ID   KBX3_EUSVA              Reviewed;          97 AA.
AC   P0DL47;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Scorpine-like peptide Ev37 {ECO:0000303|PubMed:23262394};
DE   Flags: Precursor;
OS   Euscorpiops validus (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Euscorpiidae; Scorpiopinae; Scorpiopini;
OC   Euscorpiops.
OX   NCBI_TaxID=1643527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=23262394; DOI=10.1016/j.pep.2012.12.004;
RA   Feng J., Yu C., Wang M., Li Z., Wu Y., Cao Z., Li W., He X., Han S.;
RT   "Expression and characterization of a novel scorpine-like peptide Ev37,
RT   from the scorpion Euscorpiops validus.";
RL   Protein Expr. Purif. 88:127-133(2013).
CC   -!- FUNCTION: Ev37 selectively inhibits Kv1.3/KCNA3 channel (IC(50)=0.95
CC       uM). Both N-terminal and C-terminal domains are likely involved in the
CC       interaction with Kv1.3, since neither Ev37-N (1-36) nor Ev37-C (37-78)
CC       block Kv1.3 channel. {ECO:0000269|PubMed:23262394}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C2F4}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not block Kv1.1/KCNA1 and Kv1.2/KCNA2 channels.
CC       Neither the full-length Ev37 nor the two individual domains (Ev37-N (1-
CC       36) and Ev37-C (37-78)) show any cytolytic effects on bacteria or on
CC       red blood cells. {ECO:0000269|PubMed:23262394}.
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 3
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DL47; -.
DR   SMR; P0DL47; -.
DR   PRIDE; P0DL47; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR029237; Long_scorpion_toxin.
DR   Pfam; PF14866; Toxin_38; 1.
DR   PROSITE; PS51862; BSPN_CSAB; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..97
FT                   /note="Scorpine-like peptide Ev37"
FT                   /id="PRO_0000433342"
FT   DOMAIN          55..95
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        58..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        68..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        72..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   97 AA;  10495 MW;  763031A663D53C22 CRC64;
     MNSKLTVIVL LALITIASCG LINEKKVQQY LDEKLPNGVV KGALKSLVHK AAKNQNLCAF
     NVDTVGMCDA DCKRQGKAKG VCHGTKCKCD VELSYKK