ID   SX12F_RHOJU             Reviewed;          83 AA.
AC   E7CLP2; P86685;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Putative beta-neurotoxin RjAa12f {ECO:0000250|UniProtKB:P15226};
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:0000305, ECO:0000312|EMBL:ADV16829.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-82, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:21605585}, and
RC   Venom gland {ECO:0000312|EMBL:ADV16829.1};
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. This toxin is lethal to insects
CC       (A.domestica). It is not toxic to mice and does not affect mammal F11
CC       sodium channels. {ECO:0000269|PubMed:21605585}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21605585}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|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   -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:21605585}.
CC   -!- MASS SPECTROMETRY: Mass=7293.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21605585};
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; HM233951; ADV16829.1; -; mRNA.
DR   AlphaFoldDB; E7CLP2; -.
DR   SMR; E7CLP2; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0044360; P:modulation of voltage-gated potassium channel activity in another organism; IDA:UniProtKB.
DR   GO; GO:0044488; P:modulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:21605585"
FT   PEPTIDE         19..82
FT                   /note="Putative beta-neurotoxin RjAa12f"
FT                   /evidence="ECO:0000269|PubMed:21605585"
FT                   /id="PRO_0000413464"
FT   PROPEP          83
FT                   /evidence="ECO:0000269|PubMed:21605585"
FT                   /id="PRO_0000413465"
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;  9383 MW;  C6B0782E910DDE92 CRC64;
     MKILIFIIAS FMLIGVECKE GYPMGRDGCK ISCVINNNFC KVECQAKWRQ SDGYCYFWGL
     SCYCTNLPED AQVWDSSTNK CGG