Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Alpha-conotoxin GID

 CA1D_CONGE              Reviewed;          66 AA.
P60274; X5IH33;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 2.
22-NOV-2017, entry version 61.
RecName: Full=Alpha-conotoxin GID {ECO:0000303|PubMed:12419800};
Flags: Precursor;
Conus geographus (Geography cone) (Nubecula geographus).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=6491;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=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]
PROTEIN SEQUENCE OF 45-63, FUNCTION, HYDROXYLATION AT PRO-60,
GAMMA-CARBOXYGLUTAMATION AT GLU-48, STRUCTURE BY NMR OF 45-63,
DISULFIDE BONDS, SYNTHESIS, MASS SPECTROMETRY, MUTAGENESIS OF ARG-56
AND 1-ILE--GLU-4, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=12419800; DOI=10.1074/jbc.M210280200;
Nicke A., Loughnan M.L., Millard E.L., Alewood P.F., Adams D.J.,
Daly N.L., Craik D.J., Lewis R.J.;
"Isolation, structure, and activity of GID, a novel alpha 4/7-
conotoxin with an extended N-terminal sequence.";
J. Biol. Chem. 278:3137-3144(2003).
[3]
FUNCTION ON ALPHA-3-BETA-2 AND ALPHA-4-BETA-2 NACHR.
PubMed=15929983; DOI=10.1074/jbc.M504229200;
Dutertre S., Nicke A., Lewis R.J.;
"Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the
nicotinic acetylcholine receptor.";
J. Biol. Chem. 280:30460-30468(2005).
[4]
FUNCTION, MUTAGENESIS OF 45-ILE--ASP-47; 45-ILE-ARG-46; ILE-45;
ARG-46; ASP-47; GLU-48; SER-51; ASN-52; PRO-53; ARG-56; VAL-57;
ASN-58; ASN-59; PRO-60; HIS-61 AND VAL-62, AND STRUCTURE BY NMR OF
[45-ILE--GLU-48 DEL]GID AND [ARG-56]GID MUTANTS.
PubMed=19098004; DOI=10.1074/jbc.M804950200;
Millard E.L., Nevin S.T., Loughnan M.L., Nicke A., Clark R.J.,
Alewood P.F., Lewis R.J., Adams D.J., Craik D.J., Daly N.L.;
"Inhibition of neuronal nicotinic acetylcholine receptor subtypes by
alpha-Conotoxin GID and analogues.";
J. Biol. Chem. 284:4944-4951(2009).
-!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
bind to the nicotinic acetylcholine receptors (nAChR) and thus
inhibit them. This toxin reversibly blocks alpha-3-beta-2
(IC(50)=3.1-5.1 nM), alpha-7 (IC(50)=4.5-5.1 nM), and alpha-4-
beta-2 (IC(50)=128.6-390 nM) nAChRs. {ECO:0000269|PubMed:12419800,
ECO:0000269|PubMed:15929983, ECO:0000269|PubMed:19098004}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12419800}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
{ECO:0000305}.
-!- PTM: Gamma-carboxyglutamation of Glu-48 seems to be not important
for nAChR inhibition. Synthetic peptides without this modification
do not show change in inhibition of alpha-7 and alpha-3-beta-2
nAChR and show a 2.3-fold increase in inhbition of alpha-4-beta-2
nAChR. {ECO:0000269|PubMed:19098004}.
-!- PTM: Hydroxylation of Pro-60 seems to be important for nAChR
inhibition. Synthetic peptides without this modification show a
small decrease in inhibition of alpha-7 and alpha-3-beta-2 nAChR
and a very important decrease in inhibition of alpha-4-beta-2
nAChR. {ECO:0000269|PubMed:19098004}.
-!- PTM: An amidation of Cys-63 increases potency against alpha-7
(2.6-fold) and alpha-3-beta-2 (2-fold) nAChR. On the other, the
peptide has no more activity on alpha-4-beta-2 nAChR with an
amidated C-63. {ECO:0000269|PubMed:19098004}.
-!- MASS SPECTROMETRY: Mass=2184.9; Method=Unknown; Range=1-63;
Evidence={ECO:0000269|PubMed:12419800};
-!- MISCELLANEOUS: This toxin does not inhibit neuronal alpha-3-beta-4
and alpha-4-beta-4 nAChR, and muscle alpha-1-beta-1-gamma-delta
nAChR. {ECO:0000269|PubMed:12419800, ECO:0000269|PubMed:15929983}.
-!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB910812; BAO65580.1; -; mRNA.
EMBL; AB910893; BAO65661.1; -; mRNA.
PDB; 1MTQ; NMR; -; A=45-63.
PDB; 5UG3; NMR; -; A=45-63.
PDB; 5UG5; NMR; -; A=45-63.
PDBsum; 1MTQ; -.
PDBsum; 5UG3; -.
