ID   ACR1_ACTTE              Reviewed;          28 AA.
AC   P0DQJ2;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=U-actitoxin-Ate1 {ECO:0000303|PubMed:31302115};
DE            Short=U-AITX-Ate1 {ECO:0000303|PubMed:31302115};
DE   Flags: Precursor;
OS   Actinia tenebrosa (Australian red waratah sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Actinia.
OX   NCBI_TaxID=6105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 16-28, STRUCTURE BY NMR OF 16-28,
RP   DISULFIDE BOND, AND SUBUNIT.
RX   PubMed=31302115; DOI=10.1016/j.toxicon.2019.07.002;
RA   Elnahriry K.A., Wai D.C.C., Krishnarjuna B., Badawy N.N., Chittoor B.,
RA   MacRaild C.A., Williams-Noonan B.J., Surm J.M., Chalmers D.K., Zhang A.H.,
RA   Peigneur S., Mobli M., Tytgat J., Prentis P., Norton R.S.;
RT   "Structural and functional characterisation of a novel peptide from the
RT   Australian sea anemone Actinia tenebrosa.";
RL   Toxicon 168:104-112(2019).
CC   -!- FUNCTION: Probable toxin expected to be employed in prey capture and/or
CC       defense against predators (based on its abundance in tentacles). Does
CC       not show activity on mammalian voltage-gated potassium and sodium
CC       channels, and does not induce change in behavior and mortality rates in
CC       crustacea (redclaw crayfish) (PubMed:31302115). Shows moderate
CC       cytotoxic activity against MCF-7 and MDA-MB-231 breast cancer cell
CC       lines (PubMed:31302115). Has only a weak affinity for lipid membranes
CC       (PubMed:31302115). {ECO:0000269|PubMed:31302115}.
CC   -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:31302115}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31302115}.
CC       Nematocyst {ECO:0000305|PubMed:31302115}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the tentacles
CC       (PubMed:31302115). Weakly expressed in acrorhagi and mesenteric
CC       filaments (PubMed:31302115). {ECO:0000269|PubMed:31302115}.
CC   -!- PTM: May be N-glycosylated at Asn-22. Activity with this modification
CC       has not be tested. {ECO:0000305|PubMed:31302115}.
CC   -!- MISCELLANEOUS: The 26-Cys-Pro-27 bond exists only in the trans-
CC       isomerization. {ECO:0000269|PubMed:31302115}.
CC   -!- MISCELLANEOUS: Does not show activity on voltage-gated potassium
CC       channels (Kv1.1-Kv1.6, Kv2.1, Kv4.2, and Shaker IR), voltage-gated
CC       sodium channels (Nav1.2, Nav1.4, Nav1.5, and Nav1.6), and the insect
CC       channel BgNav1. {ECO:0000269|PubMed:31302115}.
CC   -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
CC       URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=30607";
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DR   PDB; 6OQP; NMR; -; A=16-28.
DR   PDBsum; 6OQP; -.
DR   AlphaFoldDB; P0DQJ2; -.
DR   Proteomes; UP000515163; Unplaced.
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   3D-structure; Disulfide bond; Nematocyst; Reference proteome; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000305|PubMed:31302115"
FT   PEPTIDE         16..28
FT                   /note="U-actitoxin-Ate1"
FT                   /evidence="ECO:0000305|PubMed:31302115"
FT                   /id="PRO_0000448542"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000269|PubMed:31302115,
FT                   ECO:0007744|PDB:6OQP"
SQ   SEQUENCE   28 AA;  3189 MW;  625E1F71D6A5DD37 CRC64;
     MSLILIFFAF TVLKSSKWIC ANRSVCPI