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