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Basic phospholipase A2 beta-bungarotoxin A-AL1 chain (Beta-BuTX A-AL1 chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (SP III-A) (Fragment)

 PA2BA_BUNMU             Reviewed;         138 AA.
Q9PTA1; Q9PRH4; Q9PSR3;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=Basic phospholipase A2 beta-bungarotoxin A-AL1 chain;
Short=Beta-BuTX A-AL1 chain;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
AltName: Full=SP III-A;
Flags: Precursor; Fragment;
Bungarus multicinctus (Many-banded krait).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
NCBI_TaxID=8616;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=10903499; DOI=10.1046/j.1432-1327.2000.01518.x;
Wu P.-F., Chang L.-S.;
"Genetic organization of A chain and B chain of beta-bungarotoxin from
Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain
genes do not share a common origin.";
Eur. J. Biochem. 267:4668-4675(2000).
[2]
PROTEIN SEQUENCE OF 19-52.
TISSUE=Venom;
PubMed=7945237; DOI=10.1042/bj3030171;
Chu C.C., Chu S.T., Chen S.W., Chen Y.H.;
"The non-phospholipase A2 subunit of beta-bungarotoxin plays an
important role in the phospholipase A2-independent neurotoxic effect:
characterization of three isotoxins with a common phospholipase A2
subunit.";
Biochem. J. 303:171-176(1994).
[3]
PROTEIN SEQUENCE OF 19-50; 83-89; 94-129 AND 136-138.
TISSUE=Venom;
PubMed=7704193; DOI=10.1016/0021-9673(94)01173-C;
Chu C.C., Li S.H., Chen Y.H.;
"Resolution of isotoxins in the beta-bungarotoxin family.";
J. Chromatogr. A 694:492-497(1995).
[4]
REVIEW.
PubMed=10936627; DOI=10.1016/S0041-0101(00)00159-8;
Rowan E.G.;
"What does beta-bungarotoxin do at the neuromuscular junction?";
Toxicon 39:107-118(2001).
-!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
neuromuscular transmission by blocking acetylcholine release from
the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis
of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 1 Ca(2+) ion.;
-!- SUBUNIT: Heterodimer; disulfide-linked. The A chains have
phospholipase A2 activity and the B chains show homology with the
basic protease inhibitors.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: This enzyme lacks one of the seven disulfide bonds found in
similar PLA2 proteins.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
subfamily. G49 sub-subfamily. {ECO:0000305}.
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EMBL; AJ251227; CAB62506.1; -; Genomic_DNA.
ProteinModelPortal; Q9PTA1; -.
SMR; Q9PTA1; -.
HOVERGEN; HBG008137; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
1: Evidence at protein level;
Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
Presynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL <1 18 {ECO:0000269|PubMed:7704193,
ECO:0000269|PubMed:7945237}.
CHAIN 19 138 Basic phospholipase A2 beta-bungarotoxin
A-AL1 chain.
/FTId=PRO_0000022846.
ACT_SITE 66 66 {ECO:0000255|PROSITE-ProRule:PRU10036}.
ACT_SITE 112 112 {ECO:0000255|PROSITE-ProRule:PRU10036}.
METAL 46 46 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 48 48 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 50 50 Calcium; via carbonyl oxygen.
{ECO:0000250}.
DISULFID 33 33 Interchain (with a B chain).
{ECO:0000250}.
DISULFID 45 137 {ECO:0000250}.
DISULFID 47 63 {ECO:0000250}.
DISULFID 69 111 {ECO:0000250}.
DISULFID 79 104 {ECO:0000250}.
DISULFID 97 109 {ECO:0000250}.
NON_TER 1 1
SEQUENCE 138 AA; 15258 MW; 9D8DB61E52C64CBD CRC64;
LAVCVSLLGA ANIPPHPLNL INFMEMIRYT IPCEKTWGEY ADYGCYCGAG GSGRPIDALD
RYCYVHGNCY GDAEKKHKCN PKTQSYSYKL TKRTIICYGA AGTCGRIVCD CDRTAALCFG
NSEYIEGHKN IDTARFCQ


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