ID   3S110_DENJA             Reviewed;          58 AA.
AC   P01419;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Toxin S5C10;
OS   Dendroaspis jamesoni kaimosae (Eastern Jameson's mamba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8619;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RX   PubMed=465532; DOI=10.1016/0005-2795(79)90101-6;
RA   Joubert F.J., Taljaard N.;
RT   "Some properties and the complete primary structures of two reduced and S-
RT   carboxymethylated polypeptides (S5C1 and S5C10) from Dendroaspis jamesoni
RT   kaimosae (Jameson's mamba) venom.";
RL   Biochim. Biophys. Acta 579:228-233(1979).
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:465532}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 5.5 mg/kg by intravenous injection.
CC       {ECO:0000269|PubMed:465532}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A01688; N1EP2J.
DR   AlphaFoldDB; P01419; -.
DR   SMR; P01419; -.
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   SUPFAM; SSF57302; SSF57302; 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..58
FT                   /note="Toxin S5C10"
FT                   /evidence="ECO:0000269|PubMed:465532"
FT                   /id="PRO_0000093661"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        17..39
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        41..50
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        51..56
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   58 AA;  6522 MW;  D0B8C3816A68E23E CRC64;
     RICYNHQSNT PATTKSCVEN SCYKSIWADH RGTIIKRGCG CPRVKSKIKC CKSDNCNL