GIG5_ANEVI
ID GIG5_ANEVI Reviewed; 60 AA.
AC P0DMZ0;
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-Avd12b {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Avd12b {ECO:0000303|PubMed:22683676};
DE AltName: Full=Gigantoxin-5 {ECO:0000303|PubMed:21281459};
DE Short=Gigt 5 {ECO:0000303|PubMed:21281459};
DE Flags: Precursor; Fragment;
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; FK749754; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DMZ0; -.
DR SMR; P0DMZ0; -.
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 Pfam; PF00008; EGF; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Nematocyst; Secreted; Signal.
FT SIGNAL <1..6
FT /evidence="ECO:0000250|UniProtKB:Q76CA1"
FT PROPEP 7..12
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433676"
FT CHAIN 13..60
FT /note="U-actitoxin-Avd12b"
FT /evidence="ECO:0000250|UniProtKB:Q76CA1"
FT /id="PRO_0000433677"
FT DOMAIN 14..56
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 18..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 27..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 46..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:21281459"
SQ SEQUENCE 60 AA; 6701 MW; 9CDC660ECB0B3B30 CRC64;
SKEGMSYEEP ENDEGVACTG QYAESFCLNG GTCRYIQSIG EYYCICVGDY TGHRCEKKQV
