ID   COWA_CONCB              Reviewed;          46 AA.
AC   P0DP16;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Contryphan-C {ECO:0000305};
DE   AltName: Full=Ca-75;
DE   Flags: Precursor; Fragment;
OS   Conus caracteristicus (Characteristic cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=89440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=30917600; DOI=10.3390/md17030193;
RA   Yao G., Peng C., Zhu Y., Fan C., Jiang H., Chen J., Cao Y., Shi Q.;
RT   "High-throughput identification and analysis of novel conotoxins from three
RT   vermivorous cone snails by transcriptome sequencing.";
RL   Mar. Drugs 17:0-0(2019).
RN   [2]
RP   PROTEIN SEQUENCE OF 38-45, MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   HYDROXYLATION AT PRO-40, D-AMINO ACID AT TRP-41, AND AMIDATION AT CYS-45.
RC   TISSUE=Venom;
RX   PubMed=17902199; DOI=10.1002/rcm.3225;
RA   Thakur S.S., Balaram P.;
RT   "Rapid mass spectral identification of contryphans. Detection of
RT   characteristic peptide ions by fragmentation of intact disulfide-bonded
RT   peptides in crude venom.";
RL   Rapid Commun. Mass Spectrom. 21:3420-3426(2007).
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:17902199}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:17902199}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=990; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17902199};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       39-Cys-hydroxyPro-40. 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   AlphaFoldDB; P0DP16; -.
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.
PE   1: Evidence at protein level;
KW   Amidation; D-amino acid; Direct protein sequencing; Disulfide bond;
KW   Hydroxylation; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          <1..6
FT                   /evidence="ECO:0000305|PubMed:30917600"
FT   PROPEP          7..37
FT                   /evidence="ECO:0000305|PubMed:30917600"
FT                   /id="PRO_0000452026"
FT   PEPTIDE         38..45
FT                   /note="Contryphan-C"
FT                   /evidence="ECO:0000269|PubMed:17902199"
FT                   /id="PRO_0000439687"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         40
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17902199"
FT   MOD_RES         41
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000269|PubMed:17902199"
FT   MOD_RES         45
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:17902199"
FT   DISULFID        39..45
FT                   /evidence="ECO:0000269|PubMed:17902199"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   46 AA;  4943 MW;  116B64476B4EF4FA CRC64;
     QVMVQGDGDQ PAARNAVPKD DNPGGEAGKF MNVLRRSGCP WEPWCG