ID   CYO19_VIOOD             Reviewed;          31 AA.
AC   P85182;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Cycloviolacin-O19;
OS   Viola odorata (Sweet violet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=97441;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=16872274; DOI=10.1042/bj20060627;
RA   Ireland D.C., Colgrave M.L., Craik D.J.;
RT   "A novel suite of cyclotides from Viola odorata: sequence variation and the
RT   implications for structure, function and stability.";
RL   Biochem. J. 400:1-12(2006).
RN   [2]
RP   TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28621949; DOI=10.1021/acs.jnatprod.6b01004;
RA   Narayani M., Chadha A., Srivastava S.;
RT   "Cyclotides from the Indian Medicinal Plant Viola odorata (Banafsha):
RT   Identification and Characterization.";
RL   J. Nat. Prod. 80:1972-1980(2017).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in petioles and runners but not in
CC       leaves, petals and roots (at protein level).
CC       {ECO:0000269|PubMed:28621949}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P56871}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:16872274}.
CC   -!- MASS SPECTROMETRY: Mass=3226.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16872274};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC       similarity to OAK1 (kalata-B1) for which the DNA sequence is known.
CC       {ECO:0000269|PubMed:16872274}.
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DR   AlphaFoldDB; P85182; -.
DR   SMR; P85182; -.
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   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   Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT   PEPTIDE         1..31
FT                   /note="Cycloviolacin-O19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:16872274"
FT                   /id="PRO_0000294948"
FT   DISULFID        5..21
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..28
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..31
FT                   /note="Cyclopeptide (Gly-Asp)"
FT                   /evidence="ECO:0000269|PubMed:16872274"
SQ   SEQUENCE   31 AA;  3253 MW;  3E36AA52F73EF3B2 CRC64;
     GTLPCGESCV WIPCISSVVG CSCKSKVCYK D