ID   ACR1A_ACTEQ             Reviewed;          72 AA.
AC   Q3C257; A0A3P8MJV8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=U-actitoxin-Aeq5b {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Aeq5b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Acrorhagin Ia {ECO:0000303|PubMed:16183092};
DE   AltName: Full=Acrorhagin-1a {ECO:0000305};
DE   Flags: Precursor;
OS   Actinia equina (Beadlet anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Actinia.
OX   NCBI_TaxID=6106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16183092; DOI=10.1016/j.toxicon.2005.08.003;
RA   Honma T., Minagawa S., Nagai H., Ishida M., Nagashima Y., Shiomi K.;
RT   "Novel peptide toxins from acrorhagi, aggressive organs of the sea anemone
RT   Actinia equina.";
RL   Toxicon 46:768-774(2005).
RN   [2] {ECO:0000312|EMBL:ATY39989.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Surm J.M., Smith H., van der Burg C.A., Stewart Z., Prentis P.J.,
RA   Pavasovic A.;
RT   "Toxin and toxin-like genes show dynamic gene family evolution and
RT   expression patterns in phylum Cnidaria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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: Toxin that is lethal to crab. It interacts with divalent
CC       metal ions (zinc and nickel) suggesting it may function as a metal ion
CC       chelator to regulate metal ion levels or as a metal ion transporter, or
CC       that its function is modulated by metal ions. Is not active against any
CC       of the voltage-gated potassium and sodium channels tested. In addition,
CC       it does not show activity in bacterial and fungal growth inhibitory
CC       assays as well as in hemolytic assays. {ECO:0000250|UniProtKB:Q3C258}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by acrorhagi.
CC       {ECO:0000269|PubMed:16183092}.
CC   -!- DOMAIN: Has the structural arrangement of two alpha-helices stabilized
CC       by disulfide bonds (CSalpha/alpha 4(S-S)).
CC       {ECO:0000250|UniProtKB:Q3C258}.
CC   -!- MISCELLANEOUS: This toxin interacts with divalent metal ions (zinc and
CC       nickel). This suggests it may function as a metal ion chelator to
CC       regulate metal ion levels or as a metal ion transporter, or that its
CC       function is modulated by metal ions. {ECO:0000250|UniProtKB:Q3C258}.
CC   -!- MISCELLANEOUS: Both Thr-23-Pro-24 and Cys-71-Pro-72 are in the trans
CC       conformation. {ECO:0000250|UniProtKB:Q3C258}.
CC   -!- SIMILARITY: Belongs to the Acrorhagin I family. {ECO:0000305}.
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DR   EMBL; AB212067; BAE46982.1; -; mRNA.
DR   EMBL; KY176769; ATY39989.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3C257; -.
DR   SMR; Q3C257; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Metal-binding; Nematocyst; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..72
FT                   /note="U-actitoxin-Aeq5b"
FT                   /evidence="ECO:0000305|PubMed:16183092"
FT                   /id="PRO_0000228112"
FT   DISULFID        33..71
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
FT   DISULFID        37..66
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
FT   DISULFID        50..56
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
SQ   SEQUENCE   72 AA;  8059 MW;  68C05FB5748081B4 CRC64;
     MNQVMTIFLV LGVIVYSVES SLTPSSDIPW EKCRHDCFAK YMSCQMSDSC HNKPSCRQCQ
     VTYAICVSTG CP