NA21_STIHL
ID NA21_STIHL Reviewed; 48 AA.
AC P19651;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Delta-stichotoxin-She1a {ECO:0000303|PubMed:22683676};
DE Short=Delta-SHTX-She1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Neurotoxin I {ECO:0000303|PubMed:1981881};
DE AltName: Full=Neurotoxin Sh I {ECO:0000303|PubMed:1973932, ECO:0000303|PubMed:2568126, ECO:0000303|PubMed:7913833};
DE Short=ShI;
DE AltName: Full=SHNA;
DE AltName: Full=Sh1;
DE AltName: Full=Toxin SHP-I;
OS Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Stichodactyla.
OX NCBI_TaxID=6123;
RN [1]
RP PROTEIN SEQUENCE, AND TOXIC DOSE.
RC TISSUE=Nematoblast;
RX PubMed=2568126; DOI=10.1021/bi00434a050;
RA Kem W.R., Parten B., Pennington M.W., Price D.A., Dunn B.M.;
RT "Isolation, characterization, and amino acid sequence of a polypeptide
RT neurotoxin occurring in the sea anemone Stichodactyla helianthus.";
RL Biochemistry 28:3483-3489(1989).
RN [2]
RP SYNTHESIS.
RX PubMed=1981881; DOI=10.1111/j.1399-3011.1990.tb01291.x;
RA Pennington M.W., Kem W.R., Norton R.S., Dunn B.M.;
RT "Chemical synthesis of a neurotoxic polypeptide from the sea anemone
RT Stichodactyla helianthus.";
RL Int. J. Pept. Protein Res. 36:335-343(1990).
RN [3]
RP STRUCTURE-FUNCTION RELATIONSHIP.
RX PubMed=7913833; DOI=10.1016/0167-4838(94)90056-6;
RA Monks S.A., Gould A.R., Lumley P.E., Alewood P.F., Kem W.R., Goss N.H.,
RA Norton R.S.;
RT "Limited proteolysis study of structure-function relationships in Sh I, a
RT polypeptide neurotoxin from a sea anemone.";
RL Biochim. Biophys. Acta 1207:93-101(1994).
RN [4]
RP MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=22015268; DOI=10.1016/j.peptides.2011.10.011;
RA Rodriguez A.A., Cassoli J.S., Sa F., Dong Z.Q., de Freitas J.C.,
RA Pimenta A.M., de Lima M.E., Konno K., Lee S.M., Garateix A.,
RA Zaharenko A.J.;
RT "Peptide fingerprinting of the neurotoxic fractions isolated from the
RT secretions of sea anemones Stichodactyla helianthus and Bunodosoma
RT granulifera. New members of the APETx-like family identified by a 454
RT pyrosequencing approach.";
RL Peptides 34:26-38(2012).
RN [5]
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).
RN [6]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=1973932; DOI=10.2210/pdb2sh1/pdb;
RA Fogh R.H., Kem W.R., Norton R.S.;
RT "Solution structure of neurotoxin I from the sea anemone Stichodactyla
RT helianthus. A nuclear magnetic resonance, distance geometry, and restrained
RT molecular dynamics study.";
RL J. Biol. Chem. 265:13016-13028(1990).
RN [7]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=7901218; DOI=10.1016/s0021-9258(19)74523-2;
RA Wilcox G.R., Fogh R.H., Norton R.S.;
RT "Refined structure in solution of the sea anemone neurotoxin ShI.";
RL J. Biol. Chem. 268:24707-24719(1993).
CC -!- FUNCTION: Binds specifically to voltage-gated sodium channels (Nav),
CC thereby delaying their inactivation during signal transduction (By
CC similarity). Is highly toxic to crabs (by intrahemocoelic injection)
CC (PubMed:2568126, PubMed:22015268), but without effect upon mice (by
CC intraperitoneal injection) (PubMed:2568126). {ECO:0000250,
CC ECO:0000269|PubMed:22015268, ECO:0000269|PubMed:2568126}.
CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst.
CC -!- MASS SPECTROMETRY: Mass=5140.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22015268};
CC -!- TOXIC DOSE: LD(50) is 0.3 ug/kg by intrahemocoelic injection.
CC {ECO:0000269|PubMed:2568126}.
CC -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC family. Type II subfamily. {ECO:0000305}.
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DR PIR; A30114; A30114.
DR PDB; 1SH1; NMR; -; A=1-48.
DR PDB; 1SHI; NMR; -; A=1-48.
DR PDB; 2SH1; NMR; -; A=1-48.
DR PDBsum; 1SH1; -.
DR PDBsum; 1SHI; -.
DR PDBsum; 2SH1; -.
DR AlphaFoldDB; P19651; -.
DR BMRB; P19651; -.
DR SMR; P19651; -.
DR TCDB; 8.B.17.1.1; the sea anemone peptide toxin class iii (shi) family.
DR EvolutionaryTrace; P19651; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR000693; Anenome_toxin.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR PIRSF; PIRSF001905; Anenome_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..48
FT /note="Delta-stichotoxin-She1a"
FT /evidence="ECO:0000269|PubMed:2568126"
FT /id="PRO_0000221529"
FT DISULFID 3..43
FT /evidence="ECO:0000269|PubMed:1973932,
FT ECO:0000269|PubMed:7901218, ECO:0007744|PDB:1SH1,
FT ECO:0007744|PDB:1SHI, ECO:0007744|PDB:2SH1"
FT DISULFID 5..33
FT /evidence="ECO:0000269|PubMed:1973932,
FT ECO:0000269|PubMed:7901218, ECO:0007744|PDB:1SH1,
FT ECO:0007744|PDB:1SHI, ECO:0007744|PDB:2SH1"
FT DISULFID 26..44
FT /evidence="ECO:0000269|PubMed:1973932,
FT ECO:0000269|PubMed:7901218, ECO:0007744|PDB:1SH1,
FT ECO:0007744|PDB:1SHI, ECO:0007744|PDB:2SH1"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1SH1"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2SH1"
FT STRAND 13..25
FT /evidence="ECO:0007829|PDB:1SH1"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1SH1"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1SH1"
SQ SEQUENCE 48 AA; 5143 MW; 5224DF20D6D4EF5F CRC64;
AACKCDDEGP DIRTAPLTGT VDLGSCNAGW EKCASYYTII ADCCRKKK
