O165_CONIM
ID O165_CONIM Reviewed; 78 AA.
AC Q5K0C1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Conotoxin 5;
DE Flags: Precursor;
OS Conus imperialis (Imperial cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX NCBI_TaxID=35631;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=15652641; DOI=10.1016/j.peptides.2004.10.027;
RA Kauferstein S., Melaun C., Mebs D.;
RT "Direct cDNA cloning of novel conopeptide precursors of the O-
RT superfamily.";
RL Peptides 26:361-367(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; AJ851187; CAH64860.1; -; mRNA.
DR AlphaFoldDB; Q5K0C1; -.
DR SMR; Q5K0C1; -.
DR ConoServer; 1076; Conotoxin-5 precursor.
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; Knottin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..49
FT /evidence="ECO:0000250"
FT /id="PRO_0000034991"
FT PEPTIDE 52..78
FT /note="Conotoxin 5"
FT /id="PRO_0000034992"
FT DISULFID 53..69
FT /evidence="ECO:0000250"
FT DISULFID 60..73
FT /evidence="ECO:0000250"
FT DISULFID 68..77
FT /evidence="ECO:0000250"
SQ SEQUENCE 78 AA; 9044 MW; 2101757363340402 CRC64;
MKLTCMMIVT VLFLTAWIFI TADNSRNGIE NLPRMRRHEM KNPKASKLNK RGCREGGEFC
GTLYEERCCS GWCFFVCV