ID   SCIT_HOTJU              Reviewed;          85 AA.
AC   Q56TT9;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Alpha-insect toxin BjaIT;
DE   AltName: Full=Bj-alpha-IT;
DE   Flags: Precursor;
OS   Hottentotta judaicus (Black scorpion) (Buthotus judaicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Hottentotta.
OX   NCBI_TaxID=6863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-46, FUNCTION, MASS
RP   SPECTROMETRY, AND TOXIC DOSE.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15705498; DOI=10.1016/j.ibmb.2004.11.005;
RA   Arnon T., Potikha T., Sher D., Elazar M., Mao W., Tal T., Bosmans F.,
RA   Tytgat J., Ben-Arie N., Zlotkin E.;
RT   "BjalphaIT: a novel scorpion alpha-toxin selective for insects -- unique
RT   pharmacological tool.";
RL   Insect Biochem. Mol. Biol. 35:187-195(2005).
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 is active against
CC       insects (para/tipE). {ECO:0000269|PubMed:15705498}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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=6948; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15705498};
CC   -!- TOXIC DOSE: PD(50) is 130 ng/g body weight to blowfly larvae, PD(50) is
CC       50 ng/g body weight to locusts (Locusta migratoria). Not toxic by
CC       subcutaneous injection into mice. {ECO:0000269|PubMed:15705498}.
CC   -!- MISCELLANEOUS: Does not affect the mammalian Nav1.2/SCN2A sodium
CC       channel. {ECO:0000305|PubMed:15705498}.
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   EMBL; AY585097; AAT52203.1; -; mRNA.
DR   AlphaFoldDB; Q56TT9; -.
DR   SMR; Q56TT9; -.
DR   PRIDE; Q56TT9; -.
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; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:15705498"
FT   CHAIN           20..83
FT                   /note="Alpha-insect toxin BjaIT"
FT                   /id="PRO_0000260005"
FT   DOMAIN          21..83
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         83
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        41..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        45..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CONFLICT        16
FT                   /note="G -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9270 MW;  A4993A2BC9EF8103 CRC64;
     MNYLVVICFA LLLMTGVESG RDAYIADNLN CAYTCGSNSY CNTECTKNGA VSGYCQWLGK
     YGNACWCINL PDKVPIRIPG ACRGR