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3L2A_BUNCE
ID   3L2A_BUNCE              Reviewed;          76 AA.
AC   D2N116;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Alpha-delta-bungarotoxin-4;
DE            Short=Alpha-delta-Bgt-4;
DE   Flags: Precursor; Fragment;
OS   Bungarus caeruleus (Indian krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=132961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Skin;
RA   Kuch U.;
RT   "Molecular evolution of alpha-bungarotoxins.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Monomer in solution, homodimer in crystal state.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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   EMBL; AM421984; CAM11302.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2N116; -.
DR   SMR; D2N116; -.
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   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          <1..2
FT                   /evidence="ECO:0000250"
FT   CHAIN           3..76
FT                   /note="Alpha-delta-bungarotoxin-4"
FT                   /id="PRO_5000559786"
FT   DISULFID        5..25
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..67
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   76 AA;  8306 MW;  AB5387AE756ABB59 CRC64;
     YTLLCHTTST SPISTVTCPS GENLCYTKMW CDAFCSSRGK VIELGCVATC PQPKPYEEVT
     CCSTDKCNPH PKQRPG
 
 
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