CA1G_CONCN
ID CA1G_CONCN Reviewed; 50 AA.
AC P0DKP8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Alpha-conotoxin CnIG;
DE Flags: Precursor; Fragment;
OS Conus consors (Singed cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX NCBI_TaxID=101297;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT CYS-48, MASS SPECTROMETRY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom duct;
RX PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA Stocklin R., Favreau P.;
RT "Large-scale discovery of conopeptides and conoproteins in the injectable
RT venom of a fish-hunting cone snail using a combined proteomic and
RT transcriptomic approach.";
RL J. Proteomics 75:5215-5225(2012).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC -!- MASS SPECTROMETRY: Mass=1353.54; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22705119};
CC -!- MISCELLANEOUS: Found in injectable (milked) (IV) venom.
CC {ECO:0000305|PubMed:22705119}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DKP8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR009958; Conotoxin_a-typ.
DR Pfam; PF07365; Toxin_8; 1.
PE 1: Evidence at protein level;
KW Amidation; Disulfide bond; Secreted; Signal; Toxin.
FT SIGNAL <1..7
FT /evidence="ECO:0000255"
FT PROPEP 8..35
FT /id="PRO_0000419874"
FT PEPTIDE 37..48
FT /note="Alpha-conotoxin CnIG"
FT /id="PRO_0000419875"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:22705119"
FT DISULFID 37..42
FT /evidence="ECO:0000250|UniProtKB:P01519"
FT DISULFID 38..48
FT /evidence="ECO:0000250|UniProtKB:P01519"
FT NON_TER 1
SQ SEQUENCE 50 AA; 5603 MW; 16617F6AB3CB24AA CRC64;
LTTTVVSFPS DSASDGRDNE AKDERSDMYE LKRNGRCCHP ACGKYFKCGR