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Mu-conotoxin GVIIJ (Conotoxin muO-GVIIJ) (G086) (G19) (MuO'section sign'-GVIIJ)

 O17J_CONGE              Reviewed;          82 AA.
X5IWS1;
15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
15-FEB-2017, sequence version 2.
10-OCT-2018, entry version 20.
RecName: Full=Mu-conotoxin GVIIJ {ECO:0000303|PubMed:26817840};
AltName: Full=Conotoxin muO-GVIIJ {ECO:0000303|PubMed:26817840};
AltName: Full=MuO'section sign'-GVIIJ {ECO:0000303|PubMed:26817840};
Flags: Precursor;
Conus geographus (Geography cone) (Nubecula geographus).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
NCBI_TaxID=6491;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-75, PROTEIN SEQUENCE OF 48-59 AND
65-74, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
TISSUE=Venom, and Venom duct;
PubMed=24662800; DOI=10.1038/ncomms4521;
Dutertre S., Jin A.-H., Vetter I., Hamilton B., Sunagar K.,
Lavergne V., Dutertre V., Fry B.G., Antunes A., Venter D.J.,
Alewood P.F., Lewis R.J.;
"Evolution of separate predation- and defence-evoked venoms in
carnivorous cone snails.";
Nat. Commun. 5:3521-3521(2014).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-82, FUNCTION,
SYNTHESIS OF 48-82, DISULFIDE BOND, BROMINATION AT TRP-49,
HYDROXYLATION AT PRO-53, S-CYSTEINYLATION AT CYS-71, AND MASS
SPECTROMETRY.
TISSUE=Venom, and Venom duct;
PubMed=24497506; DOI=10.1073/pnas.1324189111;
Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
"A disulfide tether stabilizes the block of sodium channels by the
conotoxin muO[section sign]-GVIIJ.";
Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
[3]
SYNTHESIS OF 48-82 (WITHOUT BROMINATION).
PubMed=26039939; DOI=10.1021/acs.biochem.5b00390;
Zhang M.M., Gajewiak J., Azam L., Bulaj G., Olivera B.M.,
Yoshikami D.;
"Probing the redox states of sodium channel cysteines at the binding
site of muO[section sign]-conotoxin GVIIJ.";
Biochemistry 54:3911-3920(2015).
[4]
FUNCTION, AND SYNTHESIS OF 48-82.
PubMed=25632083; DOI=10.1152/jn.01004.2014;
Wilson M.J., Zhang M.M., Gajewiak J., Azam L., Rivier J.E.,
Olivera B.M., Yoshikami D.;
"Alpha- and beta-subunit composition of voltage-gated sodium channels
investigated with mu-conotoxins and the recently discovered
muO'section sign'-conotoxin GVIIJ.";
J. Neurophysiol. 113:2289-2301(2015).
[5]
STRUCTURE BY NMR OF 48-82 OF MUTANT CYS-71, SYNTHESIS OF 48-82
(WITHOUT BROMINATION), FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF
TRP-49; TRP-49; ASP-52; PRO-53; THR-56; LYS-59; LEU-60; ARG-61;
LEU-62; TYR-63; SER-66; PHE-68; ASP-70; TYR-72; THR-73; LYS-74;
THR-75; LYS-77; ASP-78 AND LYS-79.
PubMed=26817840; DOI=10.1074/jbc.M115.697672;
Green B.R., Gajewiak J., Chhabra S., Skalicky J.J., Zhang M.,
Rivier J.E., Bulaj G., Olivera B.M., Yoshikami D., Norton R.S.;
"Structural basis for the inhibition of voltage-gated sodium channels
by conotoxin muO-GVIIJ.";
J. Biol. Chem. 291:7205-7220(2016).
-!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav).
