3NO21_BUNCA
ID 3NO21_BUNCA Reviewed; 86 AA.
AC Q8AY51;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Weak toxin 1 {ECO:0000312|EMBL:AAL30059.1};
DE Flags: Precursor;
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 [MRNA].
RC TISSUE=Venom gland;
RA Tsai I.H., Wang Y.M., Hsu H.Y.;
RT "Structural and functional genomics of Bungarus candidus.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR OF 22-86, AND DISULFIDE BONDS.
RA Vivekanandan S., Jois S.D., Kini R.M., Troncone L.R.P., De Magalhaes L.,
RA Ujikawa G.Y., Ramos A.T.;
RT "NMR solution structure of bungatoxin from Bungarus candidus (Malayan
RT krait) venom.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: Binds with low affinity to muscular (alpha-1-beta-1-delta-
CC epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal
CC (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).
CC {ECO:0000250|UniProtKB:O42255}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Orphan group II sub-subfamily. {ECO:0000305}.
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DR EMBL; AY057877; AAL30059.1; -; mRNA.
DR PDB; 2JQP; NMR; -; A=22-86.
DR PDBsum; 2JQP; -.
DR AlphaFoldDB; Q8AY51; -.
DR BMRB; Q8AY51; -.
DR SMR; Q8AY51; -.
DR EvolutionaryTrace; Q8AY51; -.
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 3D-structure; Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..86
FT /note="Weak toxin 1"
FT /id="PRO_0000316184"
FT DISULFID 24..45
FT /evidence="ECO:0000269|Ref.2, ECO:0000312|PDB:2JQP"
FT DISULFID 27..32
FT /evidence="ECO:0000269|Ref.2, ECO:0000312|PDB:2JQP"
FT DISULFID 38..63
FT /evidence="ECO:0000269|Ref.2, ECO:0000312|PDB:2JQP"
FT DISULFID 67..78
FT /evidence="ECO:0000269|Ref.2, ECO:0000312|PDB:2JQP"
FT DISULFID 79..84
FT /evidence="ECO:0000269|Ref.2, ECO:0000312|PDB:2JQP"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2JQP"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2JQP"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2JQP"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:2JQP"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2JQP"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:2JQP"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:2JQP"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2JQP"
SQ SEQUENCE 86 AA; 9713 MW; 590A59EA8DBC8EB2 CRC64;
MKTLLLTLVV VAIVCLDLGY TLTCLICPEK DCQKVHTCRN EEKICVKRFY DKNQLGWRAQ
RGCAVSCPKA KPNETVQCCS TDKCNK