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Alpha-conotoxin ImI (Alpha-CTx ImI) (Fragment)

 CA1_CONIM               Reviewed;          17 AA.
P50983; Q8I6R4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
31-JAN-2018, entry version 98.
RecName: Full=Alpha-conotoxin ImI {ECO:0000303|PubMed:15609996, ECO:0000303|PubMed:8206995};
Short=Alpha-CTx ImI {ECO:0000303|PubMed:12384509};
Flags: Precursor; Fragment;
Conus imperialis (Imperial cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus; Stephanoconus.
NCBI_TaxID=35631;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SYNTHESIS OF 5-16, FUNCTION, AND
MUTAGENESIS OF PRO-10.
TISSUE=Venom duct;
PubMed=12384509; DOI=10.1074/jbc.M204565200;
Ellison M.A., McIntosh J.M., Olivera B.M.;
"Alpha-conotoxins ImI and ImII: similar alpha 7 nicotinic receptor
antagonists act at different sites.";
J. Biol. Chem. 278:757-764(2003).
[2]
PROTEIN SEQUENCE OF 5-16, FUNCTION, SYNTHESIS OF 5-16, DISULFIDE
BONDS, SUBCELLULAR LOCATION, AMIDATION AT CYS-16, AND MASS
SPECTROMETRY.
TISSUE=Venom;
PubMed=8206995;
McIntosh J.M., Yoshikami D., Mahe E., Nielsen D.B., Rivier J.E.,
Gray W.R., Olivera B.M.;
"A nicotinic acetylcholine receptor ligand of unique specificity,
alpha-conotoxin ImI.";
J. Biol. Chem. 269:16733-16739(1994).
[3]
FUNCTION, AND SYNTHESIS OF 5-16.
PubMed=7651351;
Johnson D.S., Martinez J., Elgoyhen A.B., Heinemann S.F.,
McIntosh J.M.;
"Alpha-conotoxin ImI exhibits subtype-specific nicotinic acetylcholine
receptor blockade: preferential inhibition of homomeric alpha 7 and
alpha 9 receptors.";
Mol. Pharmacol. 48:194-199(1995).
[4]
FUNCTION, SYNTHESIS OF 5-16, 3D-STRUCTURE MODELING, AND SUBUNIT.
PubMed=15609996; DOI=10.1021/bi048918g;
Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
"Alpha-conotoxins ImI and ImII target distinct regions of the human
alpha7 nicotinic acetylcholine receptor and distinguish human
nicotinic receptor subtypes.";
Biochemistry 43:16019-16026(2004).
[5]
SYNTHESIS OF 5-16, AND ROLE OF HYDROXYLATION.
PubMed=18189422; DOI=10.1021/bi701934m;
Lopez-Vera E., Walewska A., Skalicky J.J., Olivera B.M., Bulaj G.;
"Role of hydroxyprolines in the in vitro oxidative folding and
biological activity of conotoxins.";
Biochemistry 47:1741-1751(2008).
[6]
FUNCTION ON ALPHA-7 AND ALPHA-3-BETA-4, AND SYNTHESIS OF 5-16.
PubMed=19131337; DOI=10.1074/jbc.M806136200;
Armishaw C., Jensen A.A., Balle T., Clark R.J., Harpsoee K.,
Skonberg C., Liljefors T., Stroemgaard K.;
"Rational design of alpha-conotoxin analogues targeting alpha7
nicotinic acetylcholine receptors: improved antagonistic activity by
incorporation of proline derivatives.";
J. Biol. Chem. 284:9498-9512(2009).
[7]
DISULFIDE BONDS (RIBBON FORM), AND FOLDING.
TISSUE=Venom;
PubMed=22891240; DOI=10.1074/jbc.M112.366781;
Safavi-Hemami H., Gorasia D.G., Steiner A.M., Williamson N.A.,
Karas J.A., Gajewiak J., Olivera B.M., Bulaj G., Purcell A.W.;
"Modulation of conotoxin structure and function is achieved through a
multienzyme complex in the venom glands of cone snails.";
J. Biol. Chem. 287:34288-34303(2012).
[8]
STRUCTURE BY NMR OF 5-16, AND DISULFIDE BONDS.
PubMed=10194298; DOI=10.1021/bi9826254;
Rogers J.P., Luginbuehl P., Shen G.S., McCabe R.T., Stevens R.C.,
Wemmer D.E.;
"NMR solution structure of alpha-conotoxin ImI and comparison to other
conotoxins specific for neuronal nicotinic acetylcholine receptors.";
Biochemistry 38:3874-3882(1999).