PDBsum; 5UG5; -.
SMR; P60274; -.
ConoServer; 98; GID.
EvolutionaryTrace; P60274; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR009958; Conotoxin_a-typ.
InterPro; IPR018072; Conotoxin_a-typ_CS.
Pfam; PF07365; Toxin_8; 1.
PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
1: Evidence at protein level;
3D-structure; Acetylcholine receptor inhibiting toxin;
Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
Hydroxylation; Ion channel impairing toxin; Neurotoxin;
Postsynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 44 {ECO:0000269|PubMed:12419800}.
/FTId=PRO_0000439929.
PEPTIDE 45 63 Alpha-conotoxin GID.
{ECO:0000269|PubMed:12419800}.
/FTId=PRO_0000044459.
REGION 45 47 N-terminal tail important for activity on
alpha-4-beta-2 nAChR.
{ECO:0000269|PubMed:12419800,
ECO:0000269|PubMed:19098004}.
SITE 47 47 Key residue for activity on alpha-7,
alpha-3-beta-2 and alpha-4-beta-2 nAChR.
{ECO:0000269|PubMed:19098004}.
SITE 53 53 Key residue for activity on alpha-7,
alpha-3-beta-2 and alpha-4-beta-2 nAChR.
{ECO:0000269|PubMed:19098004}.
SITE 56 56 Key residue for activity on alpha-7 and
alpha-4-beta-2 nAChR.
{ECO:0000269|PubMed:12419800,
ECO:0000269|PubMed:19098004}.
SITE 58 58 Key residue for activity on alpha-7 and
alpha-4-beta-2 nAChR.
{ECO:0000269|PubMed:19098004}.
MOD_RES 48 48 4-carboxyglutamate.
{ECO:0000269|PubMed:12419800}.
MOD_RES 60 60 4-hydroxyproline.
{ECO:0000269|PubMed:12419800}.
DISULFID 49 55 {ECO:0000269|PubMed:12419800,
ECO:0000312|PDB:1MTQ}.
DISULFID 50 63 {ECO:0000269|PubMed:12419800,
ECO:0000312|PDB:1MTQ}.
MUTAGEN 45 48 Missing: No change or small decrease in
inhibition of alpha-3-beta-2 and alpha-7
nAChRs, 4.4-fold decrease in inhibition
of alpha-4-beta-2 nAChR.
{ECO:0000269|PubMed:12419800}.
MUTAGEN 45 47 IRD->A: 3.4-fold and 9.6-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 45 47 Missing: 19.7-fold and 22.9-fold decrease
in inhibition of alpha-7 and alpha-3-
beta-2 nAChR, respectively, and complete
loss of activity on alpha-4-beta-2 nAChR;
when associated with A-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 45 47 Missing: 2.5-fold and 18-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 45 46 IR->A: 2.8-fold and 5.8-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 45 46 Missing: 2.5-fold decrease in inhibition
of alpha-7 nAChR; when associated with
lack of gamma-carboxyglutamation at Glu-
48. {ECO:0000269|PubMed:19098004}.
MUTAGEN 45 45 I->A: No change in inhibition of alpha-7,
4.6-fold and 2-fold decrease in
inhibition of alpha-3-beta-2 and alpha-4-
beta-2 nAChR, respectively; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 46 46 R->A: 2.5-fold and 28.7-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 47 47 D->A: 8.3-fold and 20.5-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 48 48 E->A: No change in inhibition of alpha-7,
alpha-3-beta-2 nAChR and 2.5-fold
increase in inhibition of alpha-4-beta-2
nAChR. 19.7-fold and 22.9-fold decrease
in inhibition of alpha-7 and alpha-3-
beta-2 nAChR, respectively, and complete
loss of activity on alpha-4-beta-2 nAChR;
when associated with 45-I--D-47 DEL.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 51 51 S->A: 2.5-fold and 3.3-fold decrease in
inhibition of alpha-7 and alpha-4-beta-2
nAChR, and 1.4-fold increase in
inhibition of alpha-3-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 52 52 N->A: Important decrease in inhibition of
alpha-7 nAChR, no change in inhibition of
alpha-3-beta-2 nAChR and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 53 53 P->A: 17.7-fold and 50-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 56 56 R->A: 3.2-fold, 13.2-fold and 10.7-fold
decrease in inhibition of alpha3-beta-2,
alpha-4-beta-2 and alpha-7 nAChRs,
respectively.
{ECO:0000269|PubMed:12419800}.
