ID   3SX_MICSU               Reviewed;          58 AA.
AC   P86094;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Short neurotoxin MS11 {ECO:0000303|PubMed:18384102};
DE   AltName: Full=Three-finger toxin;
DE            Short=3FTx;
OS   Micrurus surinamensis (Surinam coral snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX   NCBI_TaxID=129470;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=18384102; DOI=10.1002/pmic.200700668;
RA   Olamendi-Portugal T., Batista C.V.F., Restano-Cassulini R., Pando V.,
RA   Villa-Hernandez O., Zavaleta-Martinez-Vargas A., Salas-Arruz M.C.,
RA   Rodriguez de la Vega R.C., Becerril B., Possani L.D.;
RT   "Proteomic analysis of the venom from the fish eating coral snake Micrurus
RT   surinamensis: novel toxins, their function and phylogeny.";
RL   Proteomics 8:1919-1932(2008).
CC   -!- FUNCTION: Produces peripheral paralysis by blocking neuromuscular
CC       transmission at the postsynaptic site. Binds to and inhibits the
CC       endogenous nicotinic acetylcholine receptors (nAChR) in the human
CC       rhabdomyosarcoma TE 671 cell line with an IC(50) of 266 mM. Not toxic
CC       to mice by intraperitoneal injection or to zebrafish by injection at
CC       the back dorsolateral region. {ECO:0000269|PubMed:18384102}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18384102}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P86094; -.
DR   SMR; P86094; -.
DR   TCDB; 8.B.23.1.4; the mambalgin (mambalgin) family.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044504; P:modulation of receptor activity in another organism; IDA:UniProtKB.
DR   Gene3D; 2.10.60.10; -; 1.
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="Short neurotoxin MS11"
FT                   /evidence="ECO:0000269|PubMed:18384102"
FT                   /id="PRO_0000371724"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        13..38
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        42..50
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        51..56
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
SQ   SEQUENCE   58 AA;  6678 MW;  523512C3402355F8 CRC64;
     LKCYGIFRKI MTCPQGQNIC EKFAYSPMHN GWMYSWGCTS NCHKGPLDKC CSTDLCNY