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Alpha-elapitoxin-Aa2e (Alpha-EPTX-Aa2e) (Aa el/Aa e2)

 3L22E_ACAAN             Reviewed;          79 AA.
P0DKW9;
06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
06-FEB-2013, sequence version 1.
22-NOV-2017, entry version 21.
RecName: Full=Alpha-elapitoxin-Aa2e;
Short=Alpha-EPTX-Aa2e;
AltName: Full=Aa el/Aa e2;
Acanthophis antarcticus (Common death adder).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae;
Acanthophis.
NCBI_TaxID=8605;
[1]
PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
AND LETHAL DOSE.
TISSUE=Venom;
PubMed=9133710; DOI=10.1016/S0041-0101(96)00159-6;
Tyler M.I., Retson-Yip K.V., Gibson M.K., Barnett D., Howe E.,
Stocklin R., Turnbull R.K., Kuchel T., Mirtschin P.;
"Isolation and amino acid sequence of a new long-chain neurotoxin with
two chromatographic isoforms (Aa el and Ae e2) from the venom of the
Australian death adder (Acanthophis antarcticus).";
Toxicon 35:555-562(1997).
-!- FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1)
and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor
(nAChR) and inhibits acetylcholine from binding to the receptor,
thereby impairing neuromuscular and neuronal transmission (By
similarity). Produces paralysis, clear dyspnea and lethality on
mice (PubMed:9133710). {ECO:0000250|UniProtKB:P60615,
ECO:0000269|PubMed:9133710}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9133710}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- MASS SPECTROMETRY: Mass=8752.02; Method=Electrospray; Range=1-79;
Evidence={ECO:0000269|PubMed:9133710};
-!- TOXIC DOSE: LD(50) is between 0.05 and 0.20 mg/kg by
intraperitoneal injection into mice. These data should be viewed
cautiously since only a few mice have been injected due to the low
amount of toxin available. {ECO:0000269|PubMed:9133710}.
-!- MISCELLANEOUS: Exists in two forms which are separated by reverse-
phase high-performance liquid chromatography, but which have the
same sequence and molecular weight. The existence of cis and trans
isomers may explain the two different elution peaks
(PubMed:9133710). {ECO:0000305|PubMed:9133710}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-
chain subfamily. Type II alpha-neurotoxin sub-subfamily.
{ECO:0000305}.
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SMR; P0DKW9; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00206; snake_toxin; 1.
InterPro; IPR003571; Snake_3FTx.
InterPro; IPR018354; Snake_toxin_con_site.
InterPro; IPR035076; Toxin/TOLIP.
Pfam; PF00087; Toxin_TOLIP; 1.
PROSITE; PS00272; SNAKE_TOXIN; 1.
1: Evidence at protein level;
Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
Disulfide bond; Ion channel impairing toxin; Neurotoxin;
Postsynaptic neurotoxin; Secreted; Toxin.
CHAIN 1 79 Alpha-elapitoxin-Aa2e.
/FTId=PRO_0000420999.
DISULFID 3 20 {ECO:0000250}.
DISULFID 13 41 {ECO:0000250}.
DISULFID 26 30 {ECO:0000250}.
DISULFID 45 56 {ECO:0000250}.
DISULFID 57 62 {ECO:0000250}.
SEQUENCE 79 AA; 8761 MW; A8B8FB1D1E8D533A CRC64;
VICYVGYNNP QTCPPGGNVC FTKTWCDARC HQLGKRVEMG CATTCPKVNR GVDIKCCSTD
KCNPFPKTTP PWKRPRGKP


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