ID   COWL_CONPU              Reviewed;           8 AA.
AC   P58785;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 1.
DT   23-FEB-2022, entry version 56.
DE   RecName: Full=Leu-contryphan-P {ECO:0000303|PubMed:10461743};
OS   Conus purpurascens (Purple cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX   NCBI_TaxID=41690;
RN   [1]
RP   PROTEIN SEQUENCE, D-AMINO ACID AT LEU-4, DISULFIDE BOND, SYNTHESIS, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=Clipperton Island; TISSUE=Venom;
RX   PubMed=10461743; DOI=10.1034/j.1399-3011.1999.00093.x;
RA   Jacobsen R.B., Jimenez E.C., De la Cruz R.G.C., Gray W.R., Cruz L.J.,
RA   Olivera B.M.;
RT   "A novel D-leucine-containing Conus peptide: diverse conformational
RT   dynamics in the contryphan family.";
RL   J. Pept. Res. 54:93-99(1999).
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:10461743}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:10461743}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=888.4; Method=LSI;
CC       Evidence={ECO:0000269|PubMed:10461743};
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   ConoServer; 1313; contryphan-P [D5>L].
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.
DR   PROSITE; PS60027; CONTRYPHAN; 1.
PE   1: Evidence at protein level;
KW   D-amino acid; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..8
FT                   /note="Leu-contryphan-P"
FT                   /evidence="ECO:0000269|PubMed:10461743"
FT                   /id="PRO_0000044505"
FT   MOD_RES         4
FT                   /note="D-leucine"
FT                   /evidence="ECO:0000269|PubMed:10461743"
FT   DISULFID        2..8
FT                   /evidence="ECO:0000269|PubMed:10461743"
SQ   SEQUENCE   8 AA;  890 MW;  75A367672732CEB8 CRC64;
     GCVLLPWC