ID   3L213_DRYCN             Reviewed;         108 AA.
AC   F8J2B3;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Long neurotoxin 13;
DE            Short=LNTX-13;
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 with high affinity to muscular (alpha-1/CHRNA1) and
CC       neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and
CC       inhibits acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular and neuronal transmission.
CC       {ECO:0000250|UniProtKB:P60615}.
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. Long-chain
CC       subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   EMBL; FJ481928; ACQ90251.1; -; mRNA.
DR   AlphaFoldDB; F8J2B3; -.
DR   SMR; F8J2B3; -.
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..108
FT                   /note="Long neurotoxin 13"
FT                   /id="PRO_0000425527"
FT   DISULFID        24..42
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..52
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..84
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   108 AA;  12242 MW;  6793C4FB4C48141E CRC64;
     MKTLLLTLVV VTIVCLDLAY TRKCYKTHPY KSEPCASGEN LCYTKTWCDF RCSQLGKAVE
     LGCAATCPTT KPYEEVTCCS TDDCNRFPNW ERPRPRPRGL LSSIMDHP