CA1B_CONAL
ID CA1B_CONAL Reviewed; 58 AA.
AC P56640;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Alpha-conotoxin AuIB {ECO:0000303|PubMed:9786965};
DE Flags: Precursor;
OS Conus aulicus (Princely cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX NCBI_TaxID=89437;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Venom;
RA Watkins M., Olivera B.M., Hillyard D.R., McIntosh J.M., Jones R.M.;
RT "Alpha-conotoxin peptides.";
RL Patent number US6797808, 28-SEP-2004.
RN [2]
RP PROTEIN SEQUENCE OF 40-54, SYNTHESIS OF 40-54, FUNCTION, AMIDATION AT
RP CYS-54, DISULFIDE BONDS, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=9786965; DOI=10.1523/jneurosci.18-21-08571.1998;
RA Luo S., Kulak J.M., Cartier G.E., Jacobsen R.B., Yoshikami D.,
RA Olivera B.M., McIntosh J.M.;
RT "Alpha-conotoxin AuIB selectively blocks alpha3 beta4 nicotinic
RT acetylcholine receptors and nicotine-evoked norepinephrine release.";
RL J. Neurosci. 18:8571-8579(1998).
RN [3]
RP FUNCTION.
RX PubMed=25466886; DOI=10.1096/fj.14-262733;
RA Heghinian M.D., Mejia M., Adams D.J., Godenschwege T.A., Mari F.;
RT "Inhibition of cholinergic pathways in Drosophila melanogaster by alpha-
RT conotoxins.";
RL FASEB J. 29:1011-1018(2015).
RN [4]
RP STRUCTURE BY NMR, AMIDATION AT CYS-54, AND DISULFIDE BONDS.
RX PubMed=10722709; DOI=10.1074/jbc.275.12.8680;
RA Cho J.H., Mok K.H., Olivera B.M., McIntosh J.M., Park K.H., Han K.H.;
RT "Nuclear magnetic resonance solution conformation of alpha-conotoxin AuIB,
RT an alpha(3)beta(4) subtype-selective neuronal nicotinic acetylcholine
RT receptor antagonist.";
RL J. Biol. Chem. 275:8680-8685(2000).
RN [5]
RP STRUCTURE BY NMR, AMIDATION AT CYS-54, AND DISULFIDE BONDS.
RX PubMed=12376538; DOI=10.1074/jbc.m208842200;
RA Dutton J.L., Bansal P.S., Hogg R.C., Adams D.J., Alewood P.F., Craik D.J.;
RT "A new level of conotoxin diversity, a non-native disulfide bond
RT connectivity in alpha-conotoxin AuIB reduces structural definition but
RT increases biological activity.";
RL J. Biol. Chem. 277:48849-48857(2002).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin blocks mammalian nAChR alpha-3-beta-4/CHRNA3-CHRNB4
CC subunits. Also exhibits inhibition of D.melanogaster alpha-7 nAChRs
CC (PubMed:25466886). {ECO:0000269|PubMed:25466886,
CC ECO:0000269|PubMed:9786965}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9786965}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:9786965}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/6 pattern.
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1572.5; Method=LSI;
CC Evidence={ECO:0000269|PubMed:9786965};
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; AR584804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B59045; B59045.
DR PDB; 1DG2; NMR; -; A=40-54.
DR PDB; 1MXN; NMR; -; A=40-54.
DR PDB; 1MXP; NMR; -; A=40-54.
DR PDBsum; 1DG2; -.
DR PDBsum; 1MXN; -.
DR PDBsum; 1MXP; -.
DR AlphaFoldDB; P56640; -.
DR SMR; P56640; -.
DR ConoServer; 2879; AuIB precursor.
DR EvolutionaryTrace; P56640; -.
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; IPR009958; Conotoxin_a-typ.
DR InterPro; IPR018072; Conotoxin_a-typ_CS.
DR Pfam; PF07365; Toxin_8; 1.
DR PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..39
FT /evidence="ECO:0000269|PubMed:9786965"
FT /id="PRO_0000381164"
FT PEPTIDE 40..54
FT /note="Alpha-conotoxin AuIB"
FT /evidence="ECO:0000269|PubMed:9786965"
FT /id="PRO_0000044455"
FT MOD_RES 54
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:10722709,
FT ECO:0000269|PubMed:12376538, ECO:0000269|PubMed:9786965"
FT DISULFID 41..47
FT /evidence="ECO:0000269|PubMed:10722709,
FT ECO:0000269|PubMed:12376538, ECO:0000269|PubMed:9786965,
FT ECO:0000312|PDB:1DG2, ECO:0000312|PDB:1MXN"
FT DISULFID 42..54
FT /evidence="ECO:0000269|PubMed:10722709,
FT ECO:0000269|PubMed:12376538, ECO:0000269|PubMed:9786965,
FT ECO:0000312|PDB:1DG2, ECO:0000312|PDB:1MXN"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1DG2"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1DG2"
SQ SEQUENCE 58 AA; 6219 MW; 309EBFCD2DF9E4D0 CRC64;
MFTVFLLVVL ATTVVSFTSD RASDGRKDAA SGLIALTMKG CCSYPPCFAT NPDCGRRR
