ID   3NX5_MICSU              Reviewed;          64 AA.
AC   P86099;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Long neurotoxin MS5 {ECO:0000303|PubMed:18384102};
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. Very weak inhibitor of the
CC       endogenous nicotinic acetylcholine receptors (nAChR) in the human
CC       rhabdomyosarcoma TE 671 cell line. This neurotoxin is lethal to
CC       zebrafish by injection at the back of the dorsolateral region, but is
CC       not toxic to mice by intraperitoneal injection.
CC       {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. Ancestral
CC       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   AlphaFoldDB; P86099; -.
DR   SMR; P86099; -.
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   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..64
FT                   /note="Long neurotoxin MS5"
FT                   /evidence="ECO:0000269|PubMed:18384102"
FT                   /id="PRO_0000371721"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        6..11
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        17..41
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        45..57
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250|UniProtKB:P81783"
SQ   SEQUENCE   64 AA;  7189 MW;  90B14A522CB4D7F0 CRC64;
     LTCHTCPYNT CANSETCPAG KNICYQKKWE EHRGERIERS CVANCPEFES SHTSLLCCTT
     ANCD