ID   3S11_NAJNI              Reviewed;          61 AA.
AC   P68419; P01429;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Short neurotoxin 1;
DE   AltName: Full=Neurotoxin delta;
OS   Naja nivea (Cape cobra) (Coluber niveus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8655;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=4995745; DOI=10.1016/s0021-9258(18)62205-7;
RA   Botes D.P., Strydom D.J., Anderson C.G., Christensen P.A.;
RT   "Snake venom toxins. Purification and properties of three toxins from Naja
RT   nivea (Linnaeus) (Cape cobra) venom and the amino acid sequence of toxin
RT   delta.";
RL   J. Biol. Chem. 246:3132-3139(1971).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4995745}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 0.086 mg/kg by intravenous injection.
CC       {ECO:0000269|PubMed:4995745}.
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; A92084; N1NJ2C.
DR   AlphaFoldDB; P68419; -.
DR   SMR; P68419; -.
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:4995745"
FT                   /id="PRO_0000093605"
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;  6844 MW;  7504536BBE96DE76 CRC64;
     LECHNQQSSQ PPTTKTCPGE TNCYKKRWRD HRGSITERGC GCPSVKKGIE INCCTTDKCN
     N