SCX28_HOTTS
ID SCX28_HOTTS Reviewed; 65 AA.
AC P84614;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Alpha-toxin Bs-Tx28;
OS Hottentotta tamulus sindicus (Scorpion) (Buthus sindicus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=42519;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, TOXIC DOSE, AND AMIDATION AT ARG-65.
RC TISSUE=Venom;
RX PubMed=16309623; DOI=10.1016/j.abb.2005.10.016;
RA Ali S.A., Wang B., Alam M., Beck A., Stoeva S., Voelter W., Abbasi A.,
RA Duszenko M.;
RT "Structure-activity relationship of an alpha-toxin Bs-Tx28 from scorpion
RT (Buthus sindicus) venom suggests a new alpha-toxin subfamily.";
RL Arch. Biochem. Biophys. 445:81-94(2006).
CC -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC channels (Nav) and inhibit the inactivation of the activated channels,
CC thereby blocking neuronal transmission. This toxin inhibits the
CC inactivation of activated TTX-sensitive sodium channels (Nav).
CC {ECO:0000269|PubMed:16309623}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16309623}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:16309623}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=7274.3; Mass_error=2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16309623};
CC -!- TOXIC DOSE: LD(50) is 0.088 ug/g by subcutaneous injection into mice,
CC 0.0023 ug/g by intracerebroventricular injection into mice and 14.3
CC ug/g in B.germanica. {ECO:0000269|PubMed:16309623}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P84614; -.
DR SMR; P84614; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR CDD; cd00107; Knot1; 1.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..65
FT /note="Alpha-toxin Bs-Tx28"
FT /id="PRO_0000066747"
FT DOMAIN 3..65
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 65
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:16309623"
FT DISULFID 13..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 17..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 23..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 27..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 65 AA; 7273 MW; 97A2A242C70B83E4 CRC64;
GVRDAYIADD KNCVYTCGSN SYCNTECTKN GAESGYCQWF GRWGNGCWCI KLPDKVPIRI
PGKCR
