ID   CYO8_VIOOD              Reviewed;         118 AA.
AC   P58440; Q5USN9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Cycloviolacin-O8;
DE   AltName: Full=Cyclotide c1;
DE   Flags: Precursor;
GN   Name=Voc1;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=15328347; DOI=10.1074/jbc.m407421200;
RA   Dutton J.L., Renda R.F., Waine C., Clark R.J., Daly N.L., Jennings C.V.,
RA   Anderson M.A., Craik D.J.;
RT   "Conserved structural and sequence elements implicated in the processing of
RT   gene-encoded circular proteins.";
RL   J. Biol. Chem. 279:46858-46867(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 85-115.
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   [3]
RP   PROTEIN SEQUENCE OF 85-115, 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   [4]
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   -!- 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: Cycloviolacin-O8 is a cyclic peptide.
CC   -!- MASS SPECTROMETRY: Mass=3225.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16872274};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; AY630564; AAU04393.1; -; mRNA.
DR   AlphaFoldDB; P58440; -.
DR   SMR; P58440; -.
DR   TCDB; 1.A.118.1.2; the plant cycltide (cyclotide) family.
DR   GO; GO:0006952; P:defense response; ISS:UniProtKB.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012323; Cyclotide_bracelet_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..84
FT                   /id="PRO_0000294936"
FT   PEPTIDE         85..115
FT                   /note="Cycloviolacin-O8"
FT                   /id="PRO_0000043615"
FT   PROPEP          116..118
FT                   /id="PRO_0000294937"
FT   DISULFID        89..105
FT   DISULFID        93..107
FT   DISULFID        98..112
FT   CROSSLNK        85..115
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   CONFLICT        90
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   118 AA;  12477 MW;  C6413100F4BA5A70 CRC64;
     MEMKNMVVGL FLIAAFALPA LATNFEKDFI THETVQAILK KVGPSSNGML DEQTISALTG
     KTIISNPVLE EALLTHSNSI NALGGTLPCG ESCVWIPCIS SVVGCSCKSK VCYKNSLA