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Alpha-cobratoxin (Alpha-CbT) (alpha-CT) (alpha-Cbtx) (Alpha-elapitoxin-Nk2a) (Alpha-EPTX-Nk2a) (Long neurotoxin 1) (Siamensis 3)

 3L21_NAJKA              Reviewed;          71 AA.
P01391;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 113.
RecName: Full=Alpha-cobratoxin {ECO:0000303|PubMed:1317211, ECO:0000303|PubMed:1939183, ECO:0000303|PubMed:2086254, ECO:0000303|PubMed:2279844, ECO:0000303|PubMed:6553056, ECO:0000303|PubMed:6771288, ECO:0000303|PubMed:6930640};
Short=Alpha-CbT {ECO:0000303|PubMed:9840221};
Short=alpha-CT {ECO:0000303|PubMed:18381281, ECO:0000303|PubMed:22223648};
Short=alpha-Cbtx {ECO:0000303|PubMed:10574958, ECO:0000303|PubMed:10852927, ECO:0000303|PubMed:11867717, ECO:0000303|PubMed:12133834, ECO:0000303|PubMed:15791209, ECO:0000303|PubMed:9305882};
AltName: Full=Alpha-elapitoxin-Nk2a {ECO:0000305};
Short=Alpha-EPTX-Nk2a {ECO:0000305};
AltName: Full=Long neurotoxin 1;
AltName: Full=Siamensis 3 {ECO:0000303|Ref.1};
Naja kaouthia (Monocled cobra) (Naja siamensis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
NCBI_TaxID=8649;
[1]
PROTEIN SEQUENCE.
TISSUE=Venom;
Karlsson E.;
"Chemistry of some potent animal toxins.";
Experientia 29:1319-1327(1973).
[2]
PROTEIN SEQUENCE OF 1-17; 24-33 AND 36-68, IDENTIFICATION BY MASS
SPECTROMETRY, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=18381281; DOI=10.1074/jbc.M802085200;
Osipov A.V., Kasheverov I.E., Makarova Y.V., Starkov V.G.,
Vorontsova O.V., Ziganshin R.K., Andreeva T.V., Serebryakova M.V.,
Benoit A., Hogg R.C., Bertrand D., Tsetlin V.I., Utkin Y.N.;
"Naturally occurring disulfide-bound dimers of three-fingered toxins:
a paradigm for biological activity diversification.";
J. Biol. Chem. 283:14571-14580(2008).
[3]
FUNCTION.
PubMed=6771288;
Kang S., Maelicke A.;
"Fluorescein isothiocyanate-labeled alpha-cobratoxin. Biochemical
characterization and interaction with acetylcholine receptor from
Electrophorus electricus.";
J. Biol. Chem. 255:7326-7332(1980).
[4]
FUNCTION.
PubMed=6553056;
Martin B.M., Chibber B.A., Maelicke A.;
"The sites of neurotoxicity in alpha-cobratoxin.";
J. Biol. Chem. 258:8714-8722(1983).
[5]
FUNCTION.
PubMed=2086254; DOI=10.1016/0014-2999(90)94190-9;
Alkondon M., Albuquerque E.X.;
"Alpha-cobratoxin blocks the nicotinic acetylcholine receptor in rat
hippocampal neurons.";
Eur. J. Pharmacol. 191:505-506(1990).
[6]
FUNCTION.
PubMed=9053737; DOI=10.1007/BF00171324;
Apel C., Ricny J., Wagner G., Wessler I.;
"Alpha-bungarotoxin, kappa-bungarotoxin, alpha-cobratoxin and
erabutoxin-b do not affect [3H]acetylcholine release from the rat
isolated left hemidiaphragm.";
Naunyn Schmiedebergs Arch. Pharmacol. 352:646-652(1995).
[7]
FUNCTION.
PubMed=9305882; DOI=10.1074/jbc.272.39.24279;
Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P.,
Bertrand D., Menez A.;
"Only snake curaremimetic toxins with a fifth disulfide bond have high
affinity for the neuronal alpha7 nicotinic receptor.";
J. Biol. Chem. 272:24279-24286(1997).
[8]
FUNCTION.
