ID   CA4A_CONER              Reviewed;          30 AA.
AC   P58782;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Alpha-conotoxin EIVA;
OS   Conus ermineus (Agate cone) (Chelyconus ermineus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX   NCBI_TaxID=55423;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, MASS SPECTROMETRY, HYDROXYLATION AT PRO-7;
RP   PRO-13; PRO-21; PRO-22 AND PRO-27, AND AMIDATION AT GLY-30.
RC   TISSUE=Venom;
RX   PubMed=9278406; DOI=10.1074/jbc.272.36.22531;
RA   Jacobsen R.B., Yoshikami D., Ellison M., Martinez J., Gray W.R.,
RA   Cartier G.E., Shon K.-J., Groebe D.R., Abramson S.N., Olivera B.M.,
RA   McIntosh J.M.;
RT   "Differential targeting of nicotinic acetylcholine receptors by novel
RT   alphaA-conotoxins.";
RL   J. Biol. Chem. 272:22531-22537(1997).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=12900418; DOI=10.1074/jbc.m303342200;
RA   Chi S.-W., Park K.-H., Suk J.-E., Olivera B.M., McIntosh J.M., Han K.-H.;
RT   "Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular
RT   nicotinic acetylcholine receptor antagonist from Conus ermineus.";
RL   J. Biol. Chem. 278:42208-42213(2003).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       This toxin binds with high affinity to both fetal (alpha-1/beta-
CC       1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta
CC       subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC   -!- MASS SPECTROMETRY: Mass=3095.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9278406};
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   PDB; 1PQR; NMR; -; A=1-30.
DR   PDBsum; 1PQR; -.
DR   AlphaFoldDB; P58782; -.
DR   SMR; P58782; -.
DR   ConoServer; 1635; EIVA.
DR   EvolutionaryTrace; P58782; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012498; Toxin_14.
DR   Pfam; PF07829; Toxin_14; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PEPTIDE         1..30
FT                   /note="Alpha-conotoxin EIVA"
FT                   /id="PRO_0000044464"
FT   MOD_RES         7
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:9278406"
FT   MOD_RES         13
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:9278406"
FT   MOD_RES         21
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:9278406"
FT   MOD_RES         22
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:9278406"
FT   MOD_RES         27
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:9278406"
FT   MOD_RES         30
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:9278406"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000269|PubMed:12900418"
FT   DISULFID        3..11
FT                   /evidence="ECO:0000269|PubMed:12900418"
FT   DISULFID        14..24
FT                   /evidence="ECO:0000269|PubMed:12900418"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:1PQR"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:1PQR"
FT   HELIX           22..25
FT                   /evidence="ECO:0007829|PDB:1PQR"
SQ   SEQUENCE   30 AA;  3023 MW;  5F373E7AAF385783 CRC64;
     GCCGPYPNAA CHPCGCKVGR PPYCDRPSGG