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COW_CONVR
ID   COW_CONVR               Reviewed;          63 AA.
AC   F5C3T9;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Contryphan-Vi {ECO:0000305};
DE   AltName: Full=Contryphan-R-like {ECO:0000312|EMBL:ADZ74135.1, ECO:0000312|EMBL:ADZ99322.1};
DE   Flags: Precursor;
OS   Conus virgo (Virgin cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virgiconus.
OX   NCBI_TaxID=89427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=22781954; DOI=10.1016/j.toxicon.2012.06.011;
RA   Liu Z., Li H., Liu N., Wu C., Jiang J., Yue J., Jing Y., Dai Q.;
RT   "Diversity and evolution of conotoxins in Conus virgo, Conus eburneus,
RT   Conus imperialis and Conus marmoreus from the South China Sea.";
RL   Toxicon 60:982-989(2012).
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:0000305|PubMed:22781954}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22781954}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
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:0000250|UniProtKB:P58787}.
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   EMBL; JF322906; ADZ74135.1; -; mRNA.
DR   EMBL; JF460782; ADZ99322.1; -; mRNA.
DR   AlphaFoldDB; F5C3T9; -.
DR   ConoServer; 4516; Contryphan-Vi 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   3: Inferred from homology;
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"
FT                   /id="PRO_0000445124"
FT   PEPTIDE         55..62
FT                   /note="Contryphan-Vi"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5007656944"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   MOD_RES         58
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   DISULFID        56..62
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
SQ   SEQUENCE   63 AA;  6806 MW;  5FB4D2CDB60D15B6 CRC64;
     MGKLTILVLV AAVLLSTQVM VQGDGDQPAD RNAVRRDDNP GGLSGKFMNV LRRSGCPWHP
     WCG
 
 
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