ID   PA2HG_OXYSA             Reviewed;          30 AA.
AC   P0DKU0;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Acidic phospholipase A2 homolog cannitoxin gamma chain;
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, MASS SPECTROMETRY, AND PTM.
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 (gamma 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   -!- PTM: Glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=17762; 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; P0DKU0; -.
DR   SMR; P0DKU0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted.
FT   CHAIN           1..>30
FT                   /note="Acidic phospholipase A2 homolog cannitoxin gamma
FT                   chain"
FT                   /id="PRO_0000420857"
FT   DISULFID        19..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000305"
FT   UNSURE          26..30
FT                   /note="Assigned by comparison with orthologs"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3388 MW;  F7F157919D09A4A2 CRC64;
     SEIPQPSLDF EQFSNMIQCT IPPGEECLAY