ID   CM3G_CONCN              Reviewed;          73 AA.
AC   P0DKQ2; S6CQB9;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Conotoxin CnIIIG {ECO:0000303|PubMed:22705119};
DE   Flags: Precursor;
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, PYROGLUTAMATE
RP   FORMATION AT GLN-51, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA   Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA   Stocklin R., Favreau P.;
RT   "Large-scale discovery of conopeptides and conoproteins in the injectable
RT   venom of a fish-hunting cone snail using a combined proteomic and
RT   transcriptomic approach.";
RL   J. Proteomics 75:5215-5225(2012).
CC   -!- FUNCTION: Shows a paralytic effect in fish.
CC       {ECO:0000269|PubMed:22705119}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22705119}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       1 branch, since 1 residue stands between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2609.04; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MISCELLANEOUS: Found in injectable (milked) (IV) venom.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- MISCELLANEOUS: Surprisingly, the propeptide sequence 20-48 has been
CC       identified in the venom. It is unknown whether it is a by-product of
CC       incomplete enzymatic degradation of the precursor, or if it has a
CC       biological function on its own (PubMed:22705119).
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; HE856380; CCI55493.1; -; mRNA.
DR   AlphaFoldDB; P0DKQ2; -.
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   Cleavage on pair of basic residues; Disulfide bond; Neurotoxin;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..48
FT                   /evidence="ECO:0000305|PubMed:22705119"
FT                   /id="PRO_0000419881"
FT   PEPTIDE         51..73
FT                   /note="Conotoxin CnIIIG"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT                   /id="PRO_0000419882"
FT   MOD_RES         51
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT   DISULFID        53..72
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        54..70
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        60..73
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ   SEQUENCE   73 AA;  8263 MW;  FBE1F59DC26A0F08 CRC64;
     MSKLGVLLTI CLLLLPLTAL PMDEDQPADQ PADRMQDDIS SEQYPLFDKR QKCCGKGMTC
     PRYFRDNFIC GCC