ID   GIG4_ANEVI              Reviewed;          77 AA.
AC   P0DMY9;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=U-actitoxin-Avd12a {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Avd12a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Gigantoxin-4 {ECO:0000303|PubMed:21281459};
DE            Short=Gigt 4 {ECO:0000303|PubMed:21281459};
DE   Flags: Precursor;
OS   Anemonia viridis (Snakelocks anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=51769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19627569; DOI=10.1186/1471-2164-10-333;
RA   Sabourault C., Ganot P., Deleury E., Allemand D., Furla P.;
RT   "Comprehensive EST analysis of the symbiotic sea anemone, Anemonia
RT   viridis.";
RL   BMC Genomics 10:333-333(2009).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=21281459; DOI=10.1186/1471-2164-12-88;
RA   Kozlov S., Grishin E.;
RT   "The mining of toxin-like polypeptides from EST database by single residue
RT   distribution analysis.";
RL   BMC Genomics 12:88-88(2011).
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:0000250|UniProtKB:Q76CA1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the EGF domain peptide family. {ECO:0000305}.
CC   -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC       1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC       {ECO:0000305}.
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DR   EMBL; FK735889; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DMY9; -.
DR   SMR; P0DMY9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; EGF-like domain; Nematocyst; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..29
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433674"
FT   CHAIN           30..77
FT                   /note="U-actitoxin-Avd12a"
FT                   /evidence="ECO:0000250|UniProtKB:Q76CA1"
FT                   /id="PRO_0000433675"
FT   DOMAIN          31..73
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        35..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        44..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        63..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   77 AA;  8653 MW;  E1405319C7432B80 CRC64;
     MALFRMLFLC AVLVLLTSKE GMSYEEPEND EGVACTGQYA ESFCLNGGTC RYIQSIGEYY
     CICNGDYTGH RCEKKQV