ID   U6TC_CONTE              Reviewed;          23 AA.
AC   P58845;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Textile convulsant peptide {ECO:0000303|Ref.1};
DE            Short=TCP {ECO:0000303|PubMed:23031820};
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AMIDATION AT PRO-23, BIOASSAY, AND
RP   FUNCTION.
RA   Cruz L.J., Ramilo C.A., Corpuz G.P., Olivera B.M.;
RT   "Conus peptides: phylogenetic range of biological activity.";
RL   Biol. Bull. 183:159-164(1992).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=22709442; DOI=10.1021/pr300312h;
RA   Bhatia S., Kil Y.J., Ueberheide B., Chait B.T., Tayo L., Cruz L., Lu B.,
RA   Yates J.R. III, Bern M.;
RT   "Constrained de novo sequencing of conotoxins.";
RL   J. Proteome Res. 11:4191-4200(2012).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, POSITION IN VENOM
RP   DUCT, AND AMIDATION AT PRO-23.
RC   TISSUE=Venom;
RX   PubMed=23031820; DOI=10.1016/j.toxicon.2012.09.013;
RA   Dobson R., Collodoro M., Gilles N., Turtoi A., De Pauw E., Quinton L.;
RT   "Secretion and maturation of conotoxins in the venom ducts of Conus
RT   textile.";
RL   Toxicon 60:1370-1379(2012).
CC   -!- FUNCTION: Causes convulsions mice. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. Is present in all duct
CC       parts with a highest content in part 2 (proximal of the venom bulb) and
CC       then decreases in concentration toward the end of the duct.
CC       {ECO:0000305|PubMed:23031820, ECO:0000305|Ref.1}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC       {ECO:0000250|UniProtKB:Q26443}.
CC   -!- PTM: The C-terminal amidation is described in Ref.1 and
CC       PubMed:23031820, but not in PubMed:22709442. {ECO:0000305}.
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DR   PIR; A59048; A59048.
DR   AlphaFoldDB; P58845; -.
DR   ConoServer; 1810; Textile convulsant peptide.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Knottin; Neurotoxin;
KW   Secreted; Toxin.
FT   PEPTIDE         1..23
FT                   /note="Textile convulsant peptide"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000044487"
FT   MOD_RES         23
FT                   /note="Proline amide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442,
FT                   ECO:0000269|PubMed:23031820, ECO:0000269|Ref.1"
FT   DISULFID        2..10
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        5..15
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        9..20
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   23 AA;  2496 MW;  AE99BDBB7DC8AD56 CRC64;
     NCPYCVVYCC PPAYCEASGC RPP