This toxin (GVIIJ(SSG)) blocks Nav1.1/SCN1A (Kd=11 nM),
Nav1.2/SCN2A (Kd=11 nM), Nav1.3/SCN3A (Kd=15 nM), Nav1.4/SCN4A
(Kd=4.7 nM), Nav1.6/SCN8A (Kd=360 nM) and Nav1.7/SCN9A (Kd=41 nM)
(PubMed:24497506, PubMed:26039939). It binds the channel at the
newly described site 8, which is composed by two surfaces whose
one contains a non-disulfide-bonded cysteine (which is free to
covalently bind the toxin Cys-71) (PubMed:24497506). It is
noteworthy that coexpression of subunits beta-2 or beta-4 (but not
beta-1 or beta-3) protects rNav1.1-1.7 against block by the toxin,
since these subunits (thanks to their extracellular domain)
covalently bind to the key cysteine of the channel, thus
preventing the covalent binding of the toxin (PubMed:24497506,
PubMed:25632083). {ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:25632083, ECO:0000269|PubMed:26039939,
ECO:0000269|PubMed:26817840}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24662800}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000305|PubMed:24662800}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin.
{ECO:0000269|PubMed:26817840}.
-!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
{ECO:0000305}.
-!- PTM: Cys-71 is a key residue that tethers to the channel by
covalent attachment, leading to nearly irreversible inhibition
(k(off) very low) (PubMed:24497506, PubMed:26817840). In order to
determine the solution structure without dimerization, this
residue was mutated to Cys. {ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
-!- MASS SPECTROMETRY: Mass=3934.49; Method=MALDI; Range=48-82;
Evidence={ECO:0000269|PubMed:24497506};
-!- MISCELLANEOUS: This toxin shows a very low affinity to
Nav1.5/SCN5A (Kd=207 uM) and does not show activity on
rNav1.8/SCN10A. {ECO:0000269|PubMed:24497506}.
-!- SIMILARITY: Belongs to the conotoxin O1 superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAO65619.1; Type=Erroneous termination; Positions=76; Note=Translated as Cys.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=synthetic GVIIJ[C71S];
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26674";
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=synthetic GVIIJ disulfide-linked with cysteamine;
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26675";
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EMBL; AB910851; BAO65619.1; ALT_SEQ; mRNA.
PDB; 2N8H; NMR; -; A=48-82.
PDBsum; 2N8H; -.
SMR; X5IWS1; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR004214; Conotoxin.
Pfam; PF02950; Conotoxin; 1.
1: Evidence at protein level;
3D-structure; Bromination; Direct protein sequencing; Disulfide bond;
Hydroxylation; Ion channel impairing toxin; Knottin; Secreted; Signal;
Toxin; Voltage-gated sodium channel impairing toxin.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 47 {ECO:0000269|PubMed:24497506}.
/FTId=PRO_0000438880.
CHAIN 48 82 Mu-conotoxin GVIIJ.
{ECO:0000269|PubMed:24497506}.
/FTId=PRO_5004957961.
SITE 59 59 Functionally important residue, that
binds to the site 8 of the channel.
{ECO:0000305|PubMed:26817840}.
SITE 61 61 Functionally important residue, that
binds to the site 8 of the channel.
{ECO:0000305|PubMed:26817840}.
SITE 63 63 Functionally important residue, that
binds to the site 8 of the channel.
{ECO:0000305|PubMed:26817840}.
SITE 71 71 Functionally important residue, that
binds to the site 8 of the channel
(distinct surface that K-59; R-61 and Y-
63). {ECO:0000305|PubMed:26817840}.
MOD_RES 49 49 6'-bromotryptophan.
{ECO:0000269|PubMed:24497506}.
MOD_RES 53 53 4-hydroxyproline.
{ECO:0000269|PubMed:24497506}.
MOD_RES 71 71 S-cysteinyl cysteine.
{ECO:0000269|PubMed:24497506}.
DISULFID 50 65 {ECO:0000244|PDB:2N8H,
ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
DISULFID 57 69 {ECO:0000244|PDB:2N8H,
ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
DISULFID 64 76 {ECO:0000244|PDB:2N8H,
ECO:0000269|PubMed:24497506,
ECO:0000269|PubMed:26817840}.
