TX41B_ETHRU
ID TX41B_ETHRU Reviewed; 78 AA.
AC A0A023W082; A0A023W078;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=U-scoloptoxin(04)-Er1b {ECO:0000305};
DE Short=U-SLPTX(04)-Er1b {ECO:0000305};
DE AltName: Full=U-scoloptoxin-Er1.1a2b {ECO:0000312|EMBL:AHY22581.1};
DE Short=U-SLPTX-Er1.1a2b {ECO:0000312|EMBL:AHY22581.1};
DE Contains:
DE RecName: Full=U-scoloptoxin-Er1.1a {ECO:0000303|PubMed:24602922};
DE Contains:
DE RecName: Full=U-scoloptoxin-Er1.2b {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 29-46 AND 47-77,
RP IDENTIFICATION BY 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; KF130725; AHY22576.1; -; mRNA.
DR EMBL; KF130726; AHY22577.1; -; mRNA.
DR EMBL; KF130730; AHY22581.1; -; mRNA.
DR AlphaFoldDB; A0A023W082; -.
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:0000255"
FT PROPEP 25..28
FT /evidence="ECO:0000305|PubMed:24602922"
FT /id="PRO_0000446699"
FT PEPTIDE 29..46
FT /note="U-scoloptoxin-Er1.1a"
FT /evidence="ECO:0000269|PubMed:24602922"
FT /id="PRO_5007368302"
FT CHAIN 47..77
FT /note="U-scoloptoxin-Er1.2b"
FT /evidence="ECO:0000250|UniProtKB:A0A023VZM6"
FT /id="PRO_0000446700"
SQ SEQUENCE 78 AA; 8833 MW; 289822BFFD7F2088 CRC64;
MTRHLIFAAV LLVCLFVCWN AVGAQDARSA FSSEETAQDQ HVMEERIFIN PAGNREKNAC
MENCRSSPNC KNYEFCSK