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3S14_WALAE
ID   3S14_WALAE              Reviewed;          83 AA.
AC   C1IC48;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Three-finger toxin W-IV {ECO:0000303|PubMed:960110};
DE   Flags: Precursor;
OS   Walterinnesia aegyptia (Desert black snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Walterinnesia.
OX   NCBI_TaxID=64182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=18405934; DOI=10.1016/j.toxicon.2008.02.012;
RA   Tsai H.-Y., Wang Y.M., Tsai I.-H.;
RT   "Cloning, characterization and phylogenetic analyses of members of three
RT   major venom families from a single specimen of Walterinnesia aegyptia.";
RL   Toxicon 51:1245-1254(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-83.
RC   TISSUE=Venom;
RX   PubMed=9080571; DOI=10.1016/s0041-0101(96)00138-9;
RA   Samejima Y., Aoki-Tomomatsu Y., Yanagisawa M., Mebs D.;
RT   "Amino acid sequence of two neurotoxins from the venom of the Egyptian
RT   black snake (Walterinnesia aegyptia).";
RL   Toxicon 35:151-157(1997).
RN   [3]
RP   FUNCTION, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=960110; DOI=10.1016/0041-0101(76)90023-4;
RA   Lee C.Y., Chen Y.M., Mebs D.;
RT   "Chromatographic separation of the venom of Egyptian black snake
RT   (Walterinnesia aegyptia) and pharmacological characterization of its
RT   components.";
RL   Toxicon 14:275-281(1976).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission. {ECO:0000269|PubMed:960110}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:960110}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 0.14 mg/kg by intraperitoneal injection in mice.
CC       {ECO:0000269|PubMed:960110}.
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; EU196556; ABX82865.1; -; mRNA.
DR   AlphaFoldDB; C1IC48; -.
DR   SMR; C1IC48; -.
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; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:9080571"
FT   CHAIN           22..83
FT                   /note="Three-finger toxin W-IV"
FT                   /evidence="ECO:0000269|PubMed:9080571"
FT                   /id="PRO_0000419225"
FT   DISULFID        24..45
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        38..62
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        64..75
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        76..81
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   83 AA;  9055 MW;  B09FEE8924642C37 CRC64;
     MKTLLLTLVV VTIVCLDLGH TLLCHNQQSS TSPTTTCCSG GESKCYKKRW PTHRGTITER
     GCGCPTVKKG IELHCCTTDQ CNL
 
 
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