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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}.
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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
 
 
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