O161_CONVR
ID O161_CONVR Reviewed; 79 AA.
AC Q5K0C7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Conotoxin Vi6.1 {ECO:0000303|PubMed:26851775};
DE AltName: Full=Conotoxin vi6a {ECO:0000303|PubMed:26851775};
DE AltName: Full=virgo 1 {ECO:0000303|PubMed:15652641};
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=15652641; DOI=10.1016/j.peptides.2004.10.027;
RA Kauferstein S., Melaun C., Mebs D.;
RT "Direct cDNA cloning of novel conopeptide precursors of the O-
RT superfamily.";
RL Peptides 26:361-367(2005).
RN [2]
RP PROTEIN SEQUENCE OF 48-79, FUNCTION, BIOASSAY, SUBCELLULAR LOCATION,
RP SYNTHESIS OF 48-79, HYDROXYLATION AT PRO-60 AND PRO-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=26851775; DOI=10.1016/j.toxicon.2016.02.001;
RA Espino S.S., Dilanyan T., Imperial J.S., Aguilar M.B., Teichert R.W.,
RA Bandyopadhyay P., Olivera B.M.;
RT "Glycine-rich conotoxins from the Virgiconus clade.";
RL Toxicon 113:11-17(2016).
CC -!- FUNCTION: Ion channel inhibitor that inhibits the increase in
CC intracellular calcium upon depolarization in DRG neurons. In vivo, both
CC intraperitoneal and intracranial injections into mice induce
CC hyperactivity. {ECO:0000269|PubMed:26851775}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26851775}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:26851775}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=3114.15; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:26851775};
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; AJ851181; CAH64854.1; -; mRNA.
DR EMBL; AJ851182; CAH64855.1; -; mRNA.
DR AlphaFoldDB; Q5K0C7; -.
DR SMR; Q5K0C7; -.
DR ConoServer; 1070; Vi6.1 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 Pfam; PF02950; Conotoxin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..47
FT /evidence="ECO:0000305|PubMed:26851775"
FT /id="PRO_0000034997"
FT PEPTIDE 48..79
FT /note="Conotoxin Vi6.1"
FT /evidence="ECO:0000269|PubMed:26851775"
FT /id="PRO_0000034998"
FT MOD_RES 60
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:26851775"
FT MOD_RES 63
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:26851775"
FT DISULFID 49..62
FT /evidence="ECO:0000250|UniProtKB:P60179"
FT DISULFID 56..67
FT /evidence="ECO:0000250|UniProtKB:P60179"
FT DISULFID 61..77
FT /evidence="ECO:0000250|UniProtKB:P60179"
SQ SEQUENCE 79 AA; 8536 MW; 4C8947657E0E5C50 CRC64;
MKLTCVLIIT VLFLTASQLI TADYSRDQRQ YRAVRLGDEM RNFKGARDCG GQGEGCYTQP
CCPGLRCRGG GTGGGVCQL
