T3A_TERVA
ID T3A_TERVA Reviewed; 21 AA.
AC A0A0B4J184;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Venom peptide Tv1 {ECO:0000303|PubMed:24713808};
DE AltName: Full=Teretoxin v3a {ECO:0000305};
OS Terebra variegata (Variegate auger snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Terebridae; Terebra.
OX NCBI_TaxID=1167563;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP STRUCTURE BY NMR, DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=24713808; DOI=10.1371/journal.pone.0094122;
RA Anand P., Grigoryan A., Bhuiyan M.H., Ueberheide B., Russell V.,
RA Quinonez J., Moy P., Chait B.T., Poget S.F., Holford M.;
RT "Sample limited characterization of a novel disulfide-rich venom peptide
RT toxin from terebrid marine snail Terebra variegata.";
RL PLoS ONE 9:E94122-E94122(2014).
CC -!- FUNCTION: Injections of 20 uM of this synthetic peptide (Ile) causes
CC partial paralysis to polychaete worms (Nereis virens), the natural prey
CC of terebrid snails (PubMed:24713808). This paralysis may be due to an
CC inhibition of nicotinic receptors at the neuromuscular junction
CC (Probable). {ECO:0000269|PubMed:24713808, ECO:0000305|PubMed:24713808}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24713808}.
CC -!- TISSUE SPECIFICITY: Expressed by the salivary gland. This peptide is
CC considered as a venom peptide. {ECO:0000305|PubMed:24713808}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 3 branch, since 3 residues stand between the fourth and the fifth
CC cysteine residues. This peptide has a cysteine scaffold similar to the
CC M superfamily of conotoxins, but it displays a disulfide pattern
CC previously unknown in native cone snail peptides.
CC {ECO:0000305|PubMed:24713808}.
CC -!- CAUTION: It is unsure whether the 3rd residue is an Ile or a Leu. NMR
CC structural calculations were carried out using only the Ile-3 form of
CC the peptide. {ECO:0000305|PubMed:24713808}.
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DR PDB; 2MIX; NMR; -; A=1-21.
DR PDBsum; 2MIX; -.
DR AlphaFoldDB; A0A0B4J184; -.
DR SMR; A0A0B4J184; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..21
FT /note="Venom peptide Tv1"
FT /id="PRO_0000435098"
FT DISULFID 4..20
FT /evidence="ECO:0000269|PubMed:24713808"
FT DISULFID 5..21
FT /evidence="ECO:0000269|PubMed:24713808"
FT DISULFID 7..16
FT /evidence="ECO:0000269|PubMed:24713808"
FT UNSURE 3
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:24713808"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2MIX"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2MIX"
SQ SEQUENCE 21 AA; 2317 MW; 3ACA754531DD4D12 CRC64;
TRICCGCYWN GSKDVCSQSC C