ID   U7A_CONTU               Reviewed;          30 AA.
AC   P58923;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Conotoxin TVIIA {ECO:0000303|PubMed:10903496, ECO:0000303|PubMed:10903497};
OS   Conus tulipa (Fish-hunting cone snail) (Tulip cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX   NCBI_TaxID=6495;
RN   [1]
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-10 AND PRO-11, SYNTHESIS, MASS
RP   SPECTROMETRY, COMPARISON WITH CONOTOXIN GS, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=10903496; DOI=10.1046/j.1432-1327.2000.01508.x;
RA   Hill J.M., Atkins A.R., Loughnan M.L., Jones A., Adams D.A., Martin R.C.,
RA   Lewis R.J., Craik D.J., Alewood P.F.;
RT   "Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 1.
RT   Isolation, characterization and chemical synthesis.";
RL   Eur. J. Biochem. 267:4642-4648(2000).
RN   [2]
RP   SYNTHESIS, STRUCTURE BY NMR, DISULFIDE BOND, AND COMPARISON WITH CONOTOXIN
RP   GS.
RX   PubMed=10903497; DOI=10.1046/j.1432-1327.2000.01507.x;
RA   Hill J.M., Alewood P.F., Craik D.J.;
RT   "Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-
RT   dimensional solution structure.";
RL   Eur. J. Biochem. 267:4649-4657(2000).
CC   -!- FUNCTION: By structural similarity with conotoxin GS, may inhibit the
CC       sodium channel (Nav). No effect was observed upon intracranial
CC       injections into mice and intraperitoneal injections into goldfish (25
CC       ug).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10903496}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:10903496}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:10903496}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- PTM: Three different forms of TVIIA exist. Pro-10 and Pro-11 of
CC       conotoxin TVIIA are hydroxylated in TVIIA, whereas Pro-10 is not
CC       hydroxylated in [Pro10]TVIIA and neither Pro-10 nor Pro-11 are
CC       hydroxylated in [Pro10,11]TVIIA. {ECO:0000269|PubMed:10903496}.
CC   -!- MASS SPECTROMETRY: Mass=3212.4; Method=Electrospray; Note=TVIIA with
CC       hydroxyPro-10 and hydroxyPro-11.;
CC       Evidence={ECO:0000269|PubMed:10903496};
CC   -!- MASS SPECTROMETRY: Mass=3196.0; Method=Electrospray; Note=[Pro10]TVIIA
CC       with hydroxyPro-11.; Evidence={ECO:0000269|PubMed:10903496};
CC   -!- MASS SPECTROMETRY: Mass=3180.0; Method=Electrospray;
CC       Note=[Pro10,Pro11]TVIIA.; Evidence={ECO:0000269|PubMed:10903496};
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DR   PDB; 1EYO; NMR; -; A=1-30.
DR   PDBsum; 1EYO; -.
DR   AlphaFoldDB; P58923; -.
DR   SMR; P58923; -.
DR   ConoServer; 1405; TVIIA.
DR   EvolutionaryTrace; P58923; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012629; Conotoxin_TVIIAGS.
DR   Pfam; PF08094; Toxin_24; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..30
FT                   /note="Conotoxin TVIIA"
FT                   /id="PRO_0000044488"
FT   MOD_RES         10
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10903496"
FT   MOD_RES         11
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10903496"
FT   DISULFID        2..14
FT                   /evidence="ECO:0000269|PubMed:10903497,
FT                   ECO:0000312|PDB:1EYO"
FT   DISULFID        9..19
FT                   /evidence="ECO:0000269|PubMed:10903497,
FT                   ECO:0000312|PDB:1EYO"
FT   DISULFID        13..24
FT                   /evidence="ECO:0000269|PubMed:10903497,
FT                   ECO:0000312|PDB:1EYO"
FT   STRAND          10..13
FT                   /evidence="ECO:0007829|PDB:1EYO"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1EYO"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:1EYO"
SQ   SEQUENCE   30 AA;  3186 MW;  D9419BC6F0DB7A30 CRC64;
     SCSGRDSRCP PVCCMGLMCS RGKCVSIYGE