ID   CO1E_CONMR              Reviewed;          62 AA.
AC   P0CH14; U6BZE4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Conotoxin Mr1e {ECO:0000303|PubMed:18465024};
DE   AltName: Full=Mr051 {ECO:0000312|EMBL:BAO02125.1};
DE   Flags: Precursor;
OS   Conus marmoreus (Marble cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX   NCBI_TaxID=42752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=24131469; DOI=10.1186/1471-2164-14-708;
RA   Lavergne V., Dutertre S., Jin A., Lewis R.J., Taft R.J., Alewood P.F.;
RT   "Systematic interrogation of the Conus marmoreus venom duct transcriptome
RT   with ConoSorter reveals 158 novel conotoxins and 13 new gene
RT   superfamilies.";
RL   BMC Genomics 14:708-708(2013).
RN   [2]
RP   PROTEIN SEQUENCE OF 52-62, MASS SPECTROMETRY, FUNCTION, SUBCELLULAR
RP   LOCATION, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=18465024; DOI=10.1111/j.1745-7270.2008.00414.x;
RA   Wang Y., Shao X., Li M., Wang S., Chi C., Wang C.;
RT   "mr1e, a conotoxin from Conus marmoreus with a novel disulfide pattern.";
RL   Acta Biochim. Biophys. Sin. 40:391-396(2008).
CC   -!- FUNCTION: Shows excitatory effect on mice by intracranial injection,
CC       followed by rigid paralysis of the rear legs and recovering after 30
CC       min. {ECO:0000269|PubMed:18465024}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18465024}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:18465024}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1301.7; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:18465024};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; AB850745; BAO02125.1; -; mRNA.
DR   AlphaFoldDB; P0CH14; -.
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; Direct protein sequencing;
KW   Disulfide bond; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..51
FT                   /evidence="ECO:0000305|PubMed:18465024"
FT                   /id="PRO_0000451773"
FT   PEPTIDE         52..62
FT                   /note="Conotoxin Mr1e"
FT                   /evidence="ECO:0000269|PubMed:18465024"
FT                   /id="PRO_0000396800"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000269|PubMed:18465024"
FT   DISULFID        53..58
FT                   /evidence="ECO:0000269|PubMed:18465024"
SQ   SEQUENCE   62 AA;  7195 MW;  3E0741C6AC021FAC CRC64;
     MGVVLFIFLV LFPLATLQLD ADQPVERHAE NKQLLNPDER RGIILHALRK RCCHSSWCKH
     LC