3S1EB_LATSE
ID 3S1EB_LATSE Reviewed; 83 AA.
AC Q90VW1; P01435;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Erabutoxin b {ECO:0000303|PubMed:4941832};
DE Short=ETXB;
DE Short=Eb {ECO:0000303|PubMed:12957382};
DE AltName: Full=Short neurotoxin 1b;
DE Flags: Precursor;
OS Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda
OS semifasciata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX NCBI_TaxID=8631;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=2602157; DOI=10.1093/nar/17.24.10490;
RA Obara K., Fuse N., Tsuchiya T., Nonomura Y., Menez A., Tamiya T.;
RT "Sequence analysis of a cDNA encoding a erabutoxin b from the sea-snake
RT Laticauda semifasciata.";
RL Nucleic Acids Res. 17:10490-10490(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Kariya Y., Araki S., Agu H., Tamiya T., Tsuchiya T.;
RT "Classification of sea snakes in genus Laticauda by nucleotide sequences
RT encoding short chain neurotoxins.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=12957382; DOI=10.1016/s0378-1119(03)00637-1;
RA Fujimi T.J., Nakajyo T., Nishimura E., Ogura E., Tsuchiya T., Tamiya T.;
RT "Molecular evolution and diversification of snake toxin genes, revealed by
RT analysis of intron sequences.";
RL Gene 313:111-118(2003).
RN [4]
RP PROTEIN SEQUENCE OF 22-83, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4941832; DOI=10.1042/bj1220453;
RA Sato S., Tamiya N.;
RT "The amino acid sequences of erabutoxins, neurotoxic proteins of sea-snake
RT (Laticauda semifasciata) venom.";
RL Biochem. J. 122:453-461(1971).
RN [5]
RP SEQUENCE REVISION, AND VARIANT ARG-80.
RX PubMed=588261; DOI=10.1042/bj1670289;
RA Maeda N., Tamiya N.;
RT "Correction of partial amino acid sequence of erabutoxins.";
RL Biochem. J. 167:289-291(1977).
RN [6]
RP PRELIMINARY PROTEIN SEQUENCE OF 22-83.
RX PubMed=857910; DOI=10.1016/0005-2795(77)90309-9;
RA Tsernoglou D., Petsko G.A., Tu A.T.;
RT "Protein sequencing by computer graphics.";
RL Biochim. Biophys. Acta 491:605-608(1977).
RN [7]
RP FUNCTION.
RX PubMed=7721859; DOI=10.1074/jbc.270.16.9362;
RA Tremeau O., Lemaire C., Drevet P., Pinkasfeld S., Ducancel F.,
RA Boulain J.-C., Menez A.;
RT "Genetic engineering of snake toxins. The functional site of Erabutoxin a,
RT as delineated by site-directed mutagenesis, includes variant residues.";
RL J. Biol. Chem. 270:9362-9369(1995).
RN [8]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=9305882; DOI=10.1074/jbc.272.39.24279;
RA Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P.,
RA Bertrand D., Menez A.;
RT "Only snake curaremimetic toxins with a fifth disulfide bond have high
RT affinity for the neuronal alpha7 nicotinic receptor.";
RL J. Biol. Chem. 272:24279-24286(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-83.
RX PubMed=964372; DOI=10.1016/0014-5793(76)80390-0;
RA Tsernoglou D., Petsko G.A.;
RT "The crystal structure of a post-synaptic neurotoxin from sea snake at 2.2-
RT A resolution.";
RL FEBS Lett. 68:1-4(1976).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 22-83, AND DISULFIDE BONDS.
RX PubMed=683181;
RA Tsernoglou D., Petsko G.A., Hudson R.A.;
RT "Structure and function of snake venom curarimimetic neurotoxins.";
RL Mol. Pharmacol. 14:710-716(1978).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-83, AND DISULFIDE BONDS.
RX PubMed=465091; DOI=10.1016/0006-291x(79)91500-6;
RA Kimball M.R., Sato A., Richardson J.S., Rosen L.S., Low B.W.;
RT "Molecular conformation of erabutoxin b; atomic coordinates at 2.5-A
RT resolution.";
RL Biochem. Biophys. Res. Commun. 88:950-959(1979).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 22-83, AND DISULFIDE BONDS.
RX PubMed=2431905; DOI=10.1111/j.1432-1033.1986.tb10481.x;
RA Low B.W., Corfield P.W.;
RT "Erabutoxin b. Structure/function relationships following initial protein
RT refinement at 0.140-nm resolution.";
RL Eur. J. Biochem. 161:579-587(1986).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-83, AND DISULFIDE BONDS.
RX PubMed=1418823; DOI=10.1107/s010876819200096x;
RA Saludjian P., Prange T., Navaza J., Menez R., Guilloteau J.P.,
RA Ries-Kautt M., Ducruix A.;
RT "Structure determination of a dimeric form of erabutoxin-b, crystallized
RT from a thiocyanate solution.";
RL Acta Crystallogr. B 48:520-531(1992).
RN [14]
RP STRUCTURE BY NMR OF 22-83, AND DISULFIDE BONDS.
RX PubMed=8027999; DOI=10.1006/jmbi.1994.1429;
RA Hatanaka H., Oka M., Kohda D., Tate S., Suda A., Tamiya N., Inagaki F.;
RT "Tertiary structure of erabutoxin b in aqueous solution as elucidated by
RT two-dimensional nuclear magnetic resonance.";
RL J. Mol. Biol. 240:155-166(1994).
