ID   CA12_CONLT              Reviewed;          68 AA.
AC   Q2I2R7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Alpha-conotoxin-like Lt1.2;
DE   AltName: Full=Lt1b;
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 a distinct nAChR binding mode from other alpha-
CC       conotoxins, due to a different three residue motif (Ala-Xaa-Ala instead
CC       of the conserved Ser-Xaa-Pro motif) (By similarity).
CC       {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}.
CC   -!- CAUTION: Conotoxins Lt1.1 and Lt1.2 are the same protein. They possess
CC       a different name due to their different precursors. {ECO:0000305}.
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DR   EMBL; DQ345365; ABC74973.1; -; mRNA.
DR   AlphaFoldDB; Q2I2R7; -.
DR   ConoServer; 544; Lt1.2 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; Amidation; 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..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000315419"
FT   PEPTIDE         49..65
FT                   /note="Alpha-conotoxin-like Lt1.2"
FT                   /id="PRO_0000315420"
FT   REGION          52..54
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:Q2I2R8"
FT   MOD_RES         65
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P85886"
FT   DISULFID        50..56
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   68 AA;  7270 MW;  2F4F745DA53B2F3D CRC64;
     MGMRMMFIMF MLVVLATTVD TFTSDRALDA MNAAASNKAS RLIALAVRGC CARAACAGIH
     QELCGGRR