MUTAGEN 49 49 W->A: 10-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 52 52 D->K: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 53 53 P->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 56 56 T->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 59 59 K->D: 280-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 60 60 L->A: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 61 61 R->D: 133-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 62 62 L->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 63 63 Y->A: 53-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 66 66 S->A: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 68 68 F->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 70 70 D->N: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 72 72 Y->A,D,R: No change or small decrease in
affinity to Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 73 73 T->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 74 74 K->D: 13-fold decrease of affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 74 74 K->G,F: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 75 75 T->A: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 77 77 K->A: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 78 78 D->K: No change in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
MUTAGEN 79 79 K->D: Small decrease in affinity to
Nav1.2/SCNA2.
{ECO:0000269|PubMed:26817840}.
STRAND 58 61 {ECO:0000244|PDB:2N8H}.
STRAND 64 67 {ECO:0000244|PDB:2N8H}.
TURN 71 74 {ECO:0000244|PDB:2N8H}.
SEQUENCE 82 AA; 8871 MW; D8A907002C69A971 CRC64;
MKLTCVVIVA ALLLTACQLI TALDCGGTQK HRALRSTIKL SLLRQHRGWC GDPGATCGKL
RLYCCSGFCD CYTKTCKDKS SA


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Related Genes :
[] Mu-conotoxin GVIIJ (Conotoxin muO-GVIIJ) (MuO'section sign'-GVIIJ)
[Scn2a Scn2a1] Sodium channel protein type 2 subunit alpha (Sodium channel protein brain II subunit alpha) (Sodium channel protein type II subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.2)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Scn4a] Sodium channel protein type 4 subunit alpha (Mu-1) (SkM1) (Sodium channel protein skeletal muscle subunit alpha) (Sodium channel protein type IV subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.4)
[Scn5a] Sodium channel protein type 5 subunit alpha (Sodium channel protein cardiac muscle subunit alpha) (Sodium channel protein type V subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.5)
[SCN2A NAC2 SCN2A1 SCN2A2] Sodium channel protein type 2 subunit alpha (HBSC II) (Sodium channel protein brain II subunit alpha) (Sodium channel protein type II subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.2)
[SCN8A MED] Sodium channel protein type 8 subunit alpha (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6)
[SCN4A] Sodium channel protein type 4 subunit alpha (SkM1) (Sodium channel protein skeletal muscle subunit alpha) (Sodium channel protein type IV subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.4)
[SCN1A NAC1 SCN1] Sodium channel protein type 1 subunit alpha (Sodium channel protein brain I subunit alpha) (Sodium channel protein type I subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.1)
[SCN9A NENA] Sodium channel protein type 9 subunit alpha (Neuroendocrine sodium channel) (hNE-Na) (Peripheral sodium channel 1) (PN1) (Sodium channel protein type IX subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.7)
[SCN3A KIAA1356 NAC3] Sodium channel protein type 3 subunit alpha (Sodium channel protein brain III subunit alpha) (Sodium channel protein type III subunit alpha) (Voltage-gated sodium channel subtype III) (Voltage-gated sodium channel subunit alpha Nav1.3)
[Scn1a] Sodium channel protein type 1 subunit alpha (Sodium channel protein brain I subunit alpha) (Sodium channel protein type I subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.1)
[Scn8a] Sodium channel protein type 8 subunit alpha (Peripheral nerve protein type 4) (PN4) (Sodium channel 6) (NaCh6) (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6)
[Scn9a] Sodium channel protein type 9 subunit alpha (Peripheral sodium channel 1) (PN1) (Sodium channel protein type IX subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.7)
[Scn3a] Sodium channel protein type 3 subunit alpha (Sodium channel protein brain III subunit alpha) (Sodium channel protein type III subunit alpha) (Voltage-gated sodium channel subtype III) (Voltage-gated sodium channel subunit alpha Nav1.3)
[] Mu-conotoxin BuIIIB (Conotoxin Bu16)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ribBA CND83_02575] Riboflavin biosynthesis protein RibBA [Includes: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA2 chain; Hemagglutinin HA1 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA2 chain; Hemagglutinin HA1 chain]
[PRKCSH G19P1] Glucosidase 2 subunit beta (80K-H protein) (Glucosidase II subunit beta) (Protein kinase C substrate 60.1 kDa protein heavy chain) (PKCSH)

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