ACR1_ACTEQ
ID ACR1_ACTEQ Reviewed; 70 AA.
AC Q3C258; A0A6C0WVJ3;
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-Aeq5a {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Aeq5a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Acrorhagin I {ECO:0000303|PubMed:16183092};
DE AltName: Full=Acrorhagin-1 {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 21-68, MASS SPECTROMETRY,
RP TOXIC DOSE, TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Nematoblast;
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:QIC50028.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=32057717; DOI=10.1016/j.margen.2020.100753;
RA Wilding C.S., Fletcher N., Smith E.K., Prentis P., Weedall G.D.,
RA Stewart Z.;
RT "The genome of the sea anemone Actinia equina (L.): meiotic toolkit genes
RT and the question of sexual reproduction.";
RL Mar. Genomics 53:100753-100753(2020).
RN [3]
RP STRUCTURE BY NMR OF 21-70, DISULFIDE BOND, AND RECOMBINANT EXPRESSION.
RX PubMed=33387653; DOI=10.1016/j.jsb.2020.107692;
RA Krishnarjuna B., Sunanda P., Villegas-Moreno J., Csoti A., Morales R.A.V.,
RA Wai D.C.C., Panyi G., Prentis P., Norton R.S.;
RT "A disulfide-stabilised helical hairpin fold in acrorhagin I: an emerging
RT structural motif in peptide toxins.";
RL J. Struct. Biol. 213:107692-107692(2021).
RN [4]
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 (PubMed:16183092). It interacts
CC with divalent metal ions (zinc and nickel) suggesting it may function
CC as a metal ion chelator to regulate metal ion levels or as a metal ion
CC transporter, or that its function is modulated by metal ions. Is not
CC active against any of the voltage-gated potassium and sodium channels
CC tested (PubMed:33387653). In addition, it does not show activity in
CC bacterial and fungal growth inhibitory assays as well as in hemolytic
CC assays (PubMed:33387653). {ECO:0000269|PubMed:16183092,
CC ECO:0000269|PubMed:33387653}.
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:0000305|PubMed:33387653}.
CC -!- MASS SPECTROMETRY: Mass=5649.0; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16183092};
CC -!- TOXIC DOSE: LD(50) is 520 ug/kg against crab (P.dehaani).
CC {ECO:0000269|PubMed:16183092}.
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:0000269|PubMed:33387653}.
CC -!- MISCELLANEOUS: Both Thr-23-Pro-24 and Cys-69-Pro-70 are in the trans
CC conformation. {ECO:0000305|PubMed:33387653}.
CC -!- MISCELLANEOUS: Has no activity on human voltage-gated potassium
CC channels Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3, Kv11.1/KCNH2/ERG1,
CC KCa1.1/KCNMA1 and KCa3.1/KCNN4, and the human sodium channel
CC Nav1.4/SCN4A. {ECO:0000269|PubMed:33387653}.
CC -!- SIMILARITY: Belongs to the Acrorhagin I family. {ECO:0000305}.
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DR EMBL; AB212066; BAE46981.1; -; mRNA.
DR EMBL; MN605639; QIC50028.1; -; Genomic_DNA.
DR PDB; 6UX5; NMR; -; A=21-70.
DR PDBsum; 6UX5; -.
DR AlphaFoldDB; Q3C258; -.
DR BMRB; Q3C258; -.
DR SMR; Q3C258; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Metal-binding;
KW Nematocyst; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:16183092"
FT CHAIN 21..70
FT /note="U-actitoxin-Aeq5a"
FT /evidence="ECO:0000305|PubMed:16183092"
FT /id="PRO_0000228111"
FT DISULFID 31..69
FT /evidence="ECO:0000269|PubMed:33387653,
FT ECO:0007744|PDB:6UX5"
FT DISULFID 35..64
FT /evidence="ECO:0000269|PubMed:33387653,
FT ECO:0007744|PDB:6UX5"
FT DISULFID 42..57
FT /evidence="ECO:0000269|PubMed:33387653,
FT ECO:0007744|PDB:6UX5"
FT DISULFID 48..54
FT /evidence="ECO:0000269|PubMed:33387653,
FT ECO:0007744|PDB:6UX5"
FT HELIX 28..44
FT /evidence="ECO:0007829|PDB:6UX5"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:6UX5"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:6UX5"
SQ SEQUENCE 70 AA; 7887 MW; 2923993D5FDC3D4B CRC64;
MNQVMTIFLV LGVIVYSVES SSTPDGTWVK CRHDCFTKYK SCQMSDSCHD EQSCHQCHVK
HTDCVNTGCP