ID   CT0C2_CONVE             Reviewed;          65 AA.
AC   Q9BPD5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Conotoxin VnMLCL-01;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residue.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; AF214999; AAG60427.1; -; mRNA.
DR   AlphaFoldDB; Q9BPD5; -.
DR   ConoServer; 686; VnMLCL-01 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..43
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000404985"
FT   PEPTIDE         46..64
FT                   /note="Conotoxin VnMLCL-01"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000404986"
FT   MOD_RES         64
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   65 AA;  6933 MW;  42E526E3753A22FA CRC64;
     MLCLPVFIIL LLLASPAAPN PLQTRIQSNL IRAGPEDANM KTDKRVIISG LLSSILVPLV
     NAIKG