ID   COWC_CONFI              Reviewed;           8 AA.
AC   P0DP14;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   23-FEB-2022, entry version 10.
DE   RecName: Full=Contryphan-Fic {ECO:0000303|PubMed:25420928};
DE   Contains:
DE     RecName: Full=Contryphan-Fid {ECO:0000303|PubMed:25420928};
OS   Conus figulinus (Fig cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX   NCBI_TaxID=101301;
RN   [1]
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=25420928; DOI=10.1002/psc.2715;
RA   Rajesh R.P.;
RT   "Novel M-Superfamily and T-Superfamily conotoxins and contryphans from the
RT   vermivorous snail Conus figulinus.";
RL   J. Pept. Sci. 21:29-39(2015).
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:0000269|PubMed:25420928}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:25420928}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- PTM: These peptides are not hydroxylated and not amidated, and no D-
CC       amino acid are detected. {ECO:0000269|PubMed:25420928}.
CC   -!- MASS SPECTROMETRY: [Contryphan-Fic]: Mass=959.5; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:25420928};
CC   -!- MASS SPECTROMETRY: [Contryphan-Fid]: Mass=902.4; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:25420928};
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011062; Contryphan_CS.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..8
FT                   /note="Contryphan-Fic"
FT                   /evidence="ECO:0000269|PubMed:25420928"
FT                   /id="PRO_0000439625"
FT   PEPTIDE         2..8
FT                   /note="Contryphan-Fid"
FT                   /evidence="ECO:0000269|PubMed:25420928"
FT                   /id="PRO_0000439626"
FT   DISULFID        2..8
FT                   /evidence="ECO:0000269|PubMed:25420928"
SQ   SEQUENCE   8 AA;  963 MW;  75A3676AB3676EB8 CRC64;
     GCPWDPWC