PA2X2_BOTPA
ID PA2X2_BOTPA Reviewed; 40 AA.
AC P0DM50;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Phospholipase A2 neuwieditoxin-2;
DE Short=NeuTX-2;
DE Short=PLA2;
DE EC=3.1.1.4;
DE AltName: Full=Neuwieditoxin-II;
DE Short=NeuTX-II;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragment;
OS Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1042543;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC TISSUE=Venom;
RA Borja-Oliveira C.R., Kassab B.H., Soares A.M., Toyama M.H., Giglio J.R.,
RA Marangoni S., Re L., Rodrigues-Simioni L.;
RT "Purification and N-terminal sequencing of two presynaptic neurotoxic PLA2,
RT neuwieditoxin-I and neuwieditoxin-II, from Bothrops neuwiedi pauloensis
RT (Jararaca pintada) venom.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 13:103-121(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows presynaptic
CC neurotoxicity. 10 ug/ml of this protein produce complete neuromuscular
CC blockade up to 70 minutes, without inhibiting the responses to
CC acetylcholine (ACh), but with a partial inhibition (67%) of the
CC response to potassium chloride (KCl). {ECO:0000269|Ref.1}.
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:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBUNIT: Dimer. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DM50; -.
DR SMR; P0DM50; -.
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 Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SUPFAM; SSF48619; SSF48619; 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; Toxin.
FT CHAIN 1..>40
FT /note="Phospholipase A2 neuwieditoxin-2"
FT /id="PRO_0000423031"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..?
FT /evidence="ECO:0000250"
FT DISULFID 28..?
FT /evidence="ECO:0000250"
FT NON_TER 40
SQ SEQUENCE 40 AA; 4524 MW; 07567EC4F9AB368D CRC64;
SLFEFAKMIL EETKRLPFPY YGAYGCYCGW GGQGQPKDAT