CC -!- FUNCTION: Binds with high affinity to muscular nicotinic acetylcholine
CC receptors (nAChRs) (tested on Torpedo marmorata, Kd=0.07 nM), and with
CC low affinity to neuronal alpha-7/CHRNA7 nAChRs (tested on chimeric
CC alpha-7/CHRNA7, Kd=22 uM) and inhibit acetylcholine from binding to the
CC receptor, thereby impairing neuromuscular transmission
CC (PubMed:7721859). Produces peripheral paralysis by blocking
CC neuromuscular transmission at the postsynaptic site.
CC {ECO:0000269|PubMed:9305882}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4941832}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:4941832}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR EMBL; X16950; CAA34824.1; -; mRNA.
DR EMBL; AB017929; BAA75749.1; -; mRNA.
DR EMBL; AB017930; BAA75750.1; -; mRNA.
DR EMBL; AB017931; BAA75751.1; -; mRNA.
DR EMBL; AB098528; BAC78201.1; -; Genomic_DNA.
DR EMBL; AB098529; BAC78202.1; -; Genomic_DNA.
DR PIR; S06931; S06931.
DR PDB; 1ERA; NMR; -; A=22-83.
DR PDB; 1FRA; NMR; -; A=22-83.
DR PDB; 1NXB; X-ray; 1.38 A; A=22-83.
DR PDB; 3EBX; X-ray; 1.40 A; A=22-83.
DR PDB; 6EBX; X-ray; 1.70 A; A/B=22-83.
DR PDBsum; 1ERA; -.
DR PDBsum; 1FRA; -.
DR PDBsum; 1NXB; -.
DR PDBsum; 3EBX; -.
DR PDBsum; 6EBX; -.
DR AlphaFoldDB; Q90VW1; -.
DR BMRB; Q90VW1; -.
DR SMR; Q90VW1; -.
DR EvolutionaryTrace; Q90VW1; -.
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;
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:4941832"
FT CHAIN 22..83
FT /note="Erabutoxin b"
FT /evidence="ECO:0000269|PubMed:4941832"
FT /id="PRO_0000035447"
FT REGION 24..38
FT /note="Loop I"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT REGION 39..44
FT /note="Stretch between loop I and loop II"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT REGION 45..62
FT /note="Loop II"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT REGION 64..75
FT /note="Loop III"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 27
FT /note="Moderately important residue for binding to
FT acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 28
FT /note="Very important residue for binding to acetylcholine
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 29
FT /note="Key residue for binding to acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 30
FT /note="Moderately important residue for binding to
FT acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 31
FT /note="Key residue for binding to acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 46
FT /note="Moderately important residue for binding to
FT acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 48
FT /note="Key residue for binding to acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 50
FT /note="Very important residue for binding to acetylcholine
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 52
FT /note="Very important residue for binding to acetylcholine
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 53
FT /note="Moderately important residue for binding to
FT acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 54
FT /note="Key residue for binding to acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 55
FT /note="Moderately important residue for binding to
FT acetylcholine receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 57
FT /note="Very important residue for binding to acetylcholine
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 59
FT /note="Very important residue for binding to acetylcholine
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT SITE 68
FT /note="Very important residue for binding to acetylcholine
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P60775"
FT DISULFID 24..45
FT /evidence="ECO:0000269|PubMed:1418823,
FT ECO:0000269|PubMed:2431905, ECO:0000269|PubMed:465091,
FT ECO:0000269|PubMed:683181, ECO:0000269|PubMed:8027999,
FT ECO:0000312|PDB:1ERA, ECO:0000312|PDB:1FRA,
FT ECO:0000312|PDB:1NXB, ECO:0000312|PDB:3EBX"
FT DISULFID 38..62
FT /evidence="ECO:0000269|PubMed:1418823,
FT ECO:0000269|PubMed:2431905, ECO:0000269|PubMed:465091,
FT ECO:0000269|PubMed:683181, ECO:0000269|PubMed:8027999,
FT ECO:0000312|PDB:1ERA, ECO:0000312|PDB:1FRA,
FT ECO:0000312|PDB:1NXB, ECO:0000312|PDB:3EBX"
FT DISULFID 64..75
FT /evidence="ECO:0000269|PubMed:1418823,
FT ECO:0000269|PubMed:2431905, ECO:0000269|PubMed:465091,
FT ECO:0000269|PubMed:683181, ECO:0000269|PubMed:8027999,
FT ECO:0000312|PDB:1ERA, ECO:0000312|PDB:1FRA,
FT ECO:0000312|PDB:1NXB, ECO:0000312|PDB:3EBX"
FT DISULFID 76..81
FT /evidence="ECO:0000269|PubMed:1418823,
FT ECO:0000269|PubMed:2431905, ECO:0000269|PubMed:465091,
FT ECO:0000269|PubMed:683181, ECO:0000269|PubMed:8027999,
FT ECO:0000312|PDB:1ERA, ECO:0000312|PDB:1FRA,
FT ECO:0000312|PDB:1NXB, ECO:0000312|PDB:3EBX"
FT VARIANT 80
FT /note="V -> R (may be a real difference between the
FT Philippine and Japanese populations)"
FT /evidence="ECO:0000269|PubMed:588261"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1NXB"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1ERA"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1NXB"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1NXB"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1NXB"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1NXB"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1NXB"
SQ SEQUENCE 83 AA; 9160 MW; BBB499DA36BE50E4 CRC64;
MKTLLLTLVV VTIVCLDLGY TRICFNHQSS QPQTTKTCSP GESSCYHKQW SDFRGTIIER
GCGCPTVKPG IKLSCCESEV CNN
