ID   COW3_CONTE              Reviewed;          63 AA.
AC   Q9NDA6;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Leu-contryphan-Tx;
DE   Flags: Precursor;
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], D-AMINO ACID AT LEU-58, AMIDATION AT CYS-62,
RP   SYNTHESIS OF 56-62, AND MASS SPECTROMETRY.
RC   TISSUE=Venom duct;
RX   PubMed=11137539; DOI=10.1016/s0041-0101(00)00210-5;
RA   Jimenez E.C., Watkins M., Juszczak L.J., Cruz L.J., Olivera B.M.;
RT   "Contryphans from Conus textile venom ducts.";
RL   Toxicon 39:803-808(2001).
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:11137539}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:11137539}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=880.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11137539};
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {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; AF166324; AAF82244.1; -; mRNA.
DR   AlphaFoldDB; Q9NDA6; -.
DR   ConoServer; 1315; Leu-contryphan-Tx 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   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; D-amino acid;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..55
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000035079"
FT   PEPTIDE         56..62
FT                   /note="Leu-contryphan-Tx"
FT                   /evidence="ECO:0000305|PubMed:11137539"
FT                   /id="PRO_0000035080"
FT   REGION          23..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         58
FT                   /note="D-leucine"
FT                   /evidence="ECO:0000305|PubMed:11137539"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:11137539"
SQ   SEQUENCE   63 AA;  6678 MW;  2A910957B7E44BB1 CRC64;
     MGKLTILVLV AAVLLSAQVM VQGDGDQPAD RKAVPREDNP GGASGKLMDV LRPKKCVLYP
     WCG