ID   TX41F_ETHRU             Reviewed;          72 AA.
AC   A0A023VZF1;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=U-scoloptoxin(04)-Er1f {ECO:0000305};
DE            Short=U-SLPTX(04)-Er1f {ECO:0000305};
DE   AltName: Full=U-scoloptoxin-Er1.1a2e {ECO:0000312|EMBL:AHY22582.1};
DE            Short=U-SLPTX-Er1.1a2e {ECO:0000312|EMBL:AHY22582.1};
DE   Contains:
DE     RecName: Full=U-scoloptoxin-Er1.1a {ECO:0000303|PubMed:24602922};
DE   Contains:
DE     RecName: Full=U-scoloptoxin-Er1.2e {ECO:0000303|PubMed:24602922};
DE   Flags: Precursor; Fragment;
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 19-36, 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 2 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the scoloptoxin-04 family. {ECO:0000305}.
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DR   EMBL; KF130731; AHY22582.1; -; mRNA.
DR   AlphaFoldDB; A0A023VZF1; -.
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..14
FT                   /evidence="ECO:0000250|UniProtKB:A0A023W082"
FT   PROPEP          15..18
FT                   /evidence="ECO:0000305|PubMed:24602922"
FT                   /id="PRO_0000446707"
FT   PEPTIDE         19..36
FT                   /note="U-scoloptoxin-Er1.1a"
FT                   /evidence="ECO:0000269|PubMed:24602922"
FT                   /id="PRO_0000446708"
FT   CHAIN           37..72
FT                   /note="U-scoloptoxin-Er1.2e"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023VZM6"
FT                   /id="PRO_0000446709"
FT   NON_TER         1
SQ   SEQUENCE   72 AA;  8069 MW;  8327535BBBE84B45 CRC64;
     LLVCLFVCWN AVGAQDARSA FSSEETAQDQ HVMEERIFIN PCRKPGKNAC MENCRSSPNC
     KTMSFVQSSI RP