ID   3S11H_OPHHA             Reviewed;          83 AA.
AC   Q69CJ8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Weak toxin DE-1 homolog 1;
DE            Short=WTX DE-1 homolog 1;
DE   Flags: Precursor;
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17616557; DOI=10.1096/fj.07-8658com;
RA   Rajagopalan N., Pung Y.F., Zhu Y.Z., Wong P.T.H., Kumar P.P., Kini R.M.;
RT   "Beta-cardiotoxin: a new three-finger toxin from Ophiophagus hannah (king
RT   cobra) venom with beta-blocker activity.";
RL   FASEB J. 21:3685-3695(2007).
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:0000250}.
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}.
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DR   EMBL; AY354200; AAR10442.1; -; mRNA.
DR   PDB; 5XWE; X-ray; 1.80 A; A/B=1-83.
DR   PDBsum; 5XWE; -.
DR   AlphaFoldDB; Q69CJ8; -.
DR   SMR; Q69CJ8; -.
DR   TopDownProteomics; Q69CJ8; -.
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   3D-structure; 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:0000255"
FT   CHAIN           22..83
FT                   /note="Weak toxin DE-1 homolog 1"
FT                   /id="PRO_0000318905"
FT   DISULFID        24..45
FT                   /evidence="ECO:0007744|PDB:5XWE"
FT   DISULFID        38..62
FT                   /evidence="ECO:0007744|PDB:5XWE"
FT   DISULFID        64..75
FT                   /evidence="ECO:0007744|PDB:5XWE"
FT   DISULFID        76..81
FT                   /evidence="ECO:0007744|PDB:5XWE"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:5XWE"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:5XWE"
FT   STRAND          45..49
FT                   /evidence="ECO:0007829|PDB:5XWE"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:5XWE"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:5XWE"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:5XWE"
SQ   SEQUENCE   83 AA;  9387 MW;  AFCD245753354BFD CRC64;
     MKPVLLTLVV VTIVCLDLGY TRICLKQEPF QPETTTTCPE GEDACYNLFW SDHSEIKIEM
     GCGCPKTEPY TNLYCCKIDS CNK