ID   3S12A_DRYCN             Reviewed;          81 AA.
AC   F8J2G3;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Short neurotoxin 2;
DE            Short=SNTX-2;
DE   Flags: Precursor;
OS   Drysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Drysdalia.
OX   NCBI_TaxID=66186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21133350; DOI=10.1021/pr1008916;
RA   Chatrath S.T., Chapeaurouge A., Lin Q., Lim T.K., Dunstan N., Mirtschin P.,
RA   Kumar P.P., Kini R.M.;
RT   "Identification of novel proteins from the venom of a cryptic snake
RT   Drysdalia coronoides by a combined transcriptomics and proteomics
RT   approach.";
RL   J. Proteome Res. 10:739-750(2011).
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:21133350}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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   EMBL; FJ752481; ACR78503.1; -; mRNA.
DR   AlphaFoldDB; F8J2G3; -.
DR   SMR; F8J2G3; -.
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; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..81
FT                   /note="Short neurotoxin 2"
FT                   /id="PRO_0000425519"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        38..60
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        62..73
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        74..79
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   81 AA;  8981 MW;  F980C857ABF230F2 CRC64;
     MKTLLLTLVV VTIVCLDLGY TMTCYNQQSS QPQTTTTCAE SSCYKKTWRD HRGTIIERGC
     GCPTVKPGIQ RVCCATDKCN N