ID   3S11_HEMHA              Reviewed;          61 AA.
AC   P01425;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Short neurotoxin 1;
DE   AltName: Full=Toxin II;
OS   Hemachatus haemachatus (Rinkhals) (Sepedon haemachatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Hemachatus.
OX   NCBI_TaxID=8626;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=5545078; DOI=10.1016/s0021-9258(19)76980-4;
RA   Strydom A.J.C., Botes D.P.;
RT   "Snake venom toxins. Purification, properties, and complete amino acid
RT   sequence of two toxins from Ringhals (Hemachatus haemachatus) venom.";
RL   J. Biol. Chem. 246:1341-1349(1971).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission. {ECO:0000250|UniProtKB:P60775}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:5545078}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 0.11 mg/kg by intravenous injection.
CC       {ECO:0000269|PubMed:5545078}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   PIR; A01694; N1RI1.
DR   AlphaFoldDB; P01425; -.
DR   SMR; P01425; -.
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..61
FT                   /note="Short neurotoxin 1"
FT                   /evidence="ECO:0000269|PubMed:5545078"
FT                   /id="PRO_0000093582"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        3..23
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        17..40
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        42..53
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        54..59
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   61 AA;  6838 MW;  204886FB0BE0056A CRC64;
     LECHNQQSSQ PPTTKSCPGD TNCYNKRWRD HRGTIIERGC GCPTVKPGIN LKCCTTDRCN
     N