ID   3S11B_BUNFA             Reviewed;          25 AA.
AC   C0HJI9;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Alpha-elapitoxin-Bf1b {ECO:0000303|PubMed:24440452};
DE            Short=Alpha-EPTX-Bf1b;
DE   Flags: Fragment;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:24440452};
RX   PubMed=24440452; DOI=10.1016/j.bcp.2014.01.004;
RA   Rusmili M.R., Tee T.Y., Mustafa M.R., Othman I., Hodgson W.C.;
RT   "Isolation and characterization of alpha-elapitoxin-Bf1b, a postsynaptic
RT   neurotoxin from Malaysian Bungarus fasciatus venom.";
RL   Biochem. Pharmacol. 88:229-236(2014).
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:24440452}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24440452}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24440452}.
CC   -!- MASS SPECTROMETRY: Mass=6982.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:24440452};
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   AlphaFoldDB; C0HJI9; -.
DR   SMR; C0HJI9; -.
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   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   SUPFAM; SSF57302; SSF57302; 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..>25
FT                   /note="Alpha-elapitoxin-Bf1b"
FT                   /evidence="ECO:0000269|PubMed:24440452"
FT                   /id="PRO_0000429398"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:P60775"
FT   NON_TER         25
FT                   /evidence="ECO:0000303|PubMed:24440452"
SQ   SEQUENCE   25 AA;  2831 MW;  6AA857B1538BD47A CRC64;
     RICLNQQSSE PQTTEICPDG EDTCY