ID   PA2HC_ACAAN             Reviewed;          20 AA.
AC   P86525;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Phospholipase A2 homolog P-elapitoxin-Aa1a gamma chain;
DE            Short=P-EPTX-Aa1a gamma chain {ECO:0000303|PubMed:20361942};
DE            Short=svPLA2 homolog;
DE   Flags: Fragment;
OS   Acanthophis antarcticus (Common death adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Acanthophis.
OX   NCBI_TaxID=8605;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   STRAIN=New South Wales {ECO:0000269|PubMed:20361942};
RC   TISSUE=Venom {ECO:0000269|PubMed:20361942};
RX   PubMed=20361942; DOI=10.1016/j.bcp.2010.03.030;
RA   Blacklow B., Escoubas P., Nicholson G.M.;
RT   "Characterisation of the heterotrimeric presynaptic phospholipase A(2)
RT   neurotoxin complex from the venom of the common death adder (Acanthophis
RT   antarcticus).";
RL   Biochem. Pharmacol. 80:277-287(2010).
CC   -!- FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) that has
CC       presynaptic neurotoxicity. Inhibits nerve-evoked twitch contractions
CC       but not responses to cholinergic agonists acetylcholine and carbachol
CC       and to depolarizing agonist KCl. Causes a fade in tetanic contractions.
CC       Displays a triphasic mode of action with depression, enhancement and
CC       blockade of neurotransmission. Does not display myotoxic activity such
CC       as changes in baseline muscle tension or inhibition of directly
CC       stimulated muscle twitches. All subunits are necessary for maximum
CC       toxicity. {ECO:0000269|PubMed:20361942}.
CC   -!- FUNCTION: Monomer: the gamma chain has no significant enzymatic
CC       activity and is not toxic by itself. {ECO:0000269|PubMed:20361942}.
CC   -!- SUBUNIT: Heterotrimer of alpha, beta and gamma chains, each related to
CC       PLA2. {ECO:0000269|PubMed:20361942}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20361942}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20361942}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:20361942}.
CC   -!- MASS SPECTROMETRY: Mass=17373; Method=MALDI; Note=glycosylated form.;
CC       Evidence={ECO:0000269|PubMed:20361942};
CC   -!- MASS SPECTROMETRY: Mass=17632; Method=MALDI; Note=glycosylated form.;
CC       Evidence={ECO:0000269|PubMed:20361942};
CC   -!- MASS SPECTROMETRY: Mass=17836; Method=MALDI; Note=glycosylated form.;
CC       Evidence={ECO:0000269|PubMed:20361942};
CC   -!- MISCELLANEOUS: Preincubation of P-elapitoxin-Aa1a with monovalent
CC       antivenom or suramin prevents or delays toxicity, respectively.
CC       Antivenom fails to reverse neurotoxicity when applied at point of 90%
CC       neuromuscular blockade. Treatment of P-elapitoxin-Aa1a with 4-
CC       bromophenacyl bromide drastically reduces enzymatic activity and
CC       toxicity, presumably by alkylating a His residue at the active site.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86525; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>20
FT                   /note="Phospholipase A2 homolog P-elapitoxin-Aa1a gamma
FT                   chain"
FT                   /id="PRO_0000395309"
FT   DISULFID        18..?
FT                   /evidence="ECO:0000250|UniProtKB:Q5G290"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:20361942"
SQ   SEQUENCE   20 AA;  2253 MW;  49DAFC54A46EAED2 CRC64;
     SIPLPSLNFE QFGNMIQCTI