CM35_CONPL
ID CM35_CONPL Reviewed; 64 AA.
AC P0CH23;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Conotoxin Pu3.5;
DE Flags: Precursor; Fragment;
OS Conus pulicarius (Flea-bitten cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX NCBI_TaxID=93154;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=20307606; DOI=10.1016/j.peptides.2010.03.010;
RA Wu X.-C., Zhou M., Peng C., Shao X.-X., Guo Z.-Y., Chi C.-W.;
RT "Novel conopeptides in a form of disulfide-crosslinked dimer.";
RL Peptides 31:1001-1006(2010).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 3 branch, since 3 residues stand between the fourth and the fifth
CC cysteine residues.
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CH23; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Secreted; Signal;
KW Toxin.
FT SIGNAL <1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..49
FT /evidence="ECO:0000250"
FT /id="PRO_0000397192"
FT PEPTIDE 50..64
FT /note="Conotoxin Pu3.5"
FT /id="PRO_0000397193"
FT DISULFID 50..63
FT /evidence="ECO:0000250"
FT DISULFID 51..58
FT /evidence="ECO:0000250"
FT DISULFID 54..62
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 64 AA; 6791 MW; ADEFC88AB9E221D5 CRC64;
LGVLLTICLL LFPLTAVPLD GDQPADQPAG RMQDDISSEQ HPFFDPVKRC CVVCNAGCSG
NCCP