CA12_CONVC
ID CA12_CONVC Reviewed; 64 AA.
AC E2DIH5;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Alpha-conotoxin Vc1.2;
DE Flags: Precursor;
OS Conus victoriae (Queen Victoria cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX NCBI_TaxID=319920;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 45-60, FUNCTION, DEVELOPMENTAL
RP STAGE, AND STRUCTURE BY NMR OF 45-60.
RC TISSUE=Embryo, and Venom duct;
RX PubMed=21504902; DOI=10.1074/jbc.m110.217703;
RA Safavi-Hemami H., Siero W.A., Kuang Z., Williamson N.A., Karas J.A.,
RA Page L.R., Macmillan D., Callaghan B., Kompella S.N., Adams D.J.,
RA Norton R.S., Purcell A.W.;
RT "Embryonic toxin expression in the cone snail Conus victoriae: primed to
RT kill or divergent function?";
RL J. Biol. Chem. 286:22546-22557(2011).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC Shows inhibition on alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=75 nM), alpha-
CC 7/CHRNA7 (IC(50)=637 nM) and alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs
CC (IC(50)=1000 nM). In addition, it also shows inhibition on high-voltage
CC activated (HVA) calcium channels currents (30% at 100 nM) that are
CC mediated by GABA(B) receptors (GABBR1 and GABBR2).
CC {ECO:0000269|PubMed:21504902}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21504902}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:21504902}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in embryos. Also slightly
CC expressed in adults, but the toxin is not found in adult venom.
CC {ECO:0000269|PubMed:21504902}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC -!- MISCELLANEOUS: Does not show activity on alpha-3/beta-4
CC (CHRNA3/CHRNB4), alpha-4/beta-2 (CHRNA4/CHRNB2) and alpha-4/beta-4
CC (CHRNA4/CHRNB4) acetylcholine receptors. {ECO:0000305|PubMed:21504902}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; GU046308; ADC80509.1; -; mRNA.
DR AlphaFoldDB; E2DIH5; -.
DR BMRB; E2DIH5; -.
DR ConoServer; 4199; Vc1.2 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.
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 Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..43
FT /evidence="ECO:0000250"
FT /id="PRO_0000425159"
FT PEPTIDE 45..60
FT /note="Alpha-conotoxin Vc1.2"
FT /id="PRO_0000425160"
FT REGION 48..50
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MOD_RES 60
FT /note="Cysteine amide"
FT /evidence="ECO:0000250"
FT DISULFID 46..52
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 47..60
FT /evidence="ECO:0000250|UniProtKB:P56636"
SQ SEQUENCE 64 AA; 6988 MW; 1B53A5F883DD2B56 CRC64;
MGMRMMFTVF LLVVLATTVV FFTSDRASDG RKAAASDLIT LTIKGCCSNP ACMVNNPQIC
GRRR
