ID   CYO1_VIOOD              Reviewed;          30 AA.
AC   P82230;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cycloviolacin-O1;
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]
RP   PROTEIN SEQUENCE, AND STRUCTURE BY NMR.
RX   PubMed=10600388; DOI=10.1006/jmbi.1999.3383;
RA   Craik D.J., Daly N.L., Bond T., Waine C.;
RT   "Plant cyclotides: a unique family of cyclic and knotted proteins that
RT   defines the cyclic cystine knot structural motif.";
RL   J. Mol. Biol. 294:1327-1336(1999).
RN   [2]
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   [3]
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).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=12482868; DOI=10.1074/jbc.m211147200;
RA   Rosengren K.J., Daly N.L., Plan M.R.R., Waine C., Craik D.J.;
RT   "Twists, knots, and rings in proteins. Structural definition of the
RT   cyclotide framework.";
RL   J. Biol. Chem. 278:8606-8616(2003).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, petals, petioles and roots but
CC       not in runners (at protein level). {ECO:0000269|PubMed:28621949}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- PTM: This is a cyclic peptide.
CC   -!- MASS SPECTROMETRY: Mass=3114.4; 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:0000305}.
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DR   PDB; 1DF6; NMR; -; A=7-30.
DR   PDB; 1NBJ; NMR; -; A=4-30.
DR   PDBsum; 1DF6; -.
DR   PDBsum; 1NBJ; -.
DR   AlphaFoldDB; P82230; -.
DR   SMR; P82230; -.
DR   EvolutionaryTrace; P82230; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Knottin;
KW   Plant defense.
FT   PEPTIDE         1..30
FT                   /note="Cycloviolacin-O1"
FT                   /id="PRO_0000043609"
FT   DISULFID        4..21
FT   DISULFID        8..23
FT   DISULFID        13..28
FT   CROSSLNK        1..30
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:1DF6"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:1DF6"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1DF6"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1DF6"
SQ   SEQUENCE   30 AA;  3141 MW;  B6F6DAD5755B8937 CRC64;
     GIPCAESCVY IPCTVTALLG CSCSNRVCYN