3NO25_WALAE
ID 3NO25_WALAE Reviewed; 86 AA.
AC C1IC49;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Three finger toxin W-V {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], PROTEIN SEQUENCE OF 22-37, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and 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 FUNCTION, AND TOXIC DOSE.
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: Three-finger toxin that binds and inhibits the muscular
CC nicotinic acetylcholine receptor (nAChR). The neuromuscular block is
CC irreversible in chick biventer cervicis, but partially reversible in
CC the rat diaphragm preparation. {ECO:0000269|PubMed:960110}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18405934}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=7400; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18405934};
CC -!- TOXIC DOSE: LD(50) is 0.2 mg/kg by intraperitoneal injection in mice.
CC {ECO:0000269|PubMed:960110}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Orphan group II sub-subfamily. {ECO:0000305}.
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DR EMBL; EU196557; ABX82866.1; -; mRNA.
DR AlphaFoldDB; C1IC49; -.
DR SMR; C1IC49; -.
DR PRIDE; C1IC49; -.
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:18405934"
FT CHAIN 22..86
FT /note="Three finger toxin W-V"
FT /evidence="ECO:0000305|PubMed:18405934"
FT /id="PRO_0000419226"
FT DISULFID 24..45
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 27..32
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 38..63
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 67..78
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 79..84
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
SQ SEQUENCE 86 AA; 9715 MW; D1C2C67C3B993249 CRC64;
MKTLLLTLVL VTIVCLDLGY TLTCLICPKK YCNQVHTCRN GENLCIKTFY EGNLLGKQFK
RGCAATCPEA RPREIVECCS RDKCNH
