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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
 
 
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