CYC11_CHACT
ID CYC11_CHACT Reviewed; 28 AA.
AC C0HKH6;
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 C11 {ECO:0000303|PubMed:22467870};
DE AltName: Full=Cyclotide chaC11 {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, FUNCTION, TISSUE SPECIFICITY, MASS SPECTROMETRY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND OXIDATION AT MET-16.
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: Chassatide C11: Probably participates in a plant defense
CC mechanism (Probable). Active against E.coli ATCC 25922 (MIC=8.5 uM) but
CC not against S.aureus ATCC 12600 or S.epidermidis ATCC 14990
CC (PubMed:22467870). Has cytotoxic and hemolytic activity
CC (PubMed:22467870). {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:22467870}.
CC -!- FUNCTION: Chassatide C11A: Probably participates in a plant defense
CC mechanism (Probable). Has no activity against bacteria up to a
CC concentration of 80 uM (PubMed:22467870). Has no cytotoxic and no
CC hemolytic activity (PubMed:22467870). {ECO:0000255|PROSITE-
CC ProRule:PRU00395, ECO:0000269|PubMed:22467870}.
CC -!- TISSUE SPECIFICITY: Expressed in fruit, pedicel and stem but not in
CC leaf and 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 -!- MASS SPECTROMETRY: Mass=3008; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22467870};
CC -!- MASS SPECTROMETRY: Mass=3024; Method=MALDI; Note=Chassatide cha11A.;
CC Evidence={ECO:0000269|PubMed:22467870};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- CAUTION: This peptide is linear as it lacks the C-terminal Asp/Asn
CC residue required for cyclization. {ECO:0000269|PubMed:22467870}.
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DR AlphaFoldDB; C0HKH6; -.
DR SMR; C0HKH6; -.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012323; Cyclotide_bracelet_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR PIRSF; PIRSF037891; Cycloviolacin; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Knottin; Oxidation; Plant defense.
FT PEPTIDE 1..28
FT /note="Chassatide C11"
FT /evidence="ECO:0000269|PubMed:22467870"
FT /id="PRO_0000440234"
FT MOD_RES 16
FT /note="Methionine sulfoxide; in form chassatide chaC11A"
FT /evidence="ECO:0000269|PubMed:22467870"
FT DISULFID 3..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 7..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 12..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
SQ SEQUENCE 28 AA; 3017 MW; 002A52E67219865D CRC64;
IPCGESCVWI PCISGMFGCS CKDKVCYS
