CA1B_CONAN
ID CA1B_CONAN Reviewed; 17 AA.
AC P0C1V7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Alpha-conotoxin AnIB {ECO:0000303|PubMed:14971903};
DE Contains:
DE RecName: Full=Alpha-conotoxin AnIA {ECO:0000303|PubMed:14971903};
OS Conus anemone (Anemone cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Floraconus.
OX NCBI_TaxID=101285;
RN [1]
RP PROTEIN SEQUENCE, SULFATION AT TYR-16, AMIDATION AT CYS-17, MASS
RP SPECTROMETRY, SYNTHESIS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-1.
RC TISSUE=Venom;
RX PubMed=14971903; DOI=10.1021/jm031010o;
RA Loughnan M.L., Nicke A., Jones A., Adams D.J., Alewood P.F., Lewis R.J.;
RT "Chemical and functional identification and characterization of novel
RT sulfated alpha-conotoxins from the cone snail Conus anemone.";
RL J. Med. Chem. 47:1234-1241(2004).
CC -!- FUNCTION: [Alpha-conotoxin AnIB]: Alpha-conotoxins act on postsynaptic
CC membranes, they bind to the nicotinic acetylcholine receptors (nAChR)
CC and thus inhibit them. This synthetic toxin blocks rat alpha-3beta-
CC 2/CHRNA3-CHRNB2 nAChRs (IC(50)=0.3 nM) and alpha-7/CHRNA7 nAChRs
CC (IC(50)=76 nM). {ECO:0000269|PubMed:14971903}.
CC -!- FUNCTION: [Alpha-conotoxin AnIA]: This synthetic toxin blocks rat
CC alpha-3-beta-2/CHRNA3-CHRNB2 nAChRs (IC(50)=0.2 nM).
CC {ECO:0000269|PubMed:14971903}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14971903}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:14971903}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- PTM: Amidation at Cys-17 is important for activity, since suppression
CC of this modification induces a 1.9-fold decrease in inhibitory potency
CC on alpha-3-beta-2/CHRNA3-CHRNB2 nAChRs (IC(50)=0.54 nM), and a 4.8-fold
CC decrease in inhibitory potency on alpha-7/CHRNA7 nAChRs (IC(50)=367
CC nM). {ECO:0000269|PubMed:14971903}.
CC -!- PTM: Sulfation at Tyr-16 is important for activity, since suppression
CC of this modification induces a 2.3-fold decrease in inhibitory potency
CC on alpha-3-beta-2/CHRNA3-CHRNB2 nAChRs (IC(50)=0.64 nM), and a 11-fold
CC decrease in inhibitory potency on alpha-7/CHRNA7 nAChRs (IC(50)=836
CC nM). {ECO:0000269|PubMed:14971903}.
CC -!- MASS SPECTROMETRY: [Alpha-conotoxin AnIB]: Mass=1787.4;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:14971903};
CC -!- MASS SPECTROMETRY: [Alpha-conotoxin AnIA]: Mass=1673.4;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:14971903};
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR PDB; 7N20; NMR; -; A=1-17.
DR PDB; 7N21; NMR; -; A=1-17.
DR PDB; 7N22; NMR; -; A=1-17.
DR PDB; 7N23; NMR; -; A=1-17.
DR PDBsum; 7N20; -.
DR PDBsum; 7N21; -.
DR PDBsum; 7N22; -.
DR PDBsum; 7N23; -.
DR AlphaFoldDB; P0C1V7; -.
DR SMR; P0C1V7; -.
DR ConoServer; 15; AnIB.
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; IPR018072; Conotoxin_a-typ_CS.
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; Sulfation; Toxin.
FT PEPTIDE 1..17
FT /note="Alpha-conotoxin AnIB"
FT /evidence="ECO:0000269|PubMed:14971903"
FT /id="PRO_0000249780"
FT PEPTIDE 3..17
FT /note="Alpha-conotoxin AnIA"
FT /evidence="ECO:0000269|PubMed:14971903"
FT /id="PRO_0000249781"
FT REGION 5..7
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MOD_RES 16
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14971903"
FT MOD_RES 17
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:14971903"
FT DISULFID 3..9
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 4..17
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MUTAGEN 1
FT /note="G->GG: 1.4-fold increase in inhibitory potency on
FT alpha-3-beta-2/CHRNA3-CHRNB2."
FT /evidence="ECO:0000269|PubMed:14971903"
FT MUTAGEN 1
FT /note="Missing: 1.6-fold increase in inhibitory potency on
FT alpha-3-beta-2/CHRNA3-CHRNB2."
FT /evidence="ECO:0000269|PubMed:14971903"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:7N20"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:7N20"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:7N20"
SQ SEQUENCE 17 AA; 1714 MW; 76F84AFDFAC99005 CRC64;
GGCCSHPACA ANNQDYC
