PA2CA_OXYSA
ID PA2CA_OXYSA Reviewed; 20 AA.
AC P0DKT7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Basic phospholipase A2 cannitoxin alpha chain;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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, CATALYTIC ACTIVITY, 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 (alpha chain): Snake venom phospholipase A2 (PLA2)
CC that possesses a low level of presynaptic activity and the same high
CC enzymatic activity than the heterotrimer. PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:16135698}.
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|PubMed:16135698};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
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=13824; 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; P0DKT7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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..>20
FT /note="Basic phospholipase A2 cannitoxin alpha chain"
FT /id="PRO_0000420854"
FT DISULFID 11..?
FT UNSURE 20
FT /note="Assigned by comparison with orthologs"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2382 MW; D8DA7AE2FB7322B9 CRC64;
NLLQFGYMIR CANGRSRPVW
