O16E_CONST
ID O16E_CONST Reviewed; 82 AA.
AC Q9XZK5; Q5K0D4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Delta-conotoxin SVIE;
DE Short=Delta-SVIE;
DE AltName: Full=Omega-conotoxin SO-6;
DE Short=Omega-conotoxin SO6;
DE AltName: Full=Omega-conotoxin-4;
DE Flags: Precursor;
GN Name=SO6;
OS Conus striatus (Striated cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX NCBI_TaxID=6493;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=10573284; DOI=10.1016/s0196-9781(99)00116-3;
RA Lu B.-S., Yu F., Zhao D., Huang P.-T., Huang C.-F.;
RT "Conopeptides from Conus striatus and Conus textile by cDNA cloning.";
RL Peptides 20:1139-1144(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-82, PROTEIN SEQUENCE OF 52-82, FUNCTION,
RP HYDROXYLATION AT PRO-65, MASS SPECTROMETRY, AND SYNTHESIS OF 52-82.
RC TISSUE=Venom, and Venom duct;
RX PubMed=11683628; DOI=10.1021/bi010683a;
RA Bulaj G., DeLaCruz R., Azimi-Zonooz A., West P., Watkins M., Yoshikami D.,
RA Olivera B.M.;
RT "Delta-conotoxin structure/function through a cladistic analysis.";
RL Biochemistry 40:13201-13208(2001).
RN [4]
RP INTERACTION WITH SODIUM CHANNELS.
RX PubMed=15990094; DOI=10.1016/j.febslet.2005.05.077;
RA Leipold E., Hansel A., Olivera B.M., Terlau H., Heinemann S.H.;
RT "Molecular interaction of delta-conotoxins with voltage-gated sodium
RT channels.";
RL FEBS Lett. 579:3881-3884(2005).
CC -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC channels (Nav) and inhibit the inactivation process (By similarity).
CC However, this toxin interacts with a conserved hydrophobic triad (YFV)
CC in the domain-4 voltage sensor of sodium channels. {ECO:0000250,
CC ECO:0000269|PubMed:11683628}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC -!- MASS SPECTROMETRY: Mass=3320; Method=Electrospray; Note=Sequence
CC shown.; Evidence={ECO:0000269|PubMed:11683628};
CC -!- MASS SPECTROMETRY: Mass=3343; Method=Electrospray; Note=Variant Glu-
CC 52.; Evidence={ECO:0000269|PubMed:11683628};
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF146351; AAD31911.1; -; mRNA.
DR EMBL; AJ851174; CAH64847.1; -; mRNA.
DR AlphaFoldDB; Q9XZK5; -.
DR ConoServer; 867; SVIE precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR InterPro; IPR012322; Conotoxin_d-typ_CS.
DR InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60005; DELTA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydroxylation; Ion channel impairing toxin; Knottin;
KW Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..51
FT /evidence="ECO:0000269|PubMed:11683628"
FT /id="PRO_0000034938"
FT PEPTIDE 52..82
FT /note="Delta-conotoxin SVIE"
FT /id="PRO_0000034939"
FT MOD_RES 65
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11683628"
FT DISULFID 54..69
FT /evidence="ECO:0000250"
FT DISULFID 61..73
FT /evidence="ECO:0000250"
FT DISULFID 68..77
FT /evidence="ECO:0000250"
FT VARIANT 52
FT /note="D -> E (minor)"
FT CONFLICT 6
FT /note="V -> M (in Ref. 2; CAH64847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 82 AA; 9217 MW; F88996FC3C54C05D CRC64;
MKLTCVMIVA VLFLTTWTFV TADDSRYGLK NLFPKARHEM KNPEASKLNK RDGCSSGGTF
CGIHPGLCCS EFCFLWCITF ID
