ID   ACR2_ACTEQ              Reviewed;          83 AA.
AC   Q3C256;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=U-actitoxin-Aeq6a {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Aeq6a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Acrorhagin II {ECO:0000303|PubMed:16183092};
DE   AltName: Full=Acrorhagin-2 {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], PROTEIN SEQUENCE OF 39-78, MASS SPECTROMETRY,
RP   AMIDATION AT PRO-82, TOXIC DOSE, TISSUE SPECIFICITY, AND FUNCTION.
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]
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. {ECO:0000269|PubMed:16183092}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by acrorhagi.
CC       {ECO:0000269|PubMed:16183092}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4873.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16183092};
CC   -!- TOXIC DOSE: LD(50) is 80 ug/kg against crab (P.dehaani).
CC       {ECO:0000269|PubMed:16183092}.
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DR   EMBL; AB212068; BAE46983.1; -; mRNA.
DR   AlphaFoldDB; Q3C256; -.
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.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Nematocyst; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..36
FT                   /evidence="ECO:0000269|PubMed:16183092"
FT                   /id="PRO_0000228113"
FT   CHAIN           39..82
FT                   /note="U-actitoxin-Aeq6a"
FT                   /id="PRO_0000228114"
FT   MOD_RES         82
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000305|PubMed:16183092"
SQ   SEQUENCE   83 AA;  9068 MW;  65F528C27BF49C18 CRC64;
     MIYKAVFVCL VLVLLGDVFC SPRNSGGGTL NDNPFEKRTD CRFVGAKCTK ANNPCVGKVC
     NGYQLYCPAD DDHCIMKLTF IPG