CA4B_CONER
ID CA4B_CONER Reviewed; 30 AA.
AC P58783;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Alpha-conotoxin EIVB;
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).
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 -!- PTM: Contains 3 disulfide bonds (By similarity). They are not added,
CC since framework IV presents two different connectivities (I-V, II-III,
CC IV-VI and I-III, II-V, IV-VI). {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=3099.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9278406};
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P58783; -.
DR SMR; P58783; -.
DR ConoServer; 1740; EIVB.
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 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 EIVB"
FT /id="PRO_0000044465"
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"
SQ SEQUENCE 30 AA; 3027 MW; 5F2D8FD1AF20F483 CRC64;
GCCGKYPNAA CHPCGCTVGR PPYCDRPSGG
