O16B_CONST
ID O16B_CONST Reviewed; 72 AA.
AC P28881; Q9UB25;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Omega-conotoxin SVIB {ECO:0000303|PubMed:1390774};
DE AltName: Full=SNX-183 {ECO:0000303|PubMed:1390774};
DE Flags: Precursor;
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 PROTEIN SEQUENCE OF 46-71, SYNTHESIS OF 46-71, FUNCTION, AMIDATION AT
RP CYS-71, SUBCELLULAR LOCATION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=1390774; DOI=10.1021/bi00156a009;
RA Ramilo C., Zafaralla G.C., Nadasdi L., Hammerland L.G., Yoshikami D.,
RA Gray W.R., Kristipati R., Ramachandran J., Miljanich G.P., Olivera B.M.,
RA Cruz L.J.;
RT "Novel alpha- and omega-conotoxins from Conus striatus venom.";
RL Biochemistry 31:9919-9926(1992).
RN [3]
RP STRUCTURE BY NMR OF 46-71, AND DISULFIDE BOND.
RX PubMed=8913308; DOI=10.1006/jmbi.1996.0576;
RA Nielsen K.J., Thomas L., Lewis R.J., Alewood P.F., Craik D.J.;
RT "A consensus structure for omega-conotoxins with different selectivities
RT for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB
RT and SNX-202.";
RL J. Mol. Biol. 263:297-310(1996).
CC -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC block voltage-gated calcium channels (Cav). This toxin blocks N-,
CC P- and Q-type calcium channels. {ECO:0000269|PubMed:1390774}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1390774}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:1390774}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000269|PubMed:8913308}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- TOXIC DOSE: On fish, this toxin causes paralysis and death on
CC intramuscular injection at doses of approximately 20 pmol/g. On
CC intracranial injection into mice, it causes respiratory distress at
CC around 70 pmol/g mouse and is lethal at around 300 pmol/g mouse.
CC {ECO:0000269|PubMed:1390774}.
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; AF146346; AAD31906.1; -; mRNA.
DR PIR; C44379; C44379.
DR PDB; 1MVJ; NMR; -; A=46-71.
DR PDBsum; 1MVJ; -.
DR AlphaFoldDB; P28881; -.
DR SMR; P28881; -.
DR ConoServer; 862; SVIB precursor.
DR EvolutionaryTrace; P28881; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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; IPR012321; Conotoxin_omega-typ_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Calcium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Knottin; Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..45
FT /evidence="ECO:0000305"
FT /id="PRO_0000034926"
FT PEPTIDE 46..71
FT /note="Omega-conotoxin SVIB"
FT /evidence="ECO:0000269|PubMed:1390774"
FT /id="PRO_0000034927"
FT MOD_RES 71
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:1390774"
FT DISULFID 46..61
FT /evidence="ECO:0000269|PubMed:8913308,
FT ECO:0000312|PDB:1MVJ"
FT DISULFID 53..65
FT /evidence="ECO:0000269|PubMed:8913308,
FT ECO:0000312|PDB:1MVJ"
FT DISULFID 60..71
FT /evidence="ECO:0000269|PubMed:8913308,
FT ECO:0000312|PDB:1MVJ"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1MVJ"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1MVJ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1MVJ"
SQ SEQUENCE 72 AA; 7741 MW; 1F753546AAD39908 CRC64;
MKLTCVVIVA VLLLTACQLI TADDSRGTQK HRALRSDTKL PMSTRCKLKG QSCRKTSYDC
CSGSCGRSGK CG