ID   CA13_CONSE              Reviewed;          63 AA.
AC   P0DPM1;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Alpha-conotoxin-like Sm1.3 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus stercusmuscarum (Fly-specked cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=89452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Watkins M., Olivera B.M., Hillyard D.R., McIntosh J.M., Jones R.M.;
RT   "Alpha-conotoxin peptides.";
RL   Patent number US6797808, 28-SEP-2004.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, OXIDATION AT
RP   MET-58, AND AMIDATION AT CYS-59.
RC   TISSUE=Venom;
RX   PubMed=22709442; DOI=10.1021/pr300312h;
RA   Bhatia S., Kil Y.J., Ueberheide B., Chait B.T., Tayo L., Cruz L., Lu B.,
RA   Yates J.R. III, Bern M.;
RT   "Constrained de novo sequencing of conotoxins.";
RL   J. Proteome Res. 11:4191-4200(2012).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22709442}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22709442}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; AR584824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DPM1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Neurotoxin; Oxidation; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..43
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445060"
FT   PEPTIDE         44..59
FT                   /note="Alpha-conotoxin-like Sm1.3"
FT                   /evidence="ECO:0000305|PubMed:22709442"
FT                   /id="PRO_0000445061"
FT   MOD_RES         58
FT                   /note="Methionine sulfoxide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   MOD_RES         59
FT                   /note="Cysteine amide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   DISULFID        45..51
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   DISULFID        46..59
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
SQ   SEQUENCE   63 AA;  6692 MW;  7F0A164CE29D3815 CRC64;
     MFTVFLLVVL ATTVVSSPSD RASDGRNAAA NEKASDVIAL ALKGCCSNPV CHLEHSNMCG
     RRR