ID   CBOA_CONVX              Reviewed;          68 AA.
AC   J7JU64;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Alpha-conotoxin VxXXIVA {ECO:0000305};
DE   AltName: Full=AlphaB-conotoxin VxXXIVA {ECO:0000303|PubMed:23382933};
DE   Flags: Precursor;
OS   Conus vexillum (Flag cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Rhizoconus.
OX   NCBI_TaxID=89431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 29-68, AND FUNCTION.
RC   TISSUE=Venom duct;
RX   PubMed=23382933; DOI=10.1371/journal.pone.0054648;
RA   Luo S., Christensen S., Zhangsun D., Wu Y., Hu Y., Zhu X., Chhabra S.,
RA   Norton R.S., McIntosh J.M.;
RT   "A novel inhibitor of alpha9alpha10 nicotinic acetylcholine receptors from
RT   Conus vexillum delineates a new conotoxin superfamily.";
RL   PLoS ONE 8:E54648-E54648(2013).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       The toxin with a disulfide connectivity C1-C2, C3-C4 (shown in the
CC       sequence annotation) block the rat nicotinic acetylcholine receptor
CC       (AChR) alpha-9-alpha-10/CHRNA9-CHRNA10 with an IC(50) of 1.2 uM,
CC       whereas the one with C1-C3, C2-C4 shows a lower activity with an IC(50)
CC       of 3.9 uM. {ECO:0000269|PubMed:23382933}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:23382933}.
CC   -!- DOMAIN: The cysteine framework is XXIV (C-CC-C). {ECO:0000305}.
CC   -!- PTM: The 3 possibles disulfide-bond connectivities isomers have been
CC       synthesized: (C1-C2, C3-C4), (C1-C3, C2-C4), and (C1-C4, C2-C3).
CC       {ECO:0000269|PubMed:23382933}.
CC   -!- MISCELLANEOUS: The 3 disulfide isomers are poorly structured in aqueous
CC       solution. {ECO:0000305|PubMed:23382933}.
CC   -!- MISCELLANEOUS: The toxin (with connectivity C1-C2, C3-C4) does not have
CC       inhibitory effect on alpha-2-beta-4/CHRNA2-CHRNB4, alpha-3-beta-
CC       2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-2/CHRNA4-
CC       CHRNB2, alpha-4-beta-4/CHRNA4-CHRNB4 and alpha-7/CHRNA7. The toxin
CC       (with connectivity C1-C4, C2-C3) does not have inhibitory effect on
CC       alpha-9-alpha-10/CHRNA9-CHRNA10 (PubMed:23382933).
CC       {ECO:0000305|PubMed:23382933}.
CC   -!- SIMILARITY: Belongs to the conotoxin B superfamily. {ECO:0000305}.
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DR   EMBL; JX297421; AFQ60002.1; -; mRNA.
DR   AlphaFoldDB; J7JU64; -.
DR   ConoServer; 5525; VxXXIVA precursor.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..68
FT                   /note="Alpha-conotoxin VxXXIVA"
FT                   /evidence="ECO:0000305|PubMed:23382933"
FT                   /id="PRO_0000422882"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000305"
FT   DISULFID        48..60
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   68 AA;  7724 MW;  BD9221F8BF7BA01A CRC64;
     METLTLLWRA SSSCLLVVLS HSLLRLLGVR CLEKSGAQPN KLFRPPCCQK GPSFARHSRC
     VYYTQSRE