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
