I364_CONLT
ID I364_CONLT Reviewed; 81 AA.
AC D2DGD9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Conotoxin Lt6.4;
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].
RX PubMed=19428762; DOI=10.1016/j.peptides.2009.01.012;
RA Yuan D.D., Liu L., Shao X.X., Peng C., Chi C.W., Guo Z.Y.;
RT "New conotoxins define the novel I3-superfamily.";
RL Peptides 30:861-865(2009).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19428762}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:19428762}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin I3 superfamily. {ECO:0000305}.
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DR EMBL; FJ531700; ACU30046.1; -; mRNA.
DR AlphaFoldDB; D2DGD9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Disulfide bond; Knottin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..42
FT /evidence="ECO:0000255"
FT /id="PRO_0000392162"
FT PEPTIDE 43..81
FT /note="Conotoxin Lt6.4"
FT /id="PRO_0000392163"
FT DISULFID 46..60
FT /evidence="ECO:0000250"
FT DISULFID 53..65
FT /evidence="ECO:0000250"
FT DISULFID 59..80
FT /evidence="ECO:0000250"
SQ SEQUENCE 81 AA; 8564 MW; 55D8AF3B2F2A0D4F CRC64;
MKLVLAIVLI LMFLSLSAGA ETSDNGVSRG GHRPQYWPVT PPSIVCLRSG EDCENNTPCC
PGLSCRVSAD LATLKLSLAC D