3L22_DENPO
ID 3L22_DENPO Reviewed; 72 AA.
AC P01397;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Alpha-elapitoxin-Dpp2c;
DE Short=Alpha-EPTX-Dpp2c;
DE AltName: Full=Long neurotoxin 2;
DE AltName: Full=Neurotoxin delta;
DE AltName: Full=Toxin TN2;
OS Dendroaspis polylepis polylepis (Black mamba).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX NCBI_TaxID=8620;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom gland;
RA Strydom D.J.;
RL Thesis (1973), University of Pretoria, South Africa.
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|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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; A01668; N2EP2D.
DR AlphaFoldDB; P01397; -.
DR SMR; P01397; -.
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; Toxin.
FT CHAIN 1..72
FT /note="Alpha-elapitoxin-Dpp2c"
FT /id="PRO_0000093539"
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"
SQ SEQUENCE 72 AA; 7948 MW; 848FFB047D812F5F CRC64;
RTCNKTPSDQ SKICPPGENI CYTKTWCDAW CSQRGKIVEL GCAATCPKVK AGVEIKCCST
DNCNKFKFGK PR