ID   3L2D_ACAAN              Reviewed;          74 AA.
AC   P34073;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Alpha-elapitoxin-Aa2d;
DE            Short=Alpha-EPTX-Aa2d;
DE   AltName: Full=Acanthophin-D;
DE   AltName: Full=Postsynaptic neurotoxin;
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, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=2158871; DOI=10.1016/0305-0491(90)90246-p;
RA   Sheumack D.D., Spence I., Tyler M.I., Howden M.E.H.;
RT   "The complete amino acid sequence of a post-synaptic neurotoxin isolated
RT   from the venom of the Australian death adder snake Acanthophis
RT   antarcticus.";
RL   Comp. Biochem. Physiol. 95B:45-50(1990).
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.
CC       {ECO:0000250|UniProtKB:P60615}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2158871}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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   PIR; A60518; A60518.
DR   AlphaFoldDB; P34073; -.
DR   SMR; P34073; -.
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..74
FT                   /note="Alpha-elapitoxin-Aa2d"
FT                   /id="PRO_0000093528"
FT   DISULFID        3..21
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..42
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..31
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  8387 MW;  4BC4DA6F38A6D816 CRC64;
     VICYRKYTNN VKTCPDGENV CYTKMWCDGF CTSRGKVVEL GCAATCPIRK PGNEVKCCST
     NKCNHPPKRK KRRP