PubMed=9840221; DOI=10.1016/S0197-0186(98)00033-3;
Dajas-Bailador F., Costa G., Dajas F., Emmett S.;
"Effects of alpha-erabutoxin, alpha-bungarotoxin, alpha-cobratoxin and
fasciculin on the nicotine-evoked release of dopamine in the rat
striatum in vivo.";
Neurochem. Int. 33:307-312(1998).
[9]
FUNCTION, SYNTHESIS, MUTAGENESIS OF LYS-23; TRP-25; ASP-27; PHE-29;
ARG-33; ARG-36; LYS-49 AND PHE-65, AND SITES LYS-23; TRP-25; ASP-27;
PHE-29; ARG-33; ARG-36; LYS-49 AND PHE-65.
PubMed=10574958; DOI=10.1074/jbc.274.49.34851;
Antil S., Servent D., Menez A.;
"Variability among the sites by which curaremimetic toxins bind to
torpedo acetylcholine receptor, as revealed by identification of the
functional residues of alpha-cobratoxin.";
J. Biol. Chem. 274:34851-34858(1999).
[10]
MUTAGENESIS OF TRP-25; ASP-27; ALA-28; PHE-29; ARG-33; LYS-35; ARG-36
AND PHE-65, AND SITES TRP-25; ASP-27; ALA-28; PHE-29; ARG-33; LYS-35;
ARG-36 AND PHE-65.
PubMed=10852927; DOI=10.1074/jbc.M909746199;
Antil-Delbeke S., Gaillard C., Tamiya T., Corringer P.-J.,
Changeux J.-P., Servent D., Menez A.;
"Molecular determinants by which a long chain toxin from snake venom
interacts with the neuronal alpha 7-nicotinic acetylcholine
receptor.";
J. Biol. Chem. 275:29594-29601(2000).
[11]
3D-STRUCTURE MODELING.
PubMed=11867717; DOI=10.1073/pnas.042699899;
Fruchart-Gaillard C., Gilquin B., Antil-Delbeke S., Le Novere N.,
Tamiya T., Corringer P.-J., Changeux J.-P., Menez A., Servent D.;
"Experimentally based model of a complex between a snake toxin and the
alpha 7 nicotinic receptor.";
Proc. Natl. Acad. Sci. U.S.A. 99:3216-3221(2002).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=6930640; DOI=10.1073/pnas.77.5.2400;
Walkinshaw M.D., Saenger W., Maelicke A.;
"Three-dimensional structure of the 'long' neurotoxin from cobra
venom.";
Proc. Natl. Acad. Sci. U.S.A. 77:2400-2404(1980).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=1939183;
Betzel C., Lange G., Pal G.P., Wilson K.S., Maelicke A., Saenger W.;
"The refined crystal structure of alpha-cobratoxin from Naja naja
siamensis at 2.4-A resolution.";
J. Biol. Chem. 266:21530-21536(1991).
[14]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=2279844;
Laplante S.R., Mikou A., Robin M., Guittet E., Delsuc M.-A.,
Charpentier I., Lallemand J.-Y.;
"Rapid determination and NMR assignments of antiparallel sheets and
helices of a scorpion and a cobra toxin.";
Int. J. Pept. Protein Res. 36:227-230(1990).
[15]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=1317211; DOI=10.1021/bi00135a018;
le Goas R., Laplante S.R., Mikou A., Delsuc M.-A., Guittet E.,
Robin M., Charpentier I., Lallemand J.-Y.;
"Alpha-cobratoxin: proton NMR assignments and solution structure.";
Biochemistry 31:4867-4875(1992).
[16]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=12133834; DOI=10.1074/jbc.M205483200;
Zeng H., Hawrot E.;
"NMR-based binding screen and structural analysis of the complex
formed between alpha-cobratoxin and an 18-mer cognate peptide derived
from the alpha 1 subunit of the nicotinic acetylcholine receptor from
Torpedo californica.";
J. Biol. Chem. 277:37439-37445(2002).
[17]
X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=15791209; DOI=10.1038/sj.emboj.7600620;
Bourne Y., Talley T.T., Hansen S.B., Taylor P., Marchot P.;
"Crystal structure of a Cbtx-AChBP complex reveals essential
interactions between snake alpha-neurotoxins and nicotinic
receptors.";
EMBO J. 24:1512-1522(2005).
[18]
ERRATUM.
