CT54_CONLT
ID CT54_CONLT Reviewed; 62 AA.
AC Q1A3R1; Q1A3Q3; Q1A3Q4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Mu-conotoxin Lt5d {ECO:0000303|PubMed:17961831};
DE AltName: Full=Lt5.4 {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], AND VARIANTS LT5.4.1 SER-55 AND LT5.4.2 ASN-56.
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 SYNTHESIS OF 51-62.
RX PubMed=23567999; DOI=10.1016/j.bcp.2013.03.019;
RA Petrel C., Hocking H.G., Reynaud M., Upert G., Favreau P., Biass D.,
RA Paolini-Bertrand M., Peigneur S., Tytgat J., Gilles N., Hartley O.,
RA Boelens R., Stocklin R., Servent D.;
RT "Identification, structural and pharmacological characterization of tau-
RT CnVA, a conopeptide that selectively interacts with somatostatin sst
RT receptor.";
RL Biochem. Pharmacol. 85:1663-1671(2013).
RN [3]
RP PROTEIN SEQUENCE OF 51-62, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=17961831; DOI=10.1016/j.peptides.2007.09.006;
RA Liu J., Wu Q., Pi C., Zhao Y., Zhou M., Wang L., Chen S., Xu A.;
RT "Isolation and characterization of a T-superfamily conotoxin from Conus
RT litteratus with targeting tetrodotoxin-sensitive sodium channels.";
RL Peptides 28:2313-2319(2007).
CC -!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). This
CC toxin inhibits tetrodotoxin(TTX)-sensitive sodium channels, but does
CC not affect TTX-resistant sodium channels. Reduces the amplitude of
CC currents without changing the activation and inactivation kinetics of
CC currents. {ECO:0000269|PubMed:17961831}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17961831}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:17961831}.
CC -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC 'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC and AC P81755). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1274.8778; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17961831};
CC -!- MISCELLANEOUS: Does not have the ability to interact with the G-protein
CC coupled somatostatin type 3 receptor (SSTR3).
CC {ECO:0000305|PubMed:23567999}.
CC -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR EMBL; DQ345353; ABC70189.1; -; mRNA.
DR EMBL; DQ345360; ABC70196.1; -; mRNA.
DR EMBL; DQ345361; ABC70197.1; -; mRNA.
DR AlphaFoldDB; Q1A3R1; -.
DR ConoServer; 1140; Lt5d precursor.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0044489; P:negative regulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
DR InterPro; IPR031565; T-conotoxin.
DR Pfam; PF16981; Chi-conotoxin; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..48
FT /id="PRO_0000315427"
FT PEPTIDE 51..62
FT /note="Mu-conotoxin Lt5d"
FT /id="PRO_0000315428"
FT VARIANT 55
FT /note="A -> S (in Lt5.4.1)"
FT /evidence="ECO:0000269|PubMed:16908117"
FT VARIANT 56
FT /note="K -> N (in Lt5.4.2)"
FT /evidence="ECO:0000269|PubMed:16908117"
SQ SEQUENCE 62 AA; 6907 MW; D9F0575D4EAD468E CRC64;
MRCLPVFIIL LLLIPSAPSV DAQPTTKDDV PLASLHDNAK RALQMFWNKR DCCPAKLLCC
NP
