ID   CDKC_CONVX              Reviewed;          47 AA.
AC   P0C1W7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Alpha-conotoxin VxXXC {ECO:0000303|PubMed:16790424};
DE   AltName: Full=VxXIIC {ECO:0000303|PubMed:16790424};
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   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-10; PRO-21 AND PRO-29, MASS
RP   SPECTROMETRY, SUBUNIT, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=16790424; DOI=10.1074/jbc.m603703200;
RA   Loughnan M., Nicke A., Jones A., Schroeder C.I., Nevin S.T., Adams D.J.,
RA   Alewood P.F., Lewis R.J.;
RT   "Identification of a novel class of nicotinic receptor antagonists: dimeric
RT   conotoxins VxXIIA, VxXIIB and VxXIIC from Conus vexillum.";
RL   J. Biol. Chem. 281:24745-24755(2006).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=19275168; DOI=10.1021/bi9000326;
RA   Loughnan M.L., Nicke A., Lawrence N., Lewis R.J.;
RT   "Novel alpha D-conopeptides and their precursors identified by cDNA cloning
RT   define the D-conotoxin superfamily.";
RL   Biochemistry 48:3717-3729(2009).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       This toxin specifically blocks mammalian neuronal nAChR of the alpha-
CC       7/CHRNA7, alpha-3-beta-2/CHRNA3-CHRNB2 and alpha-4-beta-2/CHRNA4-CHRNB2
CC       subtypes. VxXXA and VxXXB inhibit alpha-7/CHRNA7 and alpha-3-beta-
CC       2/CHRNA3-CHRNB2 nAChR more efficiently than VxXXC. VxXXB is the most
CC       effective at inhibiting alpha-4-beta-2/CHRNA4-CHRNB2 nAChR, followed by
CC       VxXXC and VxXXA. {ECO:0000269|PubMed:16790424}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16790424}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16790424}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:16790424}.
CC   -!- DOMAIN: The cysteine framework is XX (C-CC-C-CC-C-C-C-C).
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000305}.
CC   -!- PTM: HydroxyPro-10 is only found in a minor form.
CC   -!- MASS SPECTROMETRY: Mass=5282.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16790424};
CC   -!- SIMILARITY: Belongs to the conotoxin D superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1W7; -.
DR   SMR; P0C1W7; -.
DR   ConoServer; 1684; VxXXC.
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.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..47
FT                   /note="Alpha-conotoxin VxXXC"
FT                   /id="PRO_0000249796"
FT   MOD_RES         10
FT                   /note="Hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:16790424"
FT   MOD_RES         21
FT                   /note="Hydroxyproline; partial"
FT                   /evidence="ECO:0000305|PubMed:16790424"
FT   MOD_RES         29
FT                   /note="Hydroxyproline; partial"
FT                   /evidence="ECO:0000305|PubMed:16790424"
SQ   SEQUENCE   47 AA;  5286 MW;  A4AF94883E74571C CRC64;
     DLRQCTRNAP GSTWGRCCLN PMCGNFCCPR SGCTCAYNWR RGIYCSC