GIG1_STIGI
ID GIG1_STIGI Reviewed; 86 AA.
AC Q76CA1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=OMEGA-stichotoxin-Sgt1a {ECO:0000303|PubMed:22683676};
DE Short=OMEGA-SHTX-Sgt1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=EGF-like peptide toxin {ECO:0000303|PubMed:12565742};
DE AltName: Full=Gigantoxin I {ECO:0000303|PubMed:12565742};
DE Short=Gigt I;
DE AltName: Full=Gigantoxin-1;
DE Flags: Precursor;
OS Stichodactyla gigantea (Giant carpet anemone) (Gigantic sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Stichodactyla.
OX NCBI_TaxID=230562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14644045; DOI=10.1016/j.bbapap.2003.08.007;
RA Honma T., Nagai H., Nagashima Y., Shiomi K.;
RT "Molecular cloning of an epidermal growth factor-like toxin and two sodium
RT channel toxins from the sea anemone Stichodactyla gigantea.";
RL Biochim. Biophys. Acta 1652:103-106(2003).
RN [2]
RP PROTEIN SEQUENCE OF 39-86, FUNCTION, AND TOXIC DOSE.
RC TISSUE=Nematoblast;
RX PubMed=12565742; DOI=10.1016/s0041-0101(02)00281-7;
RA Shiomi K., Honma T., Ide M., Nagashima Y., Ishida M., Chino M.;
RT "An epidermal growth factor-like toxin and two sodium channel toxins from
RT the sea anemone Stichodactyla gigantea.";
RL Toxicon 41:229-236(2003).
RN [3]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
CC -!- FUNCTION: Has both toxic and EGF activity. Its EGF activity consists of
CC rounding cells (morphological change) and inducing tyrosine
CC phosphorylation of the EGFR in A431 cells, but with a lower potency
CC that human EGF. {ECO:0000269|PubMed:12565742}.
CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst.
CC -!- TOXIC DOSE: PD(50) is 215 ug/kg to crabs. LD(50) is >1000 ug/kg to
CC crabs. {ECO:0000269|PubMed:12565742}.
CC -!- SIMILARITY: Belongs to the EGF domain peptide family. {ECO:0000305}.
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DR EMBL; AB110014; BAD01579.1; -; mRNA.
DR AlphaFoldDB; Q76CA1; -.
DR SMR; Q76CA1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR000742; EGF-like_dom.
DR Pfam; PF00008; EGF; 1.
DR SMART; SM00181; EGF; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Nematocyst; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..36
FT /evidence="ECO:0000269|PubMed:12565742"
FT /id="PRO_0000007592"
FT CHAIN 39..86
FT /note="OMEGA-stichotoxin-Sgt1a"
FT /evidence="ECO:0000269|PubMed:12565742"
FT /id="PRO_0000007593"
FT DOMAIN 40..82
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 44..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 53..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 72..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 86 AA; 9622 MW; 363FBA4D1230D6A7 CRC64;
MASFRTLFAC VVILCCVLWS SMARYGEDME VETEMNKRDV GVACTGQYAS SFCLNGGTCR
YIPELGEYYC ICPGDYTGHR CEQMSV
