ID   3L22_DENVI              Reviewed;          73 AA.
AC   P01395;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Alpha-elapitoxin-Dv2a;
DE            Short=Alpha-EPTX-Dv2a;
DE   AltName: Full=Long neurotoxin 2;
DE   AltName: Full=Toxin I/V;
OS   Dendroaspis viridis (Western green mamba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8621;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=976267; DOI=10.1111/j.1432-1033.1976.tb10832.x;
RA   Bechis G., Granier C., van Rietschoten J., Jover E., Rochat H., Miranda F.;
RT   "Purification of six neurotoxins from the venom of Dendroaspis viridis.
RT   Primary structure of two long toxins.";
RL   Eur. J. Biochem. 68:445-456(1976).
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:976267}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 0.045 mg/kg by subcutaneous injection for variant
CC       I, and 0.08 mg/kg for variant V. {ECO:0000269|PubMed:976267}.
CC   -!- MISCELLANEOUS: The variant I sequence is shown.
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   PIR; A01666; N2EP2V.
DR   AlphaFoldDB; P01395; -.
DR   SMR; P01395; -.
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   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
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; Toxin.
FT   CHAIN           1..73
FT                   /note="Alpha-elapitoxin-Dv2a"
FT                   /id="PRO_0000093542"
FT   DISULFID        3..21
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..42
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..31
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250"
FT   VARIANT         73
FT                   /note="Missing (in variant V)"
SQ   SEQUENCE   73 AA;  8054 MW;  0D7A3BC25B46C63B CRC64;
     RTCYKTPSVK PETCPHGENI CYTETWCDAW CSQRGKRVEL GCAATCPKVK AGVGIKCCST
     DNCNPFPVWN PRG