ID   COWW_CONPU              Reviewed;          63 AA.
AC   P58784;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Contryphan-P {ECO:0000303|PubMed:11041849, ECO:0000303|PubMed:9531419};
DE   AltName: Full=Trp-Contryphan-P {ECO:0000303|PubMed:9531419};
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Gulf of California; TISSUE=Venom duct;
RX   PubMed=9531419; DOI=10.1111/j.1399-3011.1998.tb01213.x;
RA   Jacobsen R.B., Jimenez E.C., Grilley M., Watkins M., Hillyard D.R.,
RA   Cruz L.J., Olivera B.M.;
RT   "The contryphans, a D-tryptophan-containing family of Conus peptides:
RT   interconversion between conformers.";
RL   J. Pept. Res. 51:173-179(1998).
RN   [2]
RP   CIS-TRANS ISOMERIZATION.
RX   PubMed=11041849; DOI=10.1021/bi0010930;
RA   Pallaghy P.K., He W., Jimenez E.C., Olivera B.M., Norton R.S.;
RT   "Structures of the contryphan family of cyclic peptides. Role of
RT   electrostatic interactions in cis-trans isomerism.";
RL   Biochemistry 39:12845-12852(2000).
RN   [3]
RP   MASS SPECTROMETRY, HYDROXYLATION AT PRO-57, D-AMINO ACID AT TRP-58,
RP   AMIDATION AT CYS-62, AND SUBCELLULAR LOCATION.
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:9531419}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=975.35; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:28152596};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       56-Cys-hydroxyPro-57. {ECO:0000305|PubMed:11041849}.
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P58784; -.
DR   SMR; P58784; -.
DR   ConoServer; 1312; Contryphan-P precursor.
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   1: Evidence at protein level;
KW   Amidation; D-amino acid; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..54
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT                   /id="PRO_0000035068"
FT   PEPTIDE         55..62
FT                   /note="Contryphan-P"
FT                   /evidence="ECO:0000269|PubMed:28152596"
FT                   /id="PRO_0000035069"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT   MOD_RES         58
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT   DISULFID        56..62
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
SQ   SEQUENCE   63 AA;  6729 MW;  5FA43CD39D7676D1 CRC64;
     MGKLTILVLV AAVLLSTQVM VQGDGDQPAY RNAAPRDDNP GGAIGKFMNV LRRSGCPWDP
     WCG