ID   COW1_CONLI              Reviewed;          63 AA.
AC   A0A1P8NVS2;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Contryphan-Li1 {ECO:0000305};
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=28152596; DOI=10.1021/acs.jproteome.6b00776;
RA   Vijayasarathy M., Basheer S.M., Franklin J.B., Balaram P.;
RT   "Contryphan genes and mature peptides in the venom of nine cone snail
RT   species by transcriptomic and mass spectrometric analysis.";
RL   J. Proteome Res. 16:763-772(2017).
CC   -!- FUNCTION: Its target is unknown, but this toxin may modulate voltage-
CC       activated calcium channels (Cav) or calcium-dependent potassium
CC       channels (KCa). {ECO:0000250|UniProtKB:P0C248,
CC       ECO:0000250|UniProtKB:P0C250, ECO:0000250|UniProtKB:P62903,
CC       ECO:0000250|UniProtKB:P83047}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28152596}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:28152596}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       56-Cys-hydroxyPro-57. The cis conformation is the major form.
CC       {ECO:0000250|UniProtKB:P58787}.
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   EMBL; KX289879; APX52856.1; -; mRNA.
DR   AlphaFoldDB; A0A1P8NVS2; -.
DR   ConoServer; 9758; Contryphan-Li1 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   InterPro; IPR011062; Contryphan_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60027; CONTRYPHAN; 1.
PE   3: Inferred from homology;
KW   Amidation; D-amino acid; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..54
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445131"
FT   PEPTIDE         55..62
FT                   /note="Contryphan-Li1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5012704268"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   MOD_RES         58
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   DISULFID        56..62
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
SQ   SEQUENCE   63 AA;  6663 MW;  B9F2344E9A87A4BC CRC64;
     MEKLTMLVLV AAVLLSAQVM VQGDGDQPAD RDAVPRDDNP GGTIGKIMNV LLPSGCPWNP
     WCG