ID   CYC4_CHACT              Reviewed;          78 AA.
AC   I0B6F3;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Chassatide C4 {ECO:0000303|PubMed:22467870};
DE   AltName: Full=Cyclotide chaC4 {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:AFH57353.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-71, MASS SPECTROMETRY,
RP   AND IDENTIFICATION BY MASS 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   -!- 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=2962; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22467870};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000303|PubMed:22467870}.
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DR   EMBL; JQ309963; AFH57353.1; -; mRNA.
DR   AlphaFoldDB; I0B6F3; -.
DR   SMR; I0B6F3; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   SUPFAM; SSF57038; SSF57038; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Plant defense; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..42
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:22467870"
FT                   /id="PRO_0000440224"
FT   PEPTIDE         43..71
FT                   /note="Chassatide C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:22467870"
FT                   /id="PRO_0000440225"
FT   PROPEP          72..78
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:22467870"
FT                   /id="PRO_0000440226"
FT   DISULFID        46..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        50..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        55..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        43..71
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:22467870"
SQ   SEQUENCE   78 AA;  8317 MW;  9EF7C460BEA107EC CRC64;
     MAKFATQLFL LTASVVMLEV QSSIVIMQDP DLGRKLIMNP ANGASCGETC FTGICFTAGC
     SCNPWPTCTR NGLNPESI