SX15F_RHOJU
ID SX15F_RHOJU Reviewed; 83 AA.
AC E7CLP4;
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 RjAa15f {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:ADV16831.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland {ECO:0000312|EMBL:ADV16831.1};
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; HM233953; ADV16831.1; -; mRNA.
DR AlphaFoldDB; E7CLP4; -.
DR SMR; E7CLP4; -.
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 Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
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 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 RjAa15f"
FT /evidence="ECO:0000255"
FT /id="PRO_0000413467"
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; 9315 MW; 704297927B2971F2 CRC64;
MKILIFIIAS FMLIGVECKE GYPMGRNGCK IPCAINDNIC KVECQAKWKQ SDGYCYSWGL
SCYCTNLLED AEVWDSSNNK CVG