ID   COW_CONVE               Reviewed;           9 AA.
AC   P83047;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Contryphan-Vn {ECO:0000303|PubMed:11688995, ECO:0000303|PubMed:12646193, ECO:0000303|PubMed:15150794};
OS   Conus ventricosus (Mediterranean cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lautoconus.
OX   NCBI_TaxID=117992;
RN   [1]
RP   PROTEIN SEQUENCE, D-AMINO ACID AT TRP-5, AMIDATION AT CYS-9, DISULFIDE
RP   BONDS, SYNTHESIS, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11688995; DOI=10.1006/bbrc.2001.5833;
RA   Massilia G.R., Schinina M.E., Ascenzi P., Polticelli F.;
RT   "Contryphan-Vn: a novel peptide from the venom of the Mediterranean snail
RT   Conus ventricosus.";
RL   Biochem. Biophys. Res. Commun. 288:908-913(2001).
RN   [2]
RP   FUNCTION, SYNTHESIS, STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=12646193; DOI=10.1016/s0006-291x(03)00331-0;
RA   Massilia G.R., Eliseo T., Grolleau F., Lapied B., Barbier J., Bournaud R.,
RA   Molgo J., Cicero D.O., Paci M., Schinina M.E., Ascenzi P., Polticelli F.;
RT   "Contryphan-Vn: a modulator of Ca2+-dependent K+ channels.";
RL   Biochem. Biophys. Res. Commun. 303:238-246(2003).
RN   [3]
RP   STRUCTURE BY NMR, DISULFIDE BONDS, AND CIS-TRANS ISOMERIZATION.
RX   PubMed=15150794; DOI=10.1002/bip.20025;
RA   Eliseo T., Cicero D.O., Romeo C., Schinina M.E., Massilia G.R.,
RA   Polticelli F., Ascenzi P., Paci M.;
RT   "Solution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent
RT   K+ channel modulator.";
RL   Biopolymers 74:189-198(2004).
CC   -!- FUNCTION: Affects both voltage-gated (Kv) and calcium-dependent
CC       potassium channel activities (KCa), with composite and diversified
CC       effects in invertebrate and vertebrate systems (PubMed:12646193). In
CC       vivo, intramuscular injection in freshwater fishes (Poecelia pinnata)
CC       causes secretion of mucous substances, a reaction already observed in
CC       fish with other contryphans (PubMed:12646193).
CC       {ECO:0000269|PubMed:12646193}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11688995}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:11688995}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1088.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11688995};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       3-Cys-Pro-4. The cis isomer is the most abundant and is thus thought to
CC       be the functionally relevant conformer. {ECO:0000269|PubMed:15150794}.
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   PDB; 1NXN; NMR; -; A=1-9.
DR   PDBsum; 1NXN; -.
DR   ConoServer; 1309; Contryphan-Vn.
DR   EvolutionaryTrace; P83047; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011062; Contryphan_CS.
DR   PROSITE; PS60027; CONTRYPHAN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation;
KW   Calcium-activated potassium channel impairing toxin; D-amino acid;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..9
FT                   /note="Contryphan-Vn"
FT                   /evidence="ECO:0000269|PubMed:11688995"
FT                   /id="PRO_0000044506"
FT   MOD_RES         5
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000269|PubMed:11688995"
FT   MOD_RES         9
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:11688995"
FT   DISULFID        3..9
FT                   /evidence="ECO:0000269|PubMed:11688995,
FT                   ECO:0000269|PubMed:12646193, ECO:0000269|PubMed:15150794"
SQ   SEQUENCE   9 AA;  1091 MW;  8D38676323676EBA CRC64;
     GDCPWKPWC