ID   3L21_AUSLA              Reviewed;          96 AA.
AC   B2BRQ5;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Alpha-elapitoxin-Al2b;
DE            Short=Alpha-EPTX-Al2b;
DE   Flags: Precursor;
OS   Austrelaps labialis (Pygmy copperhead) (Denisonia superba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Austrelaps.
OX   NCBI_TaxID=471292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=18307759; DOI=10.1186/1471-2148-8-70;
RA   Doley R., Tram N.N.B., Reza M.A., Kini R.M.;
RT   "Unusual accelerated rate of deletions and insertions in toxin genes in the
RT   venom glands of the pygmy copperhead (Austrelaps labialis) from Kangaroo
RT   island.";
RL   BMC Evol. Biol. 8:70-70(2008).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=20950587; DOI=10.1016/j.bcp.2010.10.004;
RA   Blacklow B., Kornhauser R., Hains P.G., Loiacono R., Escoubas P.,
RA   Graudins A., Nicholson G.M.;
RT   "alpha-Elapitoxin-Aa2a, a long-chain snake alpha-neurotoxin with potent
RT   actions on muscle (alpha1)(2)betagammadelta nicotinic receptors, lacks the
RT   classical high affinity for neuronal alpha7 nicotinic receptors.";
RL   Biochem. Pharmacol. 81:314-325(2011).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-96, FUNCTION, AND SUBCELLULAR LOCATION.
RA   Nicholson G.;
RL   Unpublished observations (APR-2012).
CC   -!- FUNCTION: Potent long-chain postsynaptic neurotoxin. Pseudo-
CC       irreversibly inhibits the nicotinic acetylcholine receptor through
CC       competitive antagonism. {ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
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   EMBL; EU003085; ABX58151.1; -; mRNA.
DR   AlphaFoldDB; B2BRQ5; -.
DR   SMR; B2BRQ5; -.
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; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   Pfam; PF00021; UPAR_LY6; 1.
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; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           22..96
FT                   /note="Alpha-elapitoxin-Al2b"
FT                   /id="PRO_0000417624"
FT   DISULFID        24..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..83
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   96 AA;  10258 MW;  A5F1C98D258BD638 CRC64;
     MKTLLLTLVV VTIVCLDFGG GLICYMGPKT PRTCPPGQNL CYTKTWCDGF CGSRGKVVVL
     GCAATCPTVK PGVDITCCAT DKCNPFPKTK APWERP