[9]
STRUCTURE BY NMR OF 5-16, AND DISULFIDE BONDS.
PubMed=10350614; DOI=10.1016/S0167-4838(99)00065-5;
Gouda H., Hirono S.;
"Solution structure of alpha-conotoxin ImI determined by two-
dimensional NMR spectroscopy.";
Biochim. Biophys. Acta 1431:384-394(1999).
[10]
STRUCTURE BY NMR OF 5-16, AND DISULFIDE BONDS.
PubMed=10050774; DOI=10.1016/S0014-5793(99)00069-1;
Maslennikov I.V., Shenkarev Z.O., Zhmak M.N., Ivanov V.T.,
Methfessel C., Tsetlin V.I., Arseniev A.S.;
"NMR spatial structure of alpha-conotoxin ImI reveals a common
scaffold in snail and snake toxins recognizing neuronal nicotinic
acetylcholine receptors.";
FEBS Lett. 444:275-280(1999).
[11]
STRUCTURE BY NMR OF 5-16, AND DISULFIDE BONDS.
PubMed=10431825; DOI=10.1016/S0014-5793(99)00831-5;
Lamthanh H., Jegou-Matheron C., Servent D., Menez A., Lancelin J.-M.;
"Minimal conformation of the alpha-conotoxin ImI for the alpha7
neuronal nicotinic acetylcholine receptor recognition: correlated CD,
NMR and binding studies.";
FEBS Lett. 454:293-298(1999).
[12]
STRUCTURE BY NMR OF 5-16, AND DISULFIDE BONDS.
PubMed=10395477; DOI=10.1021/jm990114p;
Gehrmann J., Daly N.L., Alewood P.F., Craik D.J.;
"Solution structure of alpha-conotoxin ImI by 1H nuclear magnetic
resonance.";
J. Med. Chem. 42:2364-2372(1999).
[13]
MUTAGENESIS OF ASP-9; ARG-11 AND ARG-15, STRUCTURE BY NMR OF 5-16 OF
THESE THREE MUTANTS, AND DISULFIDE BONDS.
PubMed=11124036; DOI=10.1006/jmbi.2000.4247;
Rogers J.P., Luginbuhl P., Pemberton K., Harty P., Wemmer D.E.,
Stevens R.C.;
"Structure-activity relationships in a peptidic alpha7 nicotinic
acetylcholine receptor antagonist.";
J. Mol. Biol. 304:911-926(2000).
-!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
bind to the nicotinic acetylcholine receptors (nAChR) and thus
inhibit them. This toxin blocks neuronal alpha-3/beta-2 (human and
rat), alpha-7 (human and rat), and alpha-3/beta-4 (human) nAChRs
(PubMed:8206995, PubMed:15609996, PubMed:19131337). Acts voltage-
independently (PubMed:15609996). Competes with alpha-bungarotoxin
for binding to the receptor (PubMed:12384509, PubMed:15609996).
Binds to a different site than alpha-conotoxin ImII
(PubMed:15609996). Is highly active against the neuromuscular
receptor in frog (PubMed:8206995). {ECO:0000269|PubMed:12384509,
ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:19131337,
ECO:0000269|PubMed:8206995}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8206995}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
{ECO:0000305}.
-!- PTM: Not hydroxylated; hydroxylation improves its folding but
impairs its activity against target receptors.
{ECO:0000269|PubMed:18189422}.
-!- MASS SPECTROMETRY: Mass=1351.48; Method=Unknown; Range=5-16;
Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:8206995};
-!- MISCELLANEOUS: This toxin is a substrate for a multienzyme complex
that regulates its folding and assembly. This complex is composed
of protein-disulfide isomerase (PDI), peptidyl-prolyl cis-trans
isomerase (PPI) and immunoglobulin-binding protein (BiP). PDI
catalyzes the oxidation and reduction of disulfide bonds.
Oxidative folding rates are further increased in the presence of
PPI with the maximum effect observed in the presence of both
enzymes. In contrast, BiP is only observed to assist folding in
the presence of microsomes, suggesting that additional cofactors
are involved. This toxin has been observed in the venom as
globular (disulfide pattern C1-C3 and C2-C4) and ribbon form (C1-
C4 and C2-C3). {ECO:0000269|PubMed:22891240}.
-!- MISCELLANEOUS: Does not inhibit alpha-2-beta-2, alpha-4-beta-2,
alpha-2-beta-4, alpha-3-beta-4, and alpha-4-beta-4 subunits
(PubMed:7651351, PubMed:15609996). Has also no effect on muscle
nAChRs alpha-1-beta-1-delta-epsilon (PubMed:15609996).
{ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:7651351}.
-!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY159318; AAN78128.1; -; Genomic_DNA.
PIR; A53709; A53709.
PDB; 1CNL; NMR; -; A=5-16.
PDB; 1E74; NMR; -; A=5-14.
PDB; 1E75; NMR; -; A=5-16.
PDB; 1E76; NMR; -; A=5-16.
PDB; 1G2G; NMR; -; A=5-16.
PDB; 1IM1; NMR; -; A=5-16.
PDB; 1IMI; NMR; -; A=5-16.
PDB; 2BC7; NMR; -; A=5-16.
PDB; 2BC8; NMR; -; A=5-16.
PDB; 2BYP; X-ray; 2.07 A; F/G/H/I/J=5-16.
PDB; 2C9T; X-ray; 2.25 A; K/M/O/P/Q/R/S/T=5-16.
PDB; 2IGU; NMR; -; A=5-16.
PDB; 2MOA; NMR; -; A=5-16.
PDBsum; 1CNL; -.
PDBsum; 1E74; -.
PDBsum; 1E75; -.
PDBsum; 1E76; -.
PDBsum; 1G2G; -.
PDBsum; 1IM1; -.
PDBsum; 1IMI; -.
PDBsum; 2BC7; -.
PDBsum; 2BC8; -.
PDBsum; 2BYP; -.
PDBsum; 2C9T; -.
PDBsum; 2IGU; -.
PDBsum; 2MOA; -.
SMR; P50983; -.
DIP; DIP-61127N; -.
IntAct; P50983; 1.
ConoServer; 93; ImI precursor.
EvolutionaryTrace; P50983; -.
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.
InterPro; IPR018072; Conotoxin_a-typ_CS.
PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
1: Evidence at protein level;
3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; Ion channel impairing toxin; Neurotoxin;
Postsynaptic neurotoxin; Secreted; Toxin.
PROPEP <1 4 {ECO:0000269|PubMed:8206995}.
/FTId=PRO_0000273426.
PEPTIDE 5 16 Alpha-conotoxin ImI.
{ECO:0000269|PubMed:8206995}.
/FTId=PRO_0000034877.
SITE 9 9 Important for binding to human alpha-7
nAChR. {ECO:0000305|PubMed:15609996}.
SITE 10 10 Important for binding to human alpha-7
nAChR. {ECO:0000305|PubMed:15609996}.
SITE 11 11 Important for binding to human alpha-7
nAChR. {ECO:0000305|PubMed:15609996}.
SITE 13 13 Important for binding to human alpha-7
nAChR. {ECO:0000305|PubMed:15609996}.
SITE 14 14 Important for binding to human alpha-7
nAChR. {ECO:0000305|PubMed:15609996}.
MOD_RES 16 16 Cysteine amide.
{ECO:0000269|PubMed:8206995}.
DISULFID 6 16 In Imi-ribbon form; alternate.
{ECO:0000269|PubMed:22891240}.
DISULFID 6 12 In Imi-globular form; alternate.
{ECO:0000269|PubMed:10050774,
ECO:0000269|PubMed:10194298,
ECO:0000269|PubMed:10350614,
ECO:0000269|PubMed:10395477,
ECO:0000269|PubMed:10431825,
ECO:0000269|PubMed:11124036}.
DISULFID 7 16 In Imi-globular form; alternate.
{ECO:0000269|PubMed:10050774,
ECO:0000269|PubMed:10194298,
ECO:0000269|PubMed:10350614,
ECO:0000269|PubMed:10395477,
ECO:0000269|PubMed:10431825,
ECO:0000269|PubMed:11124036}.
DISULFID 7 12 In Imi-ribbon form; alternate.
{ECO:0000269|PubMed:22891240}.
MUTAGEN 9 9 D->L: Reduction of toxicity.
{ECO:0000269|PubMed:11124036}.
MUTAGEN 10 10 P->R: Loss of ability to compete with
alpha-bungarotoxin.
{ECO:0000269|PubMed:12384509}.
MUTAGEN 11 11 R->L: Reduction of toxicity.
{ECO:0000269|PubMed:11124036}.
MUTAGEN 15 15 R->E: No loss of activity.
{ECO:0000269|PubMed:11124036}.
NON_TER 1 1
HELIX 6 8 {ECO:0000244|PDB:2BYP}.
TURN 10 12 {ECO:0000244|PDB:2BYP}.
HELIX 13 15 {ECO:0000244|PDB:2BYP}.
SEQUENCE 17 AA; 1938 MW; 9590D9CEA50279CF CRC64;
IVRRGCCSDP RCAWRCG


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