ID   3L22E_ACAAN             Reviewed;          79 AA.
AC   P0DKW9;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Alpha-elapitoxin-Aa2e;
DE            Short=Alpha-EPTX-Aa2e;
DE   AltName: Full=Aa el/Aa e2;
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]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=9133710; DOI=10.1016/s0041-0101(96)00159-6;
RA   Tyler M.I., Retson-Yip K.V., Gibson M.K., Barnett D., Howe E., Stocklin R.,
RA   Turnbull R.K., Kuchel T., Mirtschin P.;
RT   "Isolation and amino acid sequence of a new long-chain neurotoxin with two
RT   chromatographic isoforms (Aa el and Ae e2) from the venom of the Australian
RT   death adder (Acanthophis antarcticus).";
RL   Toxicon 35:555-562(1997).
CC   -!- FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1) and
CC       neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and
CC       inhibits acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular and neuronal transmission (By similarity). Produces
CC       paralysis, clear dyspnea and lethality on mice (PubMed:9133710).
CC       {ECO:0000250|UniProtKB:P60615, ECO:0000269|PubMed:9133710}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9133710}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=8752.02; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9133710};
CC   -!- TOXIC DOSE: LD(50) is between 0.05 and 0.20 mg/kg by intraperitoneal
CC       injection into mice. These data should be viewed cautiously since only
CC       a few mice have been injected due to the low amount of toxin available.
CC       {ECO:0000269|PubMed:9133710}.
CC   -!- MISCELLANEOUS: Exists in two forms which are separated by reverse-phase
CC       high-performance liquid chromatography, but which have the same
CC       sequence and molecular weight. The existence of cis and trans isomers
CC       may explain the two different elution peaks (PubMed:9133710).
CC       {ECO:0000305|PubMed:9133710}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC       subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DKW9; -.
DR   SMR; P0DKW9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..79
FT                   /note="Alpha-elapitoxin-Aa2e"
FT                   /id="PRO_0000420999"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..30
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..62
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   79 AA;  8761 MW;  A8B8FB1D1E8D533A CRC64;
     VICYVGYNNP QTCPPGGNVC FTKTWCDARC HQLGKRVEMG CATTCPKVNR GVDIKCCSTD
     KCNPFPKTTP PWKRPRGKP