CA1A_CONVE
ID CA1A_CONVE Reviewed; 17 AA.
AC P0C8V4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Alpha-conotoxin-like Vn {ECO:0000303|PubMed:18266261};
DE AltName: Full=Vn1A {ECO:0000305};
OS Conus ventricosus (Mediterranean cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lautoconus.
OX NCBI_TaxID=117992;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT CYS-17, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=18266261; DOI=10.1002/jssc.200700448;
RA Romeo C., Di Francesco L., Oliverio M., Palazzo P., Massilia G.R.,
RA Ascenzi P., Polticelli F., Schinina M.E.;
RT "Conus ventricosus venom peptides profiling by HPLC-MS: a new insight in
RT the intraspecific variation.";
RL J. Sep. Sci. 31:488-498(2008).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18266261}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:18266261}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C8V4; -.
DR ConoServer; 3712; Vn1A.
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; Amidation;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..17
FT /note="Alpha-conotoxin-like Vn"
FT /id="PRO_0000366082"
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 17
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:18266261"
FT DISULFID 3..9
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 4..17
FT /evidence="ECO:0000250|UniProtKB:P56636"
SQ SEQUENCE 17 AA; 1723 MW; 76F7F3995FD87F15 CRC64;
GGCCSYPPCA VSNPQHC