O16C_CONPI
ID O16C_CONPI Reviewed; 24 AA.
AC P0CH19;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Conotoxin pr6c {ECO:0000303|PubMed:20570703};
OS Conus parius (Cone snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX NCBI_TaxID=505247;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=20570703; DOI=10.1016/j.peptides.2010.05.020;
RA Jimenez E.C., Olivera B.M.;
RT "Divergent M- and O-superfamily peptides from venom of fish-hunting Conus
RT parius.";
RL Peptides 31:1678-1683(2010).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20570703}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:20570703}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- PTM: The three Pro-12, Pro-13 and Pro-24 were found to be not
CC hydroxylated. {ECO:0000269|PubMed:20570703}.
CC -!- MASS SPECTROMETRY: Mass=2614.0; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:20570703};
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DR AlphaFoldDB; P0CH19; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Secreted; Toxin.
FT PEPTIDE 1..24
FT /note="Conotoxin pr6c"
FT /evidence="ECO:0000269|PubMed:20570703"
FT /id="PRO_0000397117"
FT DISULFID 3..11
FT /evidence="ECO:0000250"
FT DISULFID 6..16
FT /evidence="ECO:0000250"
FT DISULFID 10..21
FT /evidence="ECO:0000250"
SQ SEQUENCE 24 AA; 2620 MW; 16F77A697AA56331 CRC64;
DQCTYCGIYC CPPKFCTSSG CRSP