CYC1_CHACT
ID CYC1_CHACT Reviewed; 29 AA.
AC C0HKH4;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Chassatide C1 {ECO:0000303|PubMed:22467870};
DE AltName: Full=Cyclotide chaC1 {ECO:0000303|PubMed:22467870};
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 {ECO:0000303|PubMed:22467870};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND IDENTIFICATION
RP 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|PROSITE-ProRule:PRU00395}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf, fruit, pedical and stem but not
CC in root (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 ECO:0000269|PubMed:22467870}.
CC -!- MASS SPECTROMETRY: Mass=2990; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22467870};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC {ECO:0000303|PubMed:22467870}.
CC -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC similarity to chassatide C4 for which the DNA sequence is known.
CC {ECO:0000305}.
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DR AlphaFoldDB; C0HKH4; -.
DR SMR; C0HKH4; -.
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.
FT PEPTIDE 1..29
FT /note="Chassatide C1"
FT /evidence="ECO:0000269|PubMed:22467870"
FT /id="PRO_0000440219"
FT DISULFID 4..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 8..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 13..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 1..29
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:22467870"
SQ SEQUENCE 29 AA; 3016 MW; 483EA1440BBFFCD3 CRC64;
GDACGETCFT GICFTAGCSC NPWPTCTRN