ID   COW_CONGE               Reviewed;          63 AA.
AC   X5IFY8;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Contryphan-G {ECO:0000303|PubMed:24662800};
DE   Flags: Precursor;
OS   Conus geographus (Geography cone) (Nubecula geographus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX   NCBI_TaxID=6491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=24662800; DOI=10.1038/ncomms4521;
RA   Dutertre S., Jin A.-H., Vetter I., Hamilton B., Sunagar K., Lavergne V.,
RA   Dutertre V., Fry B.G., Antunes A., Venter D.J., Alewood P.F., Lewis R.J.;
RT   "Evolution of separate predation- and defence-evoked venoms in carnivorous
RT   cone snails.";
RL   Nat. Commun. 5:3521-3521(2014).
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:24662800}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:24662800}.
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; AB910805; BAO65573.1; -; mRNA.
DR   AlphaFoldDB; X5IFY8; -.
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; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..54
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445140"
FT   PEPTIDE         55..62
FT                   /note="Contryphan-G"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5004956815"
FT   REGION          24..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"
FT   DISULFID        56..62
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
SQ   SEQUENCE   63 AA;  6738 MW;  9CB3D166F357FFE0 CRC64;
     MGKLTILVLV AAVLLSTQAM VQGDGDQPAA RNAVPRDDNP DGPSAKFMNV QRRSGCPWEP
     WCG