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Beta-insect excitatory toxin Bj-xtrIT (Bjxtr-IT) (BjxtrIT)

 SIXE_HOTJU              Reviewed;          94 AA.
P56637;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 1.
25-OCT-2017, entry version 95.
RecName: Full=Beta-insect excitatory toxin Bj-xtrIT;
Short=Bjxtr-IT;
Short=BjxtrIT;
Flags: Precursor;
Name=XTRIT;
Hottentotta judaicus (Black scorpion) (Buthotus judaicus).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Scorpiones; Buthida; Buthoidea; Buthidae; Hottentotta.
NCBI_TaxID=6863;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=9753689; DOI=10.1016/S0969-2126(98)00111-7;
Oren D.A., Froy O., Amit E., Kleinberger-Doron N., Gurevitz M.,
Shaanan B.;
"An excitatory scorpion toxin with a distinctive feature: an
additional alpha helix at the C-terminus and its implications for
interaction with insect sodium channels.";
Structure 6:1095-1103(1998).
[2]
PROTEIN SEQUENCE OF 19-48, MASS SPECTROMETRY, PARALYTIC DOSE, AND
MUTAGENESIS.
TISSUE=Venom;
PubMed=10026198; DOI=10.1074/jbc.274.9.5769;
Froy O., Zilberberg N., Gordon D., Turkov M., Gilles N.,
Stankiewicz M., Pelhate M., Loret E., Oren D.A., Shaanan B.,
Gurevitz M.;
"The putative bioactive surface of insect-selective scorpion
excitatory neurotoxins.";
J. Biol. Chem. 274:5769-5776(1999).
[3]
SYNTHESIS OF 19-94, AND MUTAGENESIS.
PubMed=14672947; DOI=10.1074/jbc.M307531200;
Cohen L., Karbat I., Gilles N., Froy O., Corzo G., Angelovici R.,
Gordon D., Gurevitz M.;
"Dissection of the functional surface of an anti-insect excitatory
toxin illuminates a putative 'hot spot' common to all scorpion beta-
toxins affecting Na+ channels.";
J. Biol. Chem. 279:8206-8211(2004).
[4]
SYNTHESIS, MUTAGENESIS OF LYS-19; LYS-20; ASP-26; LYS-30; GLU-33;
GLU-48; LYS-51; GLU-56; 71-GLU--ASP-73; ASP-72; LYS-74; ASP-81;
LYS-84; LYS-85 AND ASP-88, AND SITE.
PubMed=15054090; DOI=10.1096/fj.03-0733com;
Karbat I., Cohen L., Gilles N., Gordon D., Gurevitz M.;
"Conversion of a scorpion toxin agonist into an antagonist highlights
an acidic residue involved in voltage sensor trapping during
activation of neuronal Na+ channels.";
FASEB J. 18:683-689(2004).
[5]
ERRATUM.
Karbat I., Cohen L., Gilles N., Gordon D., Gurevitz M.;
FASEB J. 18:947-947(2004).
-!- FUNCTION: Excitatory insect toxins induce a spastic paralysis.
They bind voltage-independently at site-4 of sodium channels (Nav)
and shift the voltage of activation toward more negative
potentials thereby affecting sodium channel activation and
promoting spontaneous and repetitive firing. This toxin is active
only on insects.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- MASS SPECTROMETRY: Mass=8455; Method=Unknown; Range=19-94;
Evidence={ECO:0000269|PubMed:10026198};
-!- TOXIC DOSE: Both variants Bjxtr-IT.56E and Bjxtr-IT.56K have an
PD(50) of 9.6 ng/100 mg of body weight of blowfly larvae.
{ECO:0000269|PubMed:10026198}.
-!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin
superfamily. Sodium channel inhibitor family. Beta subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ012312; CAA09987.1; -; mRNA.
EMBL; AJ012313; CAA09988.1; -; mRNA.
PDB; 1BCG; X-ray; 2.10 A; A=19-94.
PDB; 4KYP; X-ray; 1.70 A; A/B/C/D=19-94.
PDBsum; 1BCG; -.
PDBsum; 4KYP; -.
ProteinModelPortal; P56637; -.
SMR; P56637; -.
EvolutionaryTrace; P56637; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
Gene3D; 3.30.30.10; -; 1.
InterPro; IPR036574; Scorpion_toxin-like_sf.
InterPro; IPR002061; Scorpion_toxinL/defensin.
Pfam; PF00537; Toxin_3; 1.
SUPFAM; SSF57095; SSF57095; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
Voltage-gated sodium channel impairing toxin.
SIGNAL 1 18 {ECO:0000269|PubMed:10026198}.
CHAIN 19 94 Beta-insect excitatory toxin Bj-xtrIT.
/FTId=PRO_0000035199.
SITE 33 33 May be involved in voltage sensor
trapping upon activation of sodium
channel.
SITE 48 48 May interact with a positively charged
residue of the receptor site.
DISULFID 34 60
DISULFID 45 65
DISULFID 49 67
DISULFID 61 87
VARIANT 56 56 E -> K.
MUTAGEN 19 19 K->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 20 20 K->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 26 26 D->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 30 30 K->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 33 33 E->A: 47.5-fold decrease in toxicity and
little effect on the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 33 33 E->F: 743-fold decrease in toxicity and
little effect on the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 33 33 E->R: >10000-fold decrease in toxicity
and little decrease in binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 48 48 E->D: 8.3-fold decrease in toxicity and
43.6-fold decrease in binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 48 48 E->L: 29-fold decrease in toxicity and
158-fold decrease in binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 48 48 E->Q: 27.3-fold decrease in toxicity and
74.5-fold decrease in binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 48 48 E->R: 608-fold decrease in toxicity and
11455-fold decrease in binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 51 51 K->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 56 56 E->I: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 71 73 EDD->AAA: Little effect on toxicity and
on the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 71 73 EDD->KRR: Little effect on toxicity and
on the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 72 72 D->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 73 73 D->A: Little effect on toxicity and on
the binding affinity.
MUTAGEN 74 74 K->T: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 81 81 D->N: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 84 84 K->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 85 85 K->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 88 88 D->A: Little effect on toxicity and on
the binding affinity.
{ECO:0000269|PubMed:15054090}.
MUTAGEN 93 94 Missing: 4.6-fold reduction of toxicity.
MUTAGEN 94 94 Missing: 5.7-fold reduction of toxicity.
STRAND 20 22 {ECO:0000244|PDB:4KYP}.
HELIX 37 40 {ECO:0000244|PDB:4KYP}.
HELIX 43 51 {ECO:0000244|PDB:4KYP}.
STRAND 56 61 {ECO:0000244|PDB:4KYP}.
STRAND 64 70 {ECO:0000244|PDB:4KYP}.
HELIX 81 89 {ECO:0000244|PDB:4KYP}.
SEQUENCE 94 AA; 10512 MW; 40F6510F26E4BB90 CRC64;
MKFFLMCLII FPIMGVLGKK NGYPLDRNGK TTECSGVNAI APHYCNSECT KVYYAESGYC
CWGACYCFGL EDDKPIGPMK DITKKYCDVQ IIPS


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