CMG1_CONLT
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