ID   TXX1B_ETHRU             Reviewed;          88 AA.
AC   A0A023W145;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=U-scoloptoxin(XY)-Er1b {ECO:0000305};
DE            Short=U-SLPTX(XY)-Er1b {ECO:0000305};
DE   AltName: Full=U-scoloptoxin-Er4.1a2b {ECO:0000312|EMBL:AHY22595.1};
DE            Short=U-SLPTX-Er4.1a2b {ECO:0000312|EMBL:AHY22595.1};
DE   Contains:
DE     RecName: Full=U-scoloptoxin-Er2.1a {ECO:0000303|PubMed:24602922};
DE   Contains:
DE     RecName: Full=U-scoloptoxin-Er2.2b {ECO:0000303|PubMed:24602922};
DE   Flags: Precursor;
OS   Ethmostigmus rubripes (Giant centipede).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Ethmostigmus.
OX   NCBI_TaxID=62613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-61, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24602922; DOI=10.1016/j.jprot.2014.02.024;
RA   Undheim E.A., Sunagar K., Hamilton B.R., Jones A., Venter D.J., Fry B.G.,
RA   King G.F.;
RT   "Multifunctional warheads: diversification of the toxin arsenal of
RT   centipedes via novel multidomain transcripts.";
RL   J. Proteomics 102:1-10(2014).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The
CC       mature toxins are clearly liberated from the multidomain precursors in
CC       the venom gland prior to venom expulsion and not by venom proteases
CC       upon secretion. {ECO:0000269|PubMed:24602922}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24602922}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the scoloptoxin-XY family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KF130744; AHY22595.1; -; mRNA.
DR   EMBL; KF130745; AHY22596.1; -; mRNA.
DR   EMBL; KF130750; AHY22601.1; -; mRNA.
DR   AlphaFoldDB; A0A023W145; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:24602922"
FT   CHAIN           25..61
FT                   /note="U-scoloptoxin-Er2.1a"
FT                   /evidence="ECO:0000269|PubMed:24602922"
FT                   /id="PRO_5007368304"
FT   PEPTIDE         64..78
FT                   /note="U-scoloptoxin-Er2.2b"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023W140"
FT                   /id="PRO_0000446852"
FT   PROPEP          79..88
FT                   /evidence="ECO:0000250|UniProtKB:A0A023W140"
FT                   /id="PRO_0000446853"
FT   REGION          66..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   88 AA;  9588 MW;  49F65B70706F5A08 CRC64;
     MASQVVLSFA LVVVLAVFVG QVDSCPSDCK CDYRSSQCRP ANDDVHPNVC IDHYCVVMNL
     AKREQRPELS PGALDDSSEE KDNEASLA