Bourne Y., Talley T.T., Hansen S.B., Taylor P., Marchot P.;
EMBO J. 25:266-266(2006).
[19]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER),
FUNCTION, AND SUBUNIT.
TISSUE=Venom;
PubMed=22223648; DOI=10.1074/jbc.M111.322313;
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G.,
Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.;
"Dimeric alpha-cobratoxin X-ray structure: localization of
intermolecular disulfides and possible mode of binding to nicotinic
acetylcholine receptors.";
J. Biol. Chem. 287:6725-6734(2012).
-!- FUNCTION: Monomer: binds with high affinity to muscular (alpha-1-
beta-1-gamma-delta (CHRNA1/CHRNB1/CHRNG/CHRND) nAChR) (IC(50)=4.5
nM on Torpedo californica membranes) and neuronal alpha-7/CHRNA7
nicotinic acetylcholine receptors (IC(50)=105 nM).
{ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:22223648}.
-!- FUNCTION: Homodimer: binds with high affinity (but lower than the
monomeric form) to muscular (IC(50)=9.7 nM) and with low affinity
to neuronal alpha-7/CHRNA7 nAChRs (IC(50)=1370 nM)
(PubMed:22223648). However, it acquires (compared to the monomeric
form) the capacity to block alpha-3/beta-2 (CHRNA3/CHRNB2) nAChRs
(PubMed:18381281). {ECO:0000269|PubMed:18381281,
ECO:0000269|PubMed:22223648}.
-!- FUNCTION: Heterodimer with cytotoxin 3 (AC P01446): is slightly
more active than the homodimer in inhibiting alpha-7 nAChR and is
considerably more active in blocking the alpha-3-beta-2 nAChR.
{ECO:0000269|PubMed:22223648}.
-!- SUBUNIT: Monomer, homo- or heterodimer with cytotoxins 1 (P60305),
2 (AC P01445), and 3 (AC P01446); disulfide-linked.
{ECO:0000269|PubMed:12133834, ECO:0000269|PubMed:1317211,
ECO:0000269|PubMed:15791209, ECO:0000269|PubMed:18381281,
ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:22223648,
ECO:0000269|PubMed:2279844, ECO:0000269|PubMed:6930640}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18381281}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- PTM: The disulfide bond Cys26-Cys30 is not necessary for toxin
activity, since reduction and alkylation of this bond does not
decrease the inhibitory activity against alpha-7 nAChR, but
surprisingly enhances the inhibitory activity against alpha-3-
beta-2. {ECO:0000269|PubMed:22223648}.
-!- MISCELLANEOUS: The monomeric form has no effect on alpha-3/beta-2
(CHRNA3/CHRNB2) nAChR (PubMed:18381281). It does not show any
blockade of the nicotine-evoked release of dopamine
(PubMed:9840221) and does not affect ACh release.
{ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:9840221}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-
chain subfamily. Type II alpha-neurotoxin sub-subfamily.
{ECO:0000305}.
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PIR; A01662; N2NJ1S.
PDB; 1CTX; X-ray; 2.80 A; A=1-71.
PDB; 1LXG; NMR; -; A=1-71.
PDB; 1LXH; NMR; -; A=1-71.
PDB; 1YI5; X-ray; 4.20 A; F/G/H/I/J=1-71.
PDB; 4AEA; X-ray; 1.94 A; A/B=1-71.
PDBsum; 1CTX; -.
PDBsum; 1LXG; -.
PDBsum; 1LXH; -.
PDBsum; 1YI5; -.
PDBsum; 4AEA; -.
ProteinModelPortal; P01391; -.
SMR; P01391; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P01391; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00206; snake_toxin; 1.
InterPro; IPR003571; Snake_3FTx.
InterPro; IPR018354; Snake_toxin_con_site.
InterPro; IPR035076; Toxin/TOLIP.
Pfam; PF00087; Toxin_TOLIP; 1.
PROSITE; PS00272; SNAKE_TOXIN; 1.
1: Evidence at protein level;
3D-structure; Acetylcholine receptor inhibiting toxin;
Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
Secreted; Toxin.
CHAIN 1 71 Alpha-cobratoxin. {ECO:0000269|Ref.1}.
/FTId=PRO_0000093554.
