TX11A_ETHRU
ID TX11A_ETHRU Reviewed; 119 AA.
AC P0DPW4;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=U-scoloptoxin(01)-Er1a {ECO:0000303|PubMed:24847043};
DE Short=U-SLPTX(01)-Er1a {ECO:0000303|PubMed:24847043};
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], AND NOMENCLATURE.
RC TISSUE=Venom gland;
RX PubMed=24847043; DOI=10.1093/molbev/msu162;
RA Undheim E.A., Jones A., Clauser K.R., Holland J.W., Pineda S.S., King G.F.,
RA Fry B.G.;
RT "Clawing through evolution: toxin diversification and convergence in the
RT ancient lineage Chilopoda (centipedes).";
RL Mol. Biol. Evol. 31:2124-2148(2014).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24847043}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24847043}.
CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the scoloptoxin-01 family. {ECO:0000305}.
CC -!- CAUTION: All E.rubripes family members described in 'Undeheim et al.,
CC 2014' have not been imported into UniProtKB. Please, refer to this
CC paper to access them. {ECO:0000305|PubMed:24847043}.
CC -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC (NCBI);
CC URL="https://www.ncbi.nlm.nih.gov/nuccore/GASI01000092";
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DR AlphaFoldDB; P0DPW4; -.
DR SMR; P0DPW4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF01607; CBM_14; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
PE 3: Inferred from homology;
KW Chitin-binding; Disulfide bond; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..119
FT /note="U-scoloptoxin(01)-Er1a"
FT /evidence="ECO:0000305"
FT /id="PRO_0000446688"
FT DOMAIN 39..97
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 74..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ SEQUENCE 119 AA; 13131 MW; E3E122FC23D35B0D CRC64;
MEIHSNIILL LLIALFAIFV KMEDEEKPPN LTRMPEGVNF ACSGKKPGFY ADEGFDCQVY
HMCSPEGQLT TYLCGPGTIF NQKKLVCDLP TNYNCADAAK DAEEANANVF KTQSSTSEP