ID   CMG1_CONLT              Reviewed;          83 AA.
AC   Q2I2P8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Conotoxin Lt16a {ECO:0000303|PubMed:25600641};
DE   AltName: Full=Lt16.1 {ECO:0000303|PubMed:16908117};
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).
RN   [2]
RP   FUNCTION, AND BIOASSAY.
RX   PubMed=25600641; DOI=10.1016/j.toxicon.2015.01.009;
RA   Zhou M., Wang L., Wu Y., Liu J., Sun D., Zhu X., Feng Y., Qin M., Chen S.,
RA   Xu A.;
RT   "Soluble expression and sodium channel activity of lt16a, a novel framework
RT   XVI conotoxin from the M-superfamily.";
RL   Toxicon 98:5-11(2015).
CC   -!- FUNCTION: This toxin inhibits both the TTX-sensitive and TTX-resistant
CC       sodium currents in adult rat dorsal root ganglion neurons. The
CC       inhibition on TTX-resistant sodium currents is stronger than on TTX-
CC       sensitive sodium currents (PubMed:25600641). When intracranially
CC       injected into mice, the toxin induces tremors (50 nM), spasms (100 nM),
CC       and death (200 nM) (PubMed:25600641). {ECO:0000269|PubMed:25600641}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:16908117}.
CC   -!- DOMAIN: The cysteine framework is XVI (C-C-CC). {ECO:0000305}.
CC   -!- PTM: Authors of PubMed:25600641 studied the activity of this peptide
CC       with the C-terminal Arg residue, which is probably cleaved in the
CC       native peptide. {ECO:0000305|PubMed:16908117}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; DQ345384; ABC74992.1; -; mRNA.
DR   AlphaFoldDB; Q2I2P8; -.
DR   ConoServer; 1170; LtXVIA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..54
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000315522"
FT   PEPTIDE         55..75
FT                   /note="Conotoxin Lt16a"
FT                   /id="PRO_0000315523"
FT   PROPEP          76..83
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000315524"
SQ   SEQUENCE   83 AA;  9572 MW;  842D3B285BE7D4B2 CRC64;
     MPKLGVSLFI FLVLFPLATL QLDGDQSAGR HAQERGEDLF KMYQYLRRAL ERRRTGEDFL
     EECMGGCAFD FCCKRSLRDT TSD