ID   COW2_CONFG              Reviewed;           8 AA.
AC   P0DPQ2;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   23-FEB-2022, entry version 6.
DE   RecName: Full=Contryphan-Fr2 {ECO:0000305};
DE   AltName: Full=Fr965 {ECO:0000303|PubMed:28152596};
OS   Conus frigidus (Frigid cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virgiconus.
OX   NCBI_TaxID=101755;
RN   [1]
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-3, D-AMINO ACID AT TRP-4,
RP   AMIDATION AT CYS-8, AND DISULFIDE BOND.
RC   TISSUE=Venom;
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:0000269|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   -!- MASS SPECTROMETRY: Mass=965.43; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:28152596};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       2-Cys-hydroxyPro-3. 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   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   PROSITE; PS60027; CONTRYPHAN; 1.
PE   1: Evidence at protein level;
KW   Amidation; D-amino acid; Direct protein sequencing; Disulfide bond;
KW   Hydroxylation; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..8
FT                   /note="Contryphan-Fr2"
FT                   /evidence="ECO:0000269|PubMed:28152596"
FT                   /id="PRO_0000445269"
FT   MOD_RES         3
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:28152596"
FT   MOD_RES         4
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT   MOD_RES         8
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:28152596"
FT   DISULFID        2..8
FT                   /evidence="ECO:0000269|PubMed:28152596"
SQ   SEQUENCE   8 AA;  953 MW;  75A365BAB3676EB8 CRC64;
     GCPWDSWC