ID   CMCC1_CONPO             Reviewed;          67 AA.
AC   D5L5Q7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Conopeptide Vt3.1;
DE   Flags: Precursor;
OS   Conus planorbis (Planorbis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Strategoconus.
OX   NCBI_TaxID=97183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 54-67, AMIDATION AT ILE-66,
RP   FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom duct;
RX   PubMed=20307606; DOI=10.1016/j.peptides.2010.03.010;
RA   Wu X.-C., Zhou M., Peng C., Shao X.-X., Guo Z.-Y., Chi C.-W.;
RT   "Novel conopeptides in a form of disulfide-crosslinked dimer.";
RL   Peptides 31:1001-1006(2010).
CC   -!- FUNCTION: The homodimer-1 (C-62 linked to C-64) causes a reversible
CC       hyperactivity (jumping, rapid circling and tail flicking), when
CC       intraventricularly injected into the brains of mice. Monomer and
CC       homodimer-2 have no activity. {ECO:0000269|PubMed:20307606}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Found in vitro with synthetic
CC       peptides. {ECO:0000269|PubMed:20307606}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is C-C.
CC   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residue.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
CC   -!- CAUTION: The name Vt3.1 given by the authors is incorrect, since the
CC       first number indicates a cysteine framework III which does not
CC       correspond to this cysteine framework. {ECO:0000305|PubMed:20307606}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GU784862; ADE35088.1; -; mRNA.
DR   AlphaFoldDB; D5L5Q7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Pfam; PF02950; Conotoxin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..50
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397201"
FT   PEPTIDE         54..66
FT                   /note="Conopeptide Vt3.1"
FT                   /id="PRO_0000397202"
FT   MOD_RES         66
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000305|PubMed:20307606"
FT   DISULFID        62
FT                   /note="Interchain (with C-64, dimer-1; with C-62, dimer-2)"
FT                   /evidence="ECO:0000305"
FT   DISULFID        64
FT                   /note="Interchain (with C-62, dimer-1; with C-62, dimer-2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   67 AA;  7742 MW;  6EC511D82674A761 CRC64;
     MLKMGVVLFI FLVLFPLATL QLNADQPVER NAENIQDLNP DKRVIKIPVP RRRGPYRRYG
     NCYCPIG