ID   COW_CONSE               Reviewed;          63 AA.
AC   P58787;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Contryphan-Sm {ECO:0000303|PubMed:11041849, ECO:0000303|PubMed:9531419};
DE   Flags: Precursor;
OS   Conus stercusmuscarum (Fly-specked cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=89452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 55-62, HYDROXYLATION AT
RP   PRO-57, D-AMINO ACID AT TRP-58, AMIDATION AT CYS-62, SYNTHESIS OF 55-62,
RP   MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and 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   STRUCTURE BY NMR OF 55-61 (MAJOR (CIS) AND MINOR (TRANS) CONFORMERS),
RP   DISULFIDE BONDS, AND 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).
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:9531419}.
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=989.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9531419};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       56-Cys-hydroxyPro-57. The cis conformation is the major form.
CC       {ECO:0000269|PubMed:11041849}.
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   PDB; 1DFY; NMR; -; A=55-62.
DR   PDB; 1DFZ; NMR; -; A=55-62.
DR   PDBsum; 1DFY; -.
DR   PDBsum; 1DFZ; -.
DR   AlphaFoldDB; P58787; -.
DR   SMR; P58787; -.
DR   ConoServer; 1311; Contryphan-Sm precursor.
DR   EvolutionaryTrace; P58787; -.
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   3D-structure; Amidation; D-amino acid; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..54
FT                   /evidence="ECO:0000269|PubMed:9531419"
FT                   /id="PRO_0000035073"
FT   PEPTIDE         55..62
FT                   /note="Contryphan-Sm"
FT                   /evidence="ECO:0000269|PubMed:9531419"
FT                   /id="PRO_0000035074"
FT   REGION          23..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:9531419"
FT   MOD_RES         58
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000269|PubMed:9531419"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:9531419"
FT   DISULFID        56..62
FT                   /evidence="ECO:0000269|PubMed:11041849,
FT                   ECO:0000312|PDB:1DFY, ECO:0000312|PDB:1DFZ"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1DFY"
SQ   SEQUENCE   63 AA;  6859 MW;  7B3A33D50721A89C CRC64;
     MGKLTILVLV AAVLLSTQVM VQGDADQPAD RDAVPRDDNP SGTDGKFMNV LRRFGCPWQP
     WCG