ID   CTA1_CONPE              Reviewed;          64 AA.
AC   Q9BPE9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Chi-conotoxin-like PnMRCL-013 {ECO:0000303|PubMed:11158371};
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   -!- FUNCTION: Chi-conotoxins inhibit the neuronal noradrenaline transporter
CC       (NET/SLC6A2). {ECO:0000250|UniProtKB:P58808}.
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 X (CC-CX[hydroxyPro]C).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; AF214980; AAG60408.1; -; mRNA.
DR   PDB; 5T6T; NMR; -; A=52-63.
DR   PDB; 5T6V; NMR; -; A=52-63.
DR   PDBsum; 5T6T; -.
DR   PDBsum; 5T6V; -.
DR   AlphaFoldDB; Q9BPE9; -.
DR   BMRB; Q9BPE9; -.
DR   SMR; Q9BPE9; -.
DR   ConoServer; 667; Pn10.1 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   1: Evidence at protein level;
KW   3D-structure; Amidation; Disulfide bond; Hydroxylation; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..51
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404979"
FT   PEPTIDE         52..63
FT                   /note="Chi-conotoxin-like PnMRCL-013"
FT                   /evidence="ECO:0000305|PubMed:11158371"
FT                   /id="PRO_0000404980"
FT   MOD_RES         62
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..60
FT                   /evidence="ECO:0000312|PDB:5T6T, ECO:0000312|PDB:5T6V"
FT   DISULFID        55..63
FT                   /evidence="ECO:0000312|PDB:5T6T, ECO:0000312|PDB:5T6V"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:5T6T"
SQ   SEQUENCE   64 AA;  6928 MW;  0AB87620FCCC1410 CRC64;
     MRCLPVFVIL LLLTASGPSV DAKVHLKTKG DGPLSSFRDN AKSTLQRLQD KSTCCGYRMC
     VPCG