ID   SCX1_RHOCR              Reviewed;          49 AA.
AC   C0HLR6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Beta-toxin Rc1 {ECO:0000303|PubMed:32973807};
DE   Flags: Fragments;
OS   Rhopalurus crassicauda (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Rhopalurus.
OX   NCBI_TaxID=2718978 {ECO:0000303|PubMed:32973807};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:32973807};
RX   PubMed=32973807; DOI=10.3389/fimmu.2020.02011;
RA   Abreu C.B., Bordon K.F., Cerni F.A., Oliveira I.S., Balenzuela C.,
RA   Alexandre-Silva G.M., Zoccal K.F., Reis M.B., Wiezel G.A., Peigneur S.,
RA   Pinheiro-Junior E.L., Tytgat J., Cunha T.M., Quinton L., Faccioli L.H.,
RA   Arantes E.C., Zottich U., Pucca M.B.;
RT   "Pioneering Study on Rhopalurus crassicauda Scorpion Venom: Isolation and
RT   Characterization of the Major Toxin and Hyaluronidase.";
RL   Front. Immunol. 11:1-15(2020).
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 (PubMed:32973807). This toxin acts on
CC       X.laevis Nav1.6/SCN8A and insect BgNav1 channels, and also displays a
CC       small but significant effect on X.laevis Nav1.4/SCN4A channels
CC       (PubMed:32973807). In mice induces nociception (licking and lifting
CC       behaviors) during the first 15 minutes after injection, and increases
CC       the release of TNF-alpha in J774.1 cells (PubMed:32973807).
CC       {ECO:0000269|PubMed:32973807}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32973807}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:32973807}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLR6; -.
DR   SMR; C0HLR6; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0044493; P:envenomation resulting in negative regulation 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; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..49
FT                   /note="Beta-toxin Rc1"
FT                   /id="PRO_0000451729"
FT   DISULFID        15..31
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   NON_CONS        27..28
SQ   SEQUENCE   49 AA;  5500 MW;  47F8BCED98CB15DC CRC64;
     KGGYPVDSKG CKISCVINNE YCSRDCTSGY CYFLRWGLAC WCDGVPPQR