ID   CA13_CONLT              Reviewed;          64 AA.
AC   Q2I2R6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Alpha-conotoxin-like Lt1.3 {ECO:0000303|PubMed:16908117};
DE   AltName: Full=Lt1c;
DE   Flags: Precursor;
OS   Conus litteratus (Lettered cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Elisaconus.
OX   NCBI_TaxID=89445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=16908117; DOI=10.1016/j.ygeno.2006.06.014;
RA   Pi C., Liu J., Peng C., Liu Y., Jiang X., Zhao Y., Tang S., Wang L.,
RA   Dong M., Chen S., Xu A.;
RT   "Diversity and evolution of conotoxins based on gene expression profiling
RT   of Conus litteratus.";
RL   Genomics 88:809-819(2006).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC       similarity). Has possibly a distinct nAChR binding mode from other
CC       alpha-conotoxins, due to a different three residue motif (lacks the
CC       Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16908117}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:16908117}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; DQ345366; ABC74974.1; -; mRNA.
DR   AlphaFoldDB; Q2I2R6; -.
DR   ConoServer; 1152; Lt1C 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   Pfam; PF07365; Toxin_8; 1.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..45
FT                   /evidence="ECO:0000305|PubMed:16908117"
FT                   /id="PRO_0000315421"
FT   PEPTIDE         46..64
FT                   /note="Alpha-conotoxin-like Lt1.3"
FT                   /evidence="ECO:0000305|PubMed:16908117"
FT                   /id="PRO_0000315422"
FT   REGION          49..51
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   DISULFID        47..53
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        48..61
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   64 AA;  7500 MW;  5D03046C35525358 CRC64;
     MGMRMMFTMF LLVVLTTTVV SFNLDRESNH ENRRTSNQIT RGMWDECCDD PPCRQNNMEH
     CPAS