ID   COW2_CONTE              Reviewed;          63 AA.
AC   Q9NDA5;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Contryphan-R/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].
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   -!- 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; AF166325; AAF82245.1; -; mRNA.
DR   AlphaFoldDB; Q9NDA5; -.
DR   ConoServer; 1314; Contryphan-Tx/R 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; Hydroxylation; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..54
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000035077"
FT   PEPTIDE         55..62
FT                   /note="Contryphan-R/Tx"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000035078"
FT   REGION          23..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   63 AA;  6710 MW;  9CB3C2C4796CFFE0 CRC64;
     MGKLTILVLV AAVLLSTQAM AQGDGDQPAA RNAVPRDDNP DGPSAKFMNV QRRSGCPWEP
     WCG