ID   CT5M_CONPE              Reviewed;          60 AA.
AC   Q9BPH2;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Conotoxin PnMRCL-022 {ECO:0000312|EMBL:AAG60383.1};
DE   Flags: Precursor;
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 V (CC-CC). {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF214955; AAG60383.1; -; mRNA.
DR   AlphaFoldDB; Q9BPH2; -.
DR   ConoServer; 642; Pn5.1 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404973"
FT   PEPTIDE         48..60
FT                   /note="Conotoxin PnMRCL-022"
FT                   /id="PRO_0000404974"
SQ   SEQUENCE   60 AA;  7082 MW;  B8500078EBA9901E CRC64;
     MRCLPVFVIL LLLIASTPSV NARPKTKDLA SFHDNAKRTQ HIFWSKRNCC IYENWCCEWI