TXX1A_ETHRU
ID TXX1A_ETHRU Reviewed; 88 AA.
AC A0A023W140; A0A023VZG5; A0A023VZP7; A0A023W0V0;
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(XY)-Er1a {ECO:0000305};
DE Short=U-SLPTX(XY)-Er1a {ECO:0000305};
DE AltName: Full=U-scoloptoxin-Er4.1a2a;
DE Short=U-SLPTX-Er4.1a2a {ECO:0000312|EMBL:AHY22590.1};
DE Contains:
DE RecName: Full=U-scoloptoxin-Er2.1a {ECO:0000303|PubMed:24602922};
DE Contains:
DE RecName: Full=U-scoloptoxin-Er2.2a {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 AND 64-78,
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 3 disulfide bonds. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the scoloptoxin-XY family. {ECO:0000305}.
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DR EMBL; KF130739; AHY22590.1; -; mRNA.
DR EMBL; KF130740; AHY22591.1; -; mRNA.
DR EMBL; KF130741; AHY22592.1; -; mRNA.
DR EMBL; KF130742; AHY22593.1; -; mRNA.
DR EMBL; KF130743; AHY22594.1; -; mRNA.
DR EMBL; KF130746; AHY22597.1; -; mRNA.
DR EMBL; KF130747; AHY22598.1; -; mRNA.
DR EMBL; KF130748; AHY22599.1; -; mRNA.
DR AlphaFoldDB; A0A023W140; -.
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 Cleavage on pair of basic residues; Direct protein sequencing;
KW 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_5007368311"
FT PEPTIDE 64..78
FT /note="U-scoloptoxin-Er2.2a"
FT /evidence="ECO:0000269|PubMed:24602922"
FT /id="PRO_0000446850"
FT PROPEP 79..88
FT /evidence="ECO:0000305|PubMed:24602922"
FT /id="PRO_0000446851"
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; 9661 MW; 49F65B70706F47BF CRC64;
MASQVVLSFA LVVVLAVFVG QVDSCPSDCK CDYRSSQCRP ANDDVHPNVC IDHYCVVMNL
AKREQRPELS PGAWDDSSEE KDNEASLA