O16D_CONPI
ID O16D_CONPI Reviewed; 32 AA.
AC P0CH20;
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 pr6d;
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, NUCLEOTIDE SEQUENCE [MRNA], HYDROXYLATION AT PRO-5, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom duct;
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC -!- MASS SPECTROMETRY: Mass=3531.1; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:20570703};
CC -!- MISCELLANEOUS: Authors confirmed the assignment of this toxin to the M
CC superfamily by cDNA sequencing.
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DR AlphaFoldDB; P0CH20; -.
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; Hydroxylation; Knottin;
KW Secreted; Toxin.
FT PEPTIDE 1..32
FT /note="Conotoxin pr6d"
FT /id="PRO_0000397118"
FT MOD_RES 5
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20570703"
FT DISULFID 7..20
FT /evidence="ECO:0000250"
FT DISULFID 14..25
FT /evidence="ECO:0000250"
FT DISULFID 19..30
FT /evidence="ECO:0000250"
SQ SEQUENCE 32 AA; 3521 MW; 8817951B9E3E0199 CRC64;
YGNFPTCSET GEDCSAMHCC RSMTCRNNIC AD