ID   3NX2_MICSU              Reviewed;          64 AA.
AC   P86096;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Long neurotoxin MS2 {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. Not toxic to mice by intraperitoneal
CC       injection or to zebrafish by injection at the back of the dorsolateral
CC       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. Ancestral
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P86096; -.
DR   SMR; P86096; -.
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 MS2"
FT                   /evidence="ECO:0000269|PubMed:18384102"
FT                   /id="PRO_0000371719"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT   DISULFID        6..11
FT                   /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT   DISULFID        17..41
FT                   /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT   DISULFID        45..57
FT                   /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
SQ   SEQUENCE   64 AA;  7309 MW;  69E9E50DF5375EF1 CRC64;
     LTCHTCPYNT CANSETCPAG KNICYQKKWE EHQGERIERR CVANCPKLGS NDKSLLCCRR
     DDCN