ID   3L21_PSETE              Reviewed;          89 AA.
AC   A8HDK6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Long neurotoxin 1;
DE            Short=LNTX-1;
DE   Flags: Precursor;
OS   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX   NCBI_TaxID=8673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=17906946; DOI=10.1007/s00018-007-7352-z;
RA   St Pierre L., Fischer H., Adams D.J., Schenning M., Lavidis N.,
RA   de Jersey J., Masci P.P., Lavin M.F.;
RT   "Distinct activities of novel neurotoxins from Australian venomous snakes
RT   for nicotinic acetylcholine receptors.";
RL   Cell. Mol. Life Sci. 64:2829-2840(2007).
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 (By similarity),
CC       thereby impairing neuromuscular and neuronal transmission
CC       (PubMed:17906946). {ECO:0000250|UniProtKB:P60615,
CC       ECO:0000269|PubMed:17906946}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Has the length of long neurotoxins, but only 4 disulfide
CC       bonds, as short neurotoxins. {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; DQ917511; ABK63540.1; -; mRNA.
DR   AlphaFoldDB; A8HDK6; -.
DR   SMR; A8HDK6; -.
DR   Proteomes; UP000472273; Unplaced.
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   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
KW   Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..89
FT                   /note="Long neurotoxin 1"
FT                   /id="PRO_5000279919"
FT   DISULFID        24..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..80
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   89 AA;  9882 MW;  7FD8F34947DE6E33 CRC64;
     MKTLLLTLVV VTIVCLDLGD SLICYLDFSV PHTCAPGEKL CYTRTWNDGR GTRIERGCAA
     TCPIPKKPEI HVTCCSTDRC NPHPKQKPH