3NO5I_BUNMU
ID 3NO5I_BUNMU Reviewed; 89 AA.
AC Q9YGJ0; Q9W796;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Gamma-bungarotoxin;
DE AltName: Full=Long neurotoxin homolog NTL2I;
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=9844743; DOI=10.1080/15216549800204362;
RA Qian Y.-C., Fan C.-Y., Gong Y., Yang S.-L.;
RT "cDNA cloning and sequence analysis of six neurotoxin-like proteins from
RT Chinese continental banded krait.";
RL Biochem. Mol. Biol. Int. 46:821-828(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Cai Q., He Z., Gong Y., Yang S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=12168693; DOI=10.1023/a:1019760401692;
RA Chang L.-S., Chung C., Wu B.-N., Yang C.-C.;
RT "Characterization and gene organization of Taiwan banded krait (Bungarus
RT multicinctus) gamma-bungarotoxin.";
RL J. Protein Chem. 21:223-229(2002).
RN [4]
RP PROTEIN SEQUENCE OF 22-89, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10082161; DOI=10.1016/s0041-0101(98)00199-8;
RA Aird S.D., Womble G.C., Yates J.R. III, Griffin P.R.;
RT "Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin
RT from venom of Bungarus multicinctus.";
RL Toxicon 37:609-625(1999).
RN [5]
RP STRUCTURE BY NMR OF 22-89, AND DISULFIDE BOND.
RX PubMed=15390258; DOI=10.1002/prot.20269;
RA Shiu J.-H., Chen C.-Y., Chang L.-S., Chen Y.-C., Chen Y.-C., Lo Y.-H.,
RA Liu Y.-C., Chuang W.-J.;
RT "Solution structure of gamma-bungarotoxin: the functional significance of
RT amino acid residues flanking the RGD motif in integrin binding.";
RL Proteins 57:839-849(2004).
CC -!- FUNCTION: Exhibits M2 muscarinic acetylcholine receptor (CHRM2)-
CC blocking activity, but has a weak binding activity toward nicotinic
CC AChR. Moreover, it inhibits collagen-induced platelet aggregation.
CC {ECO:0000269|PubMed:12168693}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10082161}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 0.15 mg/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:10082161}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Orphan group V sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ006135; CAA06885.1; -; mRNA.
DR EMBL; AF142324; AAD41806.1; -; mRNA.
DR EMBL; AJ416991; CAD01082.1; -; Genomic_DNA.
DR PIR; A59187; A59187.
DR PDB; 1MR6; NMR; -; A=22-89.
DR PDBsum; 1MR6; -.
DR AlphaFoldDB; Q9YGJ0; -.
DR SMR; Q9YGJ0; -.
DR EvolutionaryTrace; Q9YGJ0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; G-protein coupled acetylcholine receptor impairing toxin;
KW G-protein coupled receptor impairing toxin; Hemostasis impairing toxin;
KW Neurotoxin; Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10082161"
FT CHAIN 22..89
FT /note="Gamma-bungarotoxin"
FT /evidence="ECO:0000269|PubMed:10082161"
FT /id="PRO_0000035425"
FT MOTIF 54..56
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00293"
FT DISULFID 24..45
FT /evidence="ECO:0000269|PubMed:15390258,
FT ECO:0000312|PDB:1MR6"
FT DISULFID 27..32
FT /evidence="ECO:0000269|PubMed:15390258,
FT ECO:0000312|PDB:1MR6"
FT DISULFID 38..66
FT /evidence="ECO:0000269|PubMed:15390258,
FT ECO:0000312|PDB:1MR6"
FT DISULFID 70..81
FT /evidence="ECO:0000269|PubMed:15390258,
FT ECO:0000312|PDB:1MR6"
FT DISULFID 82..87
FT /evidence="ECO:0000269|PubMed:15390258,
FT ECO:0000312|PDB:1MR6"
FT CONFLICT 2
FT /note="K -> E (in Ref. 2; AAD41806)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1MR6"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1MR6"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1MR6"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1MR6"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1MR6"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1MR6"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1MR6"
SQ SEQUENCE 89 AA; 9826 MW; 368E86E7BA19D49C CRC64;
MKTLLLTLVV VTIVCLDLGY TMQCKTCSFY TCPNSETCPD GKNICVKRSW TAVRGDGPKR
EIRRECAATC PPSKLGLTVF CCTTDNCNH