MUTAGEN 56 56 R->A: 9.6-fold and 3.1-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 57 57 V->A: 2.2-fold decrease in inhibition of
alpha-7 nAChR, 5.7-fold increase in
inhibition of alpha-3-beta-2 nAChR, and
no change in activity on alpha-4-beta-2
nAChR; when associated with lack of
gamma-carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 58 58 N->A: 10.1-fold decrease in inhibition of
alpha-7 nAChR, 2.6-fold increase in
inhibition of alpha-3-beta-2 nAChR, and
complete loss of activity on alpha-4-
beta-2 nAChR; when associated with lack
of gamma-carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 59 59 N->A: No change in inhibition of alpha-7
and alpha-3-beta-2 nAChR and complete
loss of activity on alpha-4-beta-2 nAChR;
when associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 60 60 P->A: 2.5-fold and 4-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, respectively, and complete loss of
activity on alpha-4-beta-2 nAChR; when
associated with lack of gamma-
carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 61 61 H->A: No change in inhibition of alpha-7
and alpha-3-beta-2 nAChR, and 4.7-fold
decrease in inhibition of alpha-4-beta-2
nAChR; when associated with lack of
gamma-carboxyglutamation at Glu-48.
{ECO:0000269|PubMed:19098004}.
MUTAGEN 62 62 V->A: 1.5-fold and 12-fold decrease in
inhibition of alpha-7 and alpha-3-beta-2
nAChR, and complete loss of activity on
alpha-4-beta-2 nAChR; when associated
with lack of gamma-carboxyglutamation at
Glu-48. {ECO:0000269|PubMed:19098004}.
TURN 49 51 {ECO:0000244|PDB:1MTQ}.
HELIX 53 58 {ECO:0000244|PDB:1MTQ}.
STRAND 59 61 {ECO:0000244|PDB:5UG3}.
SEQUENCE 66 AA; 7428 MW; A366397F42F3A876 CRC64;
MGMRMMFTVF LLVVLAATIV SFTSDRASDG RNVAAKAFHR IGRTIRDECC SNPACRVNNP
HVCRRR


Related products :

Catalog number Product name Quantity
08CON015-00500 α-conotoxin GI (alpha conotoxin GI), α-conotoxin G blocks nAChR receptors 500 ug
08CON015-01000 α-conotoxin GI (alpha conotoxin GI), α-conotoxin G blocks nAChR receptors 1000 ug
08CON011-00500 α-conotoxin IMI (alpha conotoxin IMI), α-conotoxin IMI blocks nAChR 500 ug
08CON011-01000 α-conotoxin IMI (alpha conotoxin IMI), α-conotoxin IMI blocks nAChR 1000 ug
08CON012-00500 α-conotoxin MI (alpha conotoxin MI), α-conotoxin MI blocks nAChR 500 ug
08CON012-01000 α-conotoxin MI (alpha conotoxin MI), α-conotoxin MI blocks nAChR 1000 ug
orb71257 alpha Conotoxin EI peptide This is alpha Conotoxin EI peptide. For research use only. 1 mg
orb72044 alpha Conotoxin GI peptide This is alpha Conotoxin GI peptide. For research use only. 0.5 mg
orb71258 alpha Conotoxin GS peptide This is alpha Conotoxin GS peptide. For research use only. 1 mg
orb72045 alpha Conotoxin IMI peptide This is alpha Conotoxin IMI peptide. For research use only. 0.5 mg
orb71259 alpha Conotoxin MI peptide This is alpha Conotoxin MI peptide. For research use only. 1 mg
orb70283 alpha Conotoxin SI peptide This is alpha Conotoxin SI peptide. For research use only. 1 mg
orb71260 alpha Conotoxin SIA peptide This is alpha Conotoxin SIA peptide. For research use only. 1 mg
08CON001-00500 ω-Conotoxin MVIIA (omega conotoxin MVIIA), ω-Conotoxin MVIIA is a Cav2.2 channel blocker 500 ug
08CON001-00100 ω-Conotoxin MVIIA (omega conotoxin MVIIA), ω-Conotoxin MVIIA is a Cav2.2 channel blocker 100 ug
08CON003-00500 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 500 ug
08CON003-01000 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 1000 ug
08CON003-00100 ω-conotoxin GVIA, ω-conotoxin GVIA blocks Cav2.2 100 ug
08CON002-00500 ω-conotoxin MVIIC (omega contoxin MVIIC), ω-conotoxin MVIIC is a calcium channel blocker 500 ug
08CON002-00100 ω-conotoxin MVIIC (omega contoxin MVIIC), ω-conotoxin MVIIC is a calcium channel blocker 100 ug
08CON002-01000 ω-conotoxin MVIIC (omega contoxin MVIIC), ω-conotoxin MVIIC is a calcium channel blocker 1000 ug
08CON006-00500 μ-Conotoxin PIIIA, μ-Conotoxin PIIIA blocks Nav1.2 and Nav1.7 channels 500 ug
08CON006-00100 μ-Conotoxin PIIIA, μ-Conotoxin PIIIA blocks Nav1.2 and Nav1.7 channels 100 ug
ST14-500 Conotoxin mI 500 µg
ST14-1 Conotoxin mI 1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur