ID   O3627_CONAE             Reviewed;          77 AA.
AC   Q9BP68;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Conotoxin ArMSGL-0141;
DE   Flags: Precursor;
OS   Conus arenatus (Sand-dusted cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=89451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin O3 superfamily. {ECO:0000305}.
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DR   EMBL; AF215070; AAG60498.1; -; mRNA.
DR   AlphaFoldDB; Q9BP68; -.
DR   SMR; Q9BP68; -.
DR   ConoServer; 757; Ar6.27 precursor.
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   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Knottin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..44
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404858"
FT   PEPTIDE         47..76
FT                   /note="Conotoxin ArMSGL-0141"
FT                   /id="PRO_0000404859"
FT   MOD_RES         76
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..75
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   77 AA;  8556 MW;  15E36B83AF41DFFB CRC64;
     MSGLGILVLT LLLLVYMATS HQDAGEKQAT QRDAINVRRR RSLTRRVAEE CEESCEDEEK
     HCCNTNNGPS CAPQCFG