3L21V_BUNMU
ID 3L21V_BUNMU Reviewed; 95 AA.
AC P60616; P01378; Q90WK0; Q9PRI7; Q9W726; Q9W797; Q9YI08;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Alpha-bungarotoxin isoform V31;
DE Short=Alpha-BTX V31;
DE Short=Alpha-Bgt(V31);
DE Short=BGTX V31;
DE AltName: Full=Long neurotoxin 1;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Liver, and Venom gland;
RX PubMed=10497260; DOI=10.1093/nar/27.20.3970;
RA Chang L.-S., Lin S.-K., Huang H.-B., Hsiao M.;
RT "Genetic organization of alpha-bungarotoxins from Bungarus multicinctus
RT (Taiwan banded krait): evidence showing that the production of alpha-
RT bungarotoxin isotoxins is not derived from edited mRNAs.";
RL Nucleic Acids Res. 27:3970-3975(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Qian Y.C., Fang C.Y., Gong Y., Yang S.;
RT "Molecular cloning of neurotoxin-like proteins from Bungarus multicinctus
RT multicinctus.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 22-95, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=3401449; DOI=10.1021/bi00408a018;
RA Kosen P.A., Finer-Moore J., McCarthy M.P., Basus V.J.;
RT "Structural studies of alpha-bungarotoxin. 3. Corrections in the primary
RT sequence and X-ray structure and characterization of an isotoxic alpha-
RT bungarotoxin.";
RL Biochemistry 27:2775-2781(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-95.
RC TISSUE=Venom gland;
RX PubMed=9837992; DOI=10.1093/nar/26.24.5624;
RA Liu L.-F., Chang C.-C., Liau M.-Y., Kuo K.-W.;
RT "Genetic characterization of the mRNAs encoding alpha-bungarotoxin:
RT isoforms and RNA editing in Bungarus multicinctus gland cells.";
RL Nucleic Acids Res. 26:5624-5629(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-95 IN COMPLEX WITH A 13-RESIDUE
RP PEPTIDE HOMOLOGOUS TO THE BINDING REGION OF THE ALPHA SUBUNIT OF
RP ACETYLCHOLINE RECEPTOR, AND DISULFIDE BONDS.
RX PubMed=11683996; DOI=10.1016/s0896-6273(01)00461-5;
RA Harel M., Kasher R., Nicolas A., Guss J.M., Balass M., Fridkin M.,
RA Smit A.B., Brejc K., Sixma T.K., Katchalski-Katzir E., Sussman J.L.,
RA Fuchs S.;
RT "The binding site of acetylcholine receptor as visualized in the X-ray
RT structure of a complex between alpha-bungarotoxin and a mimotope peptide.";
RL Neuron 32:265-275(2001).
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. {ECO:0000250|UniProtKB:P60615,
CC ECO:0000269|PubMed:10497260}.
CC -!- SUBUNIT: Monomer in solution, homodimer in crystal state.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P60616; Q9UGM1: CHRNA9; Xeno; NbExp=2; IntAct=EBI-16123259, EBI-9008641;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3401449}.
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}.
CC -!- CAUTION: PubMed:9837992 indicates that a number of mRNA with sequence
CC conflict(s) are produced by RNA editing. This seems not to be the case
CC as discussed in PubMed:10497260. {ECO:0000305}.
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DR EMBL; Y17693; CAB51843.1; -; Genomic_DNA.
DR EMBL; Y17057; CAB51841.1; -; mRNA.
DR EMBL; AJ007766; CAB50692.1; -; mRNA.
DR EMBL; AF142323; AAD41805.1; -; mRNA.
DR EMBL; AF056414; AAC83995.1; -; mRNA.
DR EMBL; AF056417; AAC83998.1; -; mRNA.
DR PDB; 1HC9; X-ray; 1.80 A; A=22-95.
DR PDB; 2QC1; X-ray; 1.94 A; A=22-95.
DR PDB; 4HQP; X-ray; 3.51 A; F/G/H/I/J=22-94.
DR PDB; 4UY2; X-ray; 2.70 A; C/D=22-95.
DR PDB; 5HBT; X-ray; 2.61 A; A=22-95.
DR PDB; 5HBV; X-ray; 2.70 A; A=22-95.
DR PDB; 7KOO; EM; 3.00 A; F/G/H/I/J=22-92.
DR PDBsum; 1HC9; -.
DR PDBsum; 2QC1; -.
DR PDBsum; 4HQP; -.
DR PDBsum; 4UY2; -.
DR PDBsum; 5HBT; -.
DR PDBsum; 5HBV; -.
DR PDBsum; 7KOO; -.
DR AlphaFoldDB; P60616; -.
DR BMRB; P60616; -.
DR PCDDB; P60616; -.
DR SMR; P60616; -.
DR DIP; DIP-61054N; -.
DR IntAct; P60616; 1.
DR EvolutionaryTrace; P60616; -.
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 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3401449"
FT CHAIN 22..95
FT /note="Alpha-bungarotoxin isoform V31"
FT /id="PRO_0000035407"
FT DISULFID 24..44
FT /evidence="ECO:0000269|PubMed:11683996"
FT DISULFID 37..65
FT /evidence="ECO:0000269|PubMed:11683996"
FT DISULFID 50..54
FT /evidence="ECO:0000269|PubMed:11683996"
FT DISULFID 69..80
FT /evidence="ECO:0000269|PubMed:11683996"
FT DISULFID 81..86
FT /evidence="ECO:0000269|PubMed:11683996"
FT CONFLICT 1..2
FT /note="MK -> MMT (in Ref. 3; AAD41805)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="F -> S (in Ref. 5; AAC83995)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="K -> R (in Ref. 3; AAD41805)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1HC9"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1HC9"
SQ SEQUENCE 95 AA; 10313 MW; 589B266798319EE4 CRC64;
MKTLLLTLVV VTIVCLDLGY TIVCHTTATS PISAVTCPPG ENLCYRKMWC DVFCSSRGKV
VELGCAATCP SKKPYEEVTC CSTDKCNPHP KQRPG
