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Alpha-conotoxin-like EpI

 CA1_CONEP               Reviewed;          56 AA.
P56638;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 2.
22-NOV-2017, entry version 70.
RecName: Full=Alpha-conotoxin-like EpI;
Flags: Precursor;
Conus episcopatus (Bishop's cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=88764;
[1]
NUCLEOTIDE SEQUENCE.
Watkins M., Olivera B.M., Hillyard D.R., Mcintosh M.J., Jones R.M.;
"Alpha-conotoxin peptides.";
Patent number JP2002534996, 22-OCT-2002.
[2]
PROTEIN SEQUENCE OF 40-55, SYNTHESIS OF 40-55, DISULFIDE BONDS,
SULFATION AT TYR-54, AMIDATION AT CYS-55, AND MASS SPECTROMETRY.
PubMed=9624161; DOI=10.1074/jbc.273.25.15667;
Loughnan M., Bond T., Atkins A., Cuevas J., Adams D.J., Broxton N.M.,
Livett B.G., Down J.G., Jones A., Alewood P.F., Lewis R.J.;
"Alpha-conotoxin EpI, a novel sulfated peptide from Conus episcopatus
that selectively targets neuronal nicotinic acetylcholine receptors.";
J. Biol. Chem. 273:15667-15674(1998).
[3]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 40-55, AMIDATION AT CYS-55,
AND DISULFIDE BONDS.
PubMed=9708977; DOI=10.1021/bi9806549;
Hu S.H., Loughnan M., Miller R., Weeks C.M., Blessing R.H.,
Alewood P.F., Lewis R.J., Martin J.L.;
"The 1.1-A resolution crystal structure of [Tyr15]EpI, a novel alpha-
conotoxin from Conus episcopatus, solved by direct methods.";
Biochemistry 37:11425-11433(1998).
-!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
bind to the nicotinic acetylcholine receptors (nAChR) and thus
inhibit them. This peptide blocks mammalian nicotinic
acetylcholine receptors composed of alpha-3/beta-2 and alpha-
3/beta-4 subunits.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
-!- MASS SPECTROMETRY: Mass=1787.02; Method=Electrospray; Range=40-55;
Note=Without sulfation.; Evidence={ECO:0000269|PubMed:9624161};
-!- MASS SPECTROMETRY: Mass=1867.08; Method=Electrospray; Range=40-55;
Note=With sulfation.; Evidence={ECO:0000269|PubMed:9624161};
-!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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EMBL; BD261428; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
PIR; A59042; A59042.
PDB; 1A0M; X-ray; 1.10 A; A/B=40-55.
PDBsum; 1A0M; -.
SMR; P56638; -.
ConoServer; 405; EpI.
EvolutionaryTrace; P56638; -.
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; Amidation;
Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
Secreted; Signal; Sulfation; Toxin.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 39 {ECO:0000269|PubMed:9624161}.
/FTId=PRO_0000392692.
PEPTIDE 40 55 Alpha-conotoxin-like EpI.
/FTId=PRO_0000044457.
MOD_RES 54 54 Sulfotyrosine.
{ECO:0000269|PubMed:9624161}.
MOD_RES 55 55 Cysteine amide.
{ECO:0000269|PubMed:9624161,
ECO:0000269|PubMed:9708977}.
DISULFID 41 47
DISULFID 42 55
HELIX 41 43 {ECO:0000244|PDB:1A0M}.
HELIX 45 50 {ECO:0000244|PDB:1A0M}.
TURN 52 54 {ECO:0000244|PDB:1A0M}.
SEQUENCE 56 AA; 5977 MW; B8523DFE3EF963CB CRC64;
MFTVFLLVVL ATTVVSFTSD RASDSRKDAA SGLIALTIKG CCSDPRCNMN NPDYCG


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