ID   SX17F_RHOJU             Reviewed;          83 AA.
AC   E7CLP5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Putative beta-neurotoxin RjAa17f {ECO:0000250|UniProtKB:Q1I176};
DE   Flags: Precursor;
OS   Rhopalurus junceus (Caribbean blue scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Rhopalurus.
OX   NCBI_TaxID=419285;
RN   [1] {ECO:0000312|EMBL:ADV16832.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland {ECO:0000312|EMBL:ADV16832.1};
RX   PubMed=21605585; DOI=10.1016/j.toxicon.2011.04.011;
RA   Garcia-Gomez B.I., Coronas F.I., Restano-Cassulini R., Rodriguez R.R.,
RA   Possani L.D.;
RT   "Biochemical and molecular characterization of the venom from the Cuban
RT   scorpion Rhopalurus junceus.";
RL   Toxicon 58:18-27(2011).
CC   -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC       channels (Nav) and shift the voltage of activation toward more negative
CC       potentials thereby affecting sodium channel activation and promoting
CC       spontaneous and repetitive firing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15226}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:21605585}.
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   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000255}.
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DR   EMBL; HM233954; ADV16832.1; -; mRNA.
DR   AlphaFoldDB; E7CLP5; -.
DR   SMR; E7CLP5; -.
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   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   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..83
FT                   /note="Putative beta-neurotoxin RjAa17f"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413468"
FT   DOMAIN          19..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        29..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        33..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        40..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   83 AA;  9346 MW;  C010856F553971F4 CRC64;
     MKILIFIIAS FMLIGVECKE GYPMGRNGCK IPCAINDNIC KTECQAKWKQ SDGYCYSPGM
     SCYCTNLPED AEVWDFSNIK CRG