ID   FX1_CONMR               Reviewed;          93 AA.
AC   P0DM17;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Conotoxin Mr105 {ECO:0000303|PubMed:23152539};
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=23152539; DOI=10.1074/mcp.m112.021469;
RA   Dutertre S., Jin A.H., Kaas Q., Jones A., Alewood P.F., Lewis R.J.;
RT   "Deep venomics reveals the mechanism for expanded peptide diversity in cone
RT   snail venom.";
RL   Mol. Cell. Proteomics 12:312-329(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23152539}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:23152539}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the F superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DM17; -.
DR   SMR; P0DM17; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..33
FT                   /evidence="ECO:0000305|PubMed:23152539"
FT                   /id="PRO_0000444681"
FT   CHAIN           34..93
FT                   /note="Conotoxin Mr105"
FT                   /evidence="ECO:0000305|PubMed:23152539"
FT                   /id="PRO_0000444682"
SQ   SEQUENCE   93 AA;  10575 MW;  FD1FB3019CC78F2C CRC64;
     MQRGAVLLGV VALLVLWPQA GAELYDVNDP DVRAMVIDGQ KLMHDCAIAN DYIDDPWWTL
     NLGAFEEKRV YHSMLSELVF CLNAFLQRRQ QAP