ID   O16K_CONTE              Reviewed;          76 AA.
AC   Q9U654;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Omega-conotoxin-like TxO5;
DE   AltName: Full=Conotoxin TxMKLT1-012;
DE   Flags: Precursor;
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
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; AF193262; AAF07973.1; -; mRNA.
DR   AlphaFoldDB; Q9U654; -.
DR   SMR; Q9U654; -.
DR   ConoServer; 1095; TxO5 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_0000404708"
FT   PEPTIDE         51..76
FT                   /note="Omega-conotoxin-like TxO5"
FT                   /id="PRO_0000404709"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..75
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   76 AA;  8628 MW;  AF2E937B4F41DF1D CRC64;
     MKLTCMMIVA VLFLTAWTFV TAITSNGLEN LFPKAHHEMK NPEASKLNKR CVPYEGPCNW
     LTQNCCDATC VVFWCL