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Basic phospholipase A2 beta-bungarotoxin A7 chain (Beta-BuTX A7 chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Fragment)

 PA2B7_BUNMU             Reviewed;         137 AA.
Q9PU97;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 79.
RecName: Full=Basic phospholipase A2 beta-bungarotoxin A7 chain;
Short=Beta-BuTX A7 chain;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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 [MRNA].
TISSUE=Venom gland;
PubMed=11732693; DOI=10.1023/A:1012237005574;
Wu P.-F., Chang L.-S.;
"Expression of A chain and B chain of beta-bungarotoxin from taiwan
banded krait: the functional implication of the interchain disulfide
bond between A chain and B chain.";
J. Protein Chem. 20:413-421(2001).
[2]
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:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion. {ECO:0000250};
-!- SUBUNIT: Heterodimer; disulfide-linked. The A chains have
phospholipase A2 activity and the B chains show homology with the
basic protease inhibitors (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
subfamily. D49 sub-subfamily. {ECO:0000305}.
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EMBL; AJ242012; CAB62384.1; -; mRNA.
ProteinModelPortal; Q9PU97; -.
SMR; Q9PU97; -.
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.
InterPro; IPR033113; PLipase_A2_His_AS.
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.
PROSITE; PS00118; PA2_HIS; 1.
2: Evidence at transcript level;
Calcium; Disulfide bond; Hydrolase; Lipid degradation;
Lipid metabolism; Metal-binding; Neurotoxin; Presynaptic neurotoxin;
Secreted; Signal; Toxin.
SIGNAL <1 17 {ECO:0000250}.
CHAIN 18 137 Basic phospholipase A2 beta-bungarotoxin
A7 chain.
/FTId=PRO_0000022845.
ACT_SITE 65 65 {ECO:0000250}.
ACT_SITE 111 111 {ECO:0000250}.
METAL 45 45 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 47 47 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 49 49 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 66 66 Calcium. {ECO:0000250}.
DISULFID 32 32 Interchain (with a B chain).
{ECO:0000250}.
DISULFID 44 136 {ECO:0000250}.
DISULFID 46 62 {ECO:0000250}.
DISULFID 61 117 {ECO:0000250}.
DISULFID 68 110 {ECO:0000250}.
DISULFID 78 103 {ECO:0000250}.
DISULFID 96 108 {ECO:0000250}.
NON_TER 1 1
SEQUENCE 137 AA; 15120 MW; 4981333D4FD85495 CRC64;
AVCVSLLGAA NIPPHPLNLI NFMEMIRYTI PCEKTWGEYA DYGCYCGAGG SGRPIDALDR
CCYVHDNCYG EAEKIPGCNP KTKTYSYKLT KRTIICYGAA GTCGRIVCDC DRTAALCFGN
SEYIEGHKNI DTKRHCR


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