ID   O168_CONVE              Reviewed;          78 AA.
AC   Q9BPA5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Omega-conotoxin-like VnMKLT1-0111;
DE   Flags: Precursor;
OS   Conus ventricosus (Mediterranean cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lautoconus.
OX   NCBI_TaxID=117992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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. {ECO:0000250}.
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   EMBL; AF215032; AAG60460.1; -; mRNA.
DR   AlphaFoldDB; Q9BPA5; -.
DR   SMR; Q9BPA5; -.
DR   ConoServer; 719; Vn6.8 precursor.
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; IPR004214; Conotoxin.
DR   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   2: Evidence at transcript level;
KW   Calcium channel impairing toxin; Cleavage on pair of basic residues;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404780"
FT   PEPTIDE         51..78
FT                   /note="Omega-conotoxin-like VnMKLT1-0111"
FT                   /id="PRO_0000404781"
FT   DISULFID        52..69
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        59..73
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        68..77
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   78 AA;  8661 MW;  AED563E95C903928 CRC64;
     MKLTCMMIVA VLFLTAWTFV TADSRNGLEY LFPKAHYEMN PEASKLNKKR DCVAGGHFCG
     FPKIGGPCCS GWCFFVCA