ID   CYC13_CHACT             Reviewed;          77 AA.
AC   I0B6G2;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Chassatide C13 {ECO:0000303|PubMed:22467870};
DE   AltName: Full=Cyclotide chaC13 {ECO:0000303|PubMed:22467870};
DE   Flags: Precursor;
OS   Chassalia chartacea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Palicoureeae;
OC   Chassalia.
OX   NCBI_TaxID=510798;
RN   [1] {ECO:0000312|EMBL:AFH57356.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RX   PubMed=22467870; DOI=10.1074/jbc.m111.338970;
RA   Nguyen G.K., Lim W.H., Nguyen P.Q., Tam J.P.;
RT   "Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from
RT   Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities.";
RL   J. Biol. Chem. 287:17598-17607(2012).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- TISSUE SPECIFICITY: Expressed in fruit and pedicel but not in root,
CC       leaf and stem (at protein level). {ECO:0000269|PubMed:22467870}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- MASS SPECTROMETRY: Mass=3373; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22467870};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; JQ309966; AFH57356.1; -; mRNA.
DR   EMBL; JQ309972; AFH57362.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0B6G2; -.
DR   SMR; I0B6G2; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012323; Cyclotide_bracelet_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   SUPFAM; SSF57038; SSF57038; 1.
DR   PROSITE; PS51052; CYCLOTIDE; 1.
DR   PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Knottin; Plant defense; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..44
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:22467870"
FT                   /id="PRO_0000440235"
FT   PEPTIDE         45..75
FT                   /note="Chassatide C13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:22467870"
FT                   /id="PRO_0000440236"
FT   PROPEP          76..77
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:22467870"
FT                   /id="PRO_0000440237"
FT   DISULFID        48..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        52..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        57..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        45..75
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000303|PubMed:22467870"
SQ   SEQUENCE   77 AA;  8581 MW;  F595BC6EECFBA3A4 CRC64;
     MAKFATQLLL FVLIASLVML EVHASNTFQV PDLGKRLLMN RDPNGFPCAE SCVYIPCTVT
     ALLGCSCRNR VCYRNEL