ID   CM31_CONTU              Reviewed;          74 AA.
AC   P0DKQ9;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Mu-conotoxin-like T3.1;
DE   Flags: Precursor;
OS   Conus tulipa (Fish-hunting cone snail) (Tulip cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX   NCBI_TaxID=6495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Olivera B.M., McIntosh M.J., Garrett J.E., Cruz L.J., Jones R.M.,
RA   Cartier G.E., Wagstaff J.D.;
RT   "Mu-conopeptides.";
RL   Patent number US6727226, 27-APR-2004.
RN   [2]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=22229737; DOI=10.1111/j.1476-5381.2012.01837.x;
RA   Favreau P., Benoit E., Hocking H.G., Carlier L., D'Hoedt D., Leipold E.,
RA   Markgraf R., Schlumberger S., Cordova M.A., Gaertner H.,
RA   Paolini-Bertrand M., Hartley O., Tytgat J., Heinemann S.H., Bertrand D.,
RA   Boelens R., Stocklin R., Molgo J.;
RT   "A novel u-conopeptide, CnIIIC, exerts potent and preferential inhibition
RT   of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine
RT   receptors.";
RL   Br. J. Pharmacol. 166:1654-1668(2012).
CC   -!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav) (By
CC       similarity). In vitro, this synthetic peptide displays a low blocking
CC       effect in mouse extensor digitorum longus muscles (IC(50)=616 nM).
CC       {ECO:0000250, ECO:0000269|PubMed:22229737}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       4 branch, since 4 residues stand between the fourth and the fifth
CC       cysteine residues.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DKQ9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..74
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000419898"
FT   PEPTIDE         51..71
FT                   /note="Mu-conotoxin-like T3.1"
FT                   /id="PRO_0000419899"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P0C350"
FT   DISULFID        53..65
FT                   /evidence="ECO:0000250|UniProtKB:P01523"
FT   DISULFID        54..70
FT                   /evidence="ECO:0000250|UniProtKB:P01523"
FT   DISULFID        60..71
FT                   /evidence="ECO:0000250|UniProtKB:P01523"
SQ   SEQUENCE   74 AA;  8269 MW;  1FC9175038E0D67B CRC64;
     MSKLGVLLTI CLLLFPLTAL PMDGDEPADR PAERMQDNIS SEQHPLFEER HGCCKGPEGC
     SSRECRPQHC CGRR