ID   O16L_CONTE              Reviewed;          81 AA.
AC   Q9U645;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Omega-conotoxin-like TxMKLT1-0223;
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; AF193271; AAF07982.1; -; mRNA.
DR   AlphaFoldDB; Q9U645; -.
DR   SMR; Q9U645; -.
DR   ConoServer; 1104; Tx6.4 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; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Signal; Toxin; Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..52
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404770"
FT   PEPTIDE         53..81
FT                   /note="Omega-conotoxin-like TxMKLT1-0223"
FT                   /id="PRO_0000404771"
FT   DISULFID        55..72
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        62..76
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   81 AA;  8975 MW;  BF66C1FF284B8F2B CRC64;
     MKLTCMMIVA VLFLTAWTFV TAVPHSSNAL ENLYLKARHE MENPEASKLN TRDDCEPPGN
     FCGMIKIGPP CCSGWCFFAC A