ID   O16A_CONTU              Reviewed;          26 AA.
AC   P58915;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Omega-conotoxin TVIA;
DE   AltName: Full=SNX-185;
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-4; PRO-10 AND PRO-21, SYNTHESIS, AND
RP   DISULFIDE BONDS.
RX   PubMed=8537186; DOI=10.1111/j.1399-3011.1995.tb00604.x;
RA   Chung D., Gaur S., Bell J.R., Ramachandran J., Nadasdi L.;
RT   "Determination of disulfide bridge pattern in omega-conopeptides.";
RL   Int. J. Pept. Protein Res. 46:320-325(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-16.
RA   Miljanich G.P., Bitner R.S., Bowersox S.S., Fox J.A., Valentino K.L.,
RA   Yamashiro D.H.;
RT   "Method of treating ischemia-related neuronal damage.";
RL   Patent number US5051403, 24-SEP-1991.
RN   [3]
RP   REVIEW.
RX   PubMed=7598513; DOI=10.1146/annurev.pa.35.040195.003423;
RA   Miljanich G.P., Ramachandran J.;
RT   "Antagonists of neuronal calcium channels: structure, function, and
RT   therapeutic implications.";
RL   Annu. Rev. Pharmacol. Toxicol. 35:707-734(1995).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P58915; -.
DR   SMR; P58915; -.
DR   ConoServer; 1727; TVIA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Hydroxylation; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..26
FT                   /note="Omega-conotoxin TVIA"
FT                   /id="PRO_0000044480"
FT   MOD_RES         4
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:8537186"
FT   MOD_RES         10
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:8537186"
FT   MOD_RES         21
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:8537186"
FT   DISULFID        1..16
FT                   /evidence="ECO:0000269|PubMed:8537186"
FT   DISULFID        8..19
FT                   /evidence="ECO:0000269|PubMed:8537186"
FT   DISULFID        15..26
FT                   /evidence="ECO:0000269|PubMed:8537186"
SQ   SEQUENCE   26 AA;  2804 MW;  A70926F3871A7883 CRC64;
     CLSPGSSCSP TSYNCCRSCN PYSRKC