ID   CT33_CONLI              Reviewed;          67 AA.
AC   Q3YEH4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Conotoxin LiC33 {ECO:0000303|PubMed:16999774};
DE   Flags: Precursor;
OS   Conus lividus (Livid cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX   NCBI_TaxID=89426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=16999774; DOI=10.1111/j.1747-0285.2006.00422.x;
RA   Luo S., Zhangsun D., Wu Y., Zhu X., Xie L., Hu Y., Zhang J., Zhao X.;
RT   "Identification and molecular diversity of T-superfamily conotoxins from
RT   Conus lividus and Conus litteratus.";
RL   Chem. Biol. Drug Des. 68:97-106(2006).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC).
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   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ141139; AAZ85404.1; -; mRNA.
DR   AlphaFoldDB; Q3YEH4; -.
DR   ConoServer; 1676; LiC33 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000274059"
FT   PEPTIDE         50..63
FT                   /note="Conotoxin LiC33"
FT                   /id="PRO_0000274060"
FT   PROPEP          65..67
FT                   /id="PRO_0000274061"
FT   MOD_RES         63
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   67 AA;  7552 MW;  EE80EBBC88C18FFD CRC64;
     MRCVPVFIIL LLLSPSAPSV DAHPKTKDDV PLASFHDDAK RTLQRLWIKA LCCYGYRFCC
     PIFGKGK