ID   CA11_CONSE              Reviewed;          61 AA.
AC   P0C8V1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Alpha-conotoxin-like Sm1.1 {ECO:0000305};
DE   Contains:
DE     RecName: Full=Alpha-conotoxin-like Sm1.1 b {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 [MRNA], AND REVIEW.
RC   TISSUE=Venom duct;
RX   PubMed=16905531; DOI=10.1074/jbc.r600020200;
RA   Olivera B.M.;
RT   "Conus peptides: biodiversity-based discovery and exogenomics.";
RL   J. Biol. Chem. 281:31173-31177(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, HYDROXYLATION AT
RP   PRO-55, 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   AlphaFoldDB; P0C8V1; -.
DR   ConoServer; 2981; Sm1.1 precursor.
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:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   InterPro; IPR018072; Conotoxin_a-typ_CS.
DR   Pfam; PF07365; Toxin_8; 1.
DR   PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..43
FT                   /evidence="ECO:0000305|PubMed:22709442"
FT                   /id="PRO_0000366070"
FT   PEPTIDE         46..59
FT                   /note="Alpha-conotoxin-like Sm1.1"
FT                   /evidence="ECO:0000305|PubMed:22709442"
FT                   /id="PRO_0000366071"
FT   PEPTIDE         48..59
FT                   /note="Alpha-conotoxin-like Sm1.1 b"
FT                   /evidence="ECO:0000305|PubMed:22709442"
FT                   /id="PRO_0000445111"
FT   REGION          19..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   MOD_RES         59
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   DISULFID        48..53
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   DISULFID        49..59
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
SQ   SEQUENCE   61 AA;  6692 MW;  496320B3FBCA2248 CRC64;
     MFTVFLLVVL ATTVVSFPSD RASDGRDDEA KDERSDMHES GRKGRGRCCH PACGPNYSCG
     R