CM34_CONPE
ID CM34_CONPE Reviewed; 36 AA.
AC Q9BP43;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Conotoxin PnMLKMF-01;
DE Flags: Precursor; Fragment;
OS Conus pennaceus (Feathered cone) (Conus episcopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX NCBI_TaxID=37335;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL Mol. Biol. Evol. 18:120-131(2001).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:11158371}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 1 branch, since 1 residue stands between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR EMBL; AF215130; AAG60535.1; -; mRNA.
DR AlphaFoldDB; Q9BP43; -.
DR ConoServer; 791; Pn3.4 precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Disulfide bond; Neurotoxin; Secreted; Toxin.
FT PROPEP <1..16
FT /evidence="ECO:0000255"
FT /id="PRO_0000404882"
FT PEPTIDE 17..36
FT /note="Conotoxin PnMLKMF-01"
FT /evidence="ECO:0000255"
FT /id="PRO_0000404883"
FT DISULFID 21..33
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 22..31
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 27..34
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT NON_TER 1
SQ SEQUENCE 36 AA; 3683 MW; 04C74E40FF71141C CRC64;
DDNPGGASGK FMNVLKGQPL CCPFGGCHEL CHCCGS