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3L22_BUNCA
ID   3L22_BUNCA              Reviewed;          75 AA.
AC   A1IVR9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Alpha-elapitoxin-Bc2b {ECO:0000305};
DE            Short=Alpha-EPTX-Bc2b {ECO:0000305};
DE   AltName: Full=Alpha-delta-Bgt-2 {ECO:0000312|EMBL:CAJ77820.1};
DE   AltName: Full=Alpha/delta-bungarotoxin-2 {ECO:0000303|PubMed:30944155};
DE            Short=Alpha/delta-BgTx-2 {ECO:0000303|PubMed:30944155};
DE   Flags: Precursor; Fragment;
OS   Bungarus candidus (Malayan krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=92438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-37 AND 40-71,
RP   FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=30944155; DOI=10.1042/bcj20180909;
RA   Utkin Y.N., Kuch U., Kasheverov I.E., Lebedev D.S., Cederlund E.,
RA   Molles B.E., Polyak I., Ivanov I.A., Prokopev N.A., Ziganshin R.H.,
RA   Jornvall H., Alvelius G., Chanhome L., Warrell D.A., Mebs D., Bergman T.,
RA   Tsetlin V.I.;
RT   "Novel long-chain neurotoxins from Bungarus candidus distinguish the two
RT   binding sites in muscle-type nicotinic acetylcholine receptors.";
RL   Biochem. J. 476:1285-1302(2019).
CC   -!- FUNCTION: Binds to muscular and neuronal nicotinic acetylcholine
CC       receptor (nAChR) and inhibits acetylcholine from binding to the
CC       receptor, thereby impairing neuromuscular and neuronal transmission
CC       (PubMed:30944155). Blocks muscle type nAChR (PubMed:30944155). Also
CC       binds with high affinity to alpha-7/CHRNA7 nAChRs (By similarity). In
CC       addition, shows a weak inhibition of neuronal alpha-3-beta-2/CHRNA3-
CC       CHRNB2 nAChR (By similarity). Selectively binds to alpha-1-delta
CC       subunit interface of the mouse muscle nicotinic acetylcholine receptor,
CC       with a 10-fold higher affinity for the adult than for the fetal
CC       receptors (By similarity). In vivo, when intraperitoneally injected
CC       into mice, causes flaccid paralysis and respiratory distress, followed
CC       by death within 2-4 hours (By similarity).
CC       {ECO:0000250|UniProtKB:A1IVR8, ECO:0000269|PubMed:30944155}.
CC   -!- SUBUNIT: Monomer in solution, homodimer in crystal state.
CC       {ECO:0000250|UniProtKB:P60615}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A1IVR8}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=8143.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:30944155};
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; AM231682; CAJ77820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1IVR9; -.
DR   SMR; A1IVR9; -.
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; Signal; Toxin.
FT   SIGNAL          <1..2
FT                   /evidence="ECO:0000269|PubMed:30944155"
FT   CHAIN           3..75
FT                   /note="Alpha-elapitoxin-Bc2b"
FT                   /evidence="ECO:0000305|PubMed:30944155"
FT                   /id="PRO_5000189421"
FT   DISULFID        5..24
FT                   /evidence="ECO:0000250|UniProtKB:P60615"
FT   DISULFID        17..45
FT                   /evidence="ECO:0000250|UniProtKB:P60615"
FT   DISULFID        30..34
FT                   /evidence="ECO:0000250|UniProtKB:P60615"
FT   DISULFID        49..60
FT                   /evidence="ECO:0000250|UniProtKB:P60615"
FT   DISULFID        61..66
FT                   /evidence="ECO:0000250|UniProtKB:P60615"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAJ77820.1"
SQ   SEQUENCE   75 AA;  8418 MW;  917333D1B4F96C0B CRC64;
     YTLLCYKTPI PINAETCPPG ENLCYTKMWC DIWCSSRGKV VELGCAATCP SKKPYEEVTC
     CSTDKCNPHP KQRPD
 
 
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