ID   PA2HC_OXYSA             Reviewed;          40 AA.
AC   P0DKT9;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Neutral phospholipase A2 homolog cannitoxin beta chain 2;
DE            Short=svPLA2 homolog;
DE   Flags: Fragment;
OS   Oxyuranus scutellatus canni (Papuan taipan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=183720;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16135698; DOI=10.1124/jpet.105.093641;
RA   Kuruppu S., Reeve S., Banerjee Y., Kini R.M., Smith A.I., Hodgson W.C.;
RT   "Isolation and pharmacological characterization of cannitoxin, a
RT   presynaptic neurotoxin from the venom of the Papuan Taipan (Oxyuranus
RT   scutellatus canni).";
RL   J. Pharmacol. Exp. Ther. 315:1196-1202(2005).
CC   -!- FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2)
CC       heterotrimer that acts as a potent presynaptic neurotoxin by blocking
CC       synaptic transmission and synaptic vesicle recycling. Enzymatic
CC       activity is essential for the neurotoxic effects (PubMed:16135698). May
CC       act by binding in a calcium-dependent fashion to neurotonal pentraxin-1
CC       (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal
CC       pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium
CC       binding protein 49 (RCN2), a protein localized in the lumen of
CC       endoplasmic reticulum (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:16135698}.
CC   -!- FUNCTION: Monomer (beta chain): Snake venom phospholipase A2 homolog
CC       that is neither toxic nor enzymatically active (PubMed:16135698). Does
CC       not bind calcium (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:16135698}.
CC   -!- SUBUNIT: Heterotrimer of alpha, beta, and gamma chains; non-covalently
CC       linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=13242; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16135698};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DKT9; -.
DR   SMR; P0DKT9; -.
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:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
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   Direct protein sequencing; Disulfide bond; Secreted.
FT   CHAIN           1..>40
FT                   /note="Neutral phospholipase A2 homolog cannitoxin beta
FT                   chain 2"
FT                   /id="PRO_0000420856"
FT   DISULFID        11..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         40
SQ   SEQUENCE   40 AA;  4473 MW;  B4B2BE65F99AE57E CRC64;
     NLVQFGFMIE CAIRNRQPAL DFMNYGCYCG TVGRGTPVDD