ID   CA1C_CONLI              Reviewed;          31 AA.
AC   H9N3R7;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Alpha-conotoxin Li1.12;
DE   AltName: Full=Livi_23 {ECO:0000303|PubMed:22337864};
DE   Flags: Precursor; Fragment;
OS   Conus lividus (Livid cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX   NCBI_TaxID=89426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=22337864; DOI=10.1093/molbev/mss068;
RA   Chang D., Duda T.F. Jr.;
RT   "Extensive and continuous duplication facilitates rapid evolution and
RT   diversification of gene families.";
RL   Mol. Biol. Evol. 29:2019-2029(2012).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       This toxin inhibits alpha-3-beta-4, alpha-6/alpha-3-beta-4, and alpha-
CC       2-beta-4 nAChRs. {ECO:0000250|UniProtKB:K8DWB5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/6 pattern.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: This toxin does not show inhibition at neuronal alpha-4-
CC       beta-4, alpha-4-beta-2, alpha-6/alpha-3-beta-2-beta-3, alpha-3-beta-2,
CC       alpha-2-beta-2, alpha-9-alpha-10, alpha-7 nAChRs and muscle alpha-1-
CC       beta-1-delta-epsilon nAChR. {ECO:0000250|UniProtKB:K8DWB5}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; JF723419; AFD18484.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9N3R7; -.
DR   SMR; H9N3R7; -.
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   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT   PROPEP          <1..15
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000439432"
FT   PEPTIDE         16..30
FT                   /note="Alpha-conotoxin Li1.12"
FT                   /evidence="ECO:0000250|UniProtKB:K8DWB5"
FT                   /id="PRO_0000439433"
FT   MOD_RES         30
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:K8DWB5"
FT   DISULFID        17..23
FT                   /evidence="ECO:0000250|UniProtKB:K8DWB5"
FT   DISULFID        18..30
FT                   /evidence="ECO:0000250|UniProtKB:K8DWB5"
FT   NON_TER         1
SQ   SEQUENCE   31 AA;  3082 MW;  79DAD3E923F46113 CRC64;
     AGNAKMSALM ALTIRGCCSH PVCSAMSPIC G