ID   M233_CONPE              Reviewed;          20 AA.
AC   Q9BP45;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Conotoxin PnMLKM-D0211;
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|PubMed:11158371}.
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       2 branch, since 2 residues stand 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; AF215128; AAG60533.1; -; mRNA.
DR   AlphaFoldDB; Q9BP45; -.
DR   ConoServer; 789; Pn3.3 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   Amidation; Cleavage on pair of basic residues; Disulfide bond;
KW   Hydroxylation; Neurotoxin; Secreted; Toxin.
FT   PROPEP          <1..3
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404896"
FT   PEPTIDE         4..19
FT                   /note="Conotoxin PnMLKM-D0211"
FT                   /id="PRO_0000404897"
FT   MOD_RES         16
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..18
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        5..14
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        10..17
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   NON_TER         1
SQ   SEQUENCE   20 AA;  2295 MW;  7EB3C48143173BBB CRC64;
     VKRCCDEEEC SSACWPCCWG