SITE 23 23 Binds to Torpedo AChR.
{ECO:0000269|PubMed:10574958}.
SITE 25 25 Binds to both neuronal alpha-7 and
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
SITE 27 27 Binds to both neuronal alpha-7 and
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
SITE 28 28 Binds to alpha-7 AChR.
{ECO:0000269|PubMed:10852927}.
SITE 29 29 Binds to both neuronal alpha-7 and
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
SITE 33 33 Binds to both neuronal alpha-7 and
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
SITE 35 35 Binds to alpha-7 AChR.
{ECO:0000269|PubMed:10852927}.
SITE 36 36 Binds to both neuronal alpha-7 and
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
SITE 49 49 Binds to Torpedo AChR.
{ECO:0000269|PubMed:10574958}.
SITE 65 65 Binds to both neuronal alpha-7 and
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
DISULFID 3 20 In monomer, partial.
{ECO:0000244|PDB:1CTX,
ECO:0000244|PDB:1LXG,
ECO:0000244|PDB:1LXH,
ECO:0000244|PDB:1YI5,
ECO:0000269|PubMed:12133834,
ECO:0000269|PubMed:1317211,
ECO:0000269|PubMed:15791209,
ECO:0000269|PubMed:1939183,
ECO:0000269|PubMed:2279844,
ECO:0000269|PubMed:6930640}.
DISULFID 3 3 Interchain (with C-20); in homodimer;
partial. {ECO:0000244|PDB:4AEA,
ECO:0000269|PubMed:22223648}.
DISULFID 14 41 {ECO:0000244|PDB:1CTX,
ECO:0000244|PDB:1LXG,
ECO:0000244|PDB:1LXH,
ECO:0000244|PDB:1YI5,
ECO:0000244|PDB:4AEA,
ECO:0000269|PubMed:12133834,
ECO:0000269|PubMed:1317211,
ECO:0000269|PubMed:15791209,
ECO:0000269|PubMed:1939183,
ECO:0000269|PubMed:22223648,
ECO:0000269|PubMed:2279844,
ECO:0000269|PubMed:6930640}.
DISULFID 20 20 Interchain (with C-3); in homodimer;
partial. {ECO:0000244|PDB:4AEA,
ECO:0000269|PubMed:22223648}.
DISULFID 26 30 {ECO:0000244|PDB:1CTX,
ECO:0000244|PDB:1LXG,
ECO:0000244|PDB:1LXH,
ECO:0000244|PDB:1YI5,
ECO:0000244|PDB:4AEA,
ECO:0000269|PubMed:12133834,
ECO:0000269|PubMed:1317211,
ECO:0000269|PubMed:15791209,
ECO:0000269|PubMed:1939183,
ECO:0000269|PubMed:22223648,
ECO:0000269|PubMed:2279844,
ECO:0000269|PubMed:6930640}.
DISULFID 45 56 {ECO:0000244|PDB:1CTX,
ECO:0000244|PDB:1LXG,
ECO:0000244|PDB:1LXH,
ECO:0000244|PDB:1YI5,
ECO:0000244|PDB:4AEA,
ECO:0000269|PubMed:12133834,
ECO:0000269|PubMed:1317211,
ECO:0000269|PubMed:15791209,
ECO:0000269|PubMed:1939183,
ECO:0000269|PubMed:22223648,
ECO:0000269|PubMed:2279844,
ECO:0000269|PubMed:6930640}.
DISULFID 57 62 {ECO:0000244|PDB:1CTX,
ECO:0000244|PDB:1LXG,
ECO:0000244|PDB:1LXH,
ECO:0000244|PDB:1YI5,
ECO:0000244|PDB:4AEA,
ECO:0000269|PubMed:12133834,
ECO:0000269|PubMed:1317211,
ECO:0000269|PubMed:15791209,
ECO:0000269|PubMed:1939183,
ECO:0000269|PubMed:22223648,
ECO:0000269|PubMed:2279844,
ECO:0000269|PubMed:6930640}.
MUTAGEN 23 23 K->E: 2-fold and 28-fold decrease in
affinity for Torpedo AChRs.
{ECO:0000269|PubMed:10574958}.
