 303:171-176(1994).
RN [3]
RP PROTEIN SEQUENCE OF 19-50; 83-89; 94-129 AND 136-138.
RC TISSUE=Venom;
RX PubMed=7704193; DOI=10.1016/0021-9673(94)01173-c;
RA Chu C.C., Li S.H., Chen Y.H.;
RT "Resolution of isotoxins in the beta-bungarotoxin family.";
RL J. Chromatogr. A 694:492-497(1995).
RN [4]
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:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion.;
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.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: This enzyme lacks one of the seven disulfide bonds found in
CC similar PLA2 proteins.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC G49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ251227; CAB62506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9PTA1; -.
DR SMR; Q9PTA1; -.
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 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.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL <1..18
FT /evidence="ECO:0000269|PubMed:7704193,
FT ECO:0000269|PubMed:7945237"
FT CHAIN 19..138
FT /note="Basic phospholipase A2 beta-bungarotoxin A-AL1
FT chain"
FT /id="PRO_0000022846"
FT ACT_SITE 66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT ACT_SITE 112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 33
FT /note="Interchain (with a B chain)"
FT /evidence="ECO:0000250"
FT DISULFID 45..137
FT /evidence="ECO:0000250"
FT DISULFID 47..63
FT /evidence="ECO:0000250"
FT DISULFID 69..111
FT /evidence="ECO:0000250"
FT DISULFID 79..104
FT /evidence="ECO:0000250"
FT DISULFID 97..109
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 138 AA; 15258 MW; 9D8DB61E52C64CBD CRC64;
LAVCVSLLGA ANIPPHPLNL INFMEMIRYT IPCEKTWGEY ADYGCYCGAG GSGRPIDALD
RYCYVHGNCY GDAEKKHKCN PKTQSYSYKL TKRTIICYGA AGTCGRIVCD CDRTAALCFG
NSEYIEGHKN IDTARFCQ
