O3628_CONAE
ID O3628_CONAE Reviewed; 39 AA.
AC Q9BP50;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Conotoxin ArMSGL-013;
DE Flags: Precursor; Fragment;
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. {ECO:0000305}.
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; AF215107; AAG60528.1; -; mRNA.
DR AlphaFoldDB; Q9BP50; -.
DR SMR; Q9BP50; -.
DR ConoServer; 785; Ar6.28 precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Disulfide bond; Knottin;
KW Neurotoxin; Secreted; Toxin.
FT PROPEP <1..5
FT /id="PRO_0000404860"
FT PEPTIDE 8..38
FT /note="Conotoxin ArMSGL-013"
FT /id="PRO_0000404861"
FT MOD_RES 38
FT /note="Tryptophan amide"
FT /evidence="ECO:0000250"
FT DISULFID 12..24
FT /evidence="ECO:0000250"
FT DISULFID 16..33
FT /evidence="ECO:0000250"
FT DISULFID 23..37
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 39 AA; 4551 MW; 1C4D2343C0BC115E CRC64;
RRSLTRRVPE ECEESCEEEE KTCCGLENGQ PFCSRICWG