MUTAGEN 25 25 W->A: 11-fold decrease in affinity for
Torpedo AChRs and 6-fold decrease in
affinity for neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
MUTAGEN 27 27 D->R: 31-fold decrease in affinity for
Torpedo AChRs and 50-fold decrease in
affinity for neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
MUTAGEN 28 28 A->G: 5-fold decrease in affinity for
neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10852927}.
MUTAGEN 29 29 F->A: 12-fold decrease in affinity for
Torpedo AChRs and 74-fold decrease in
affinity for neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
MUTAGEN 33 33 R->E: 767-fold decrease in affinity for
Torpedo AChRs and 339-fold decrease in
affinity for neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
MUTAGEN 35 35 K->A: 11-fold decrease in affinity for
neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10852927}.
MUTAGEN 36 36 R->A: 16-fold decrease in affinity for
Torpedo AChRs.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
MUTAGEN 49 49 K->E: 3-fold and 53-fold decrease in
affinity for Torpedo AChRs.
{ECO:0000269|PubMed:10574958}.
MUTAGEN 65 65 F->A: 7-fold decrease in affinity for
Torpedo AChRs and 15-fold decrease in
affinity for neuronal alpha-7 AChR.
{ECO:0000269|PubMed:10574958,
ECO:0000269|PubMed:10852927}.
STRAND 6 10 {ECO:0000244|PDB:1CTX}.
STRAND 19 25 {ECO:0000244|PDB:4AEA}.
TURN 27 29 {ECO:0000244|PDB:1LXG}.
HELIX 30 33 {ECO:0000244|PDB:4AEA}.
STRAND 36 44 {ECO:0000244|PDB:4AEA}.
STRAND 52 57 {ECO:0000244|PDB:4AEA}.
STRAND 59 63 {ECO:0000244|PDB:1LXG}.
SEQUENCE 71 AA; 7831 MW; 6F07ADD885E9AC33 CRC64;
IRCFITPDIT SKDCPNGHVC YTKTWCDAFC SIRGKRVDLG CAATCPTVKT GVDIQCCSTD
NCNPFPTRKR P


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18-272-195931 HIF2 alpha - Rabbit polyclonal to HIF2 alpha; EPAS-1; Member of PAS protein 2; Basic-helix-loop-helix-PAS protein MOP2; Hypoxia-inducible factor 2 alpha; HIF-2 alpha; HIF2 alpha; HIF-1 alpha-like fact 0.2 ml
E0441r ELISA Anterior pituitary glycoprotein hormones common subunit alpha,Cga,Cga1,Follicle-stimulating hormone alpha chain,Follitropin alpha chain,FSH-alpha,Glycoprotein hormones alpha chain,LSH-alpha,Lute 96T
U0441r CLIA Anterior pituitary glycoprotein hormones common subunit alpha,Cga,Cga1,Follicle-stimulating hormone alpha chain,Follitropin alpha chain,FSH-alpha,Glycoprotein hormones alpha chain,LSH-alpha,Lutei 96T
E0441h ELISA Anterior pituitary glycoprotein hormones common subunit alpha,CGA,CG-alpha,Choriogonadotropin alpha chain,Chorionic gonadotrophin subunit alpha,Follicle-stimulating hormone alpha chain,Follitrop 96T
E0441h ELISA kit Anterior pituitary glycoprotein hormones common subunit alpha,CGA,CG-alpha,Choriogonadotropin alpha chain,Chorionic gonadotrophin subunit alpha,Follicle-stimulating hormone alpha chain,Foll 96T
U0441h CLIA Anterior pituitary glycoprotein hormones common subunit alpha,CGA,CG-alpha,Choriogonadotropin alpha chain,Chorionic gonadotrophin subunit alpha,Follicle-stimulating hormone alpha chain,Follitropi 96T
E0441Rb ELISA Anterior pituitary glycoprotein hormones common subunit alpha,CGA,Follicle-stimulating hormone alpha chain,Follitropin alpha chain,FSH-alpha,Glycoprotein hormones alpha chain,LSH-alpha,Luteinizi 96T
E0441p ELISA Anterior pituitary glycoprotein hormones common subunit alpha,CGA,Follicle-stimulating hormone alpha chain,Follitropin alpha chain,FSH-alpha,Glycoprotein hormones alpha chain,LSH-alpha,Luteinizi 96T


 

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