ID   CYO13_VIOOD             Reviewed;         115 AA.
AC   Q5USN8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Cycloviolacin-O13;
DE   AltName: Full=Cyclotide c3;
DE   Flags: Precursor;
GN   Name=Voc3 {ECO:0000303|PubMed:15328347};
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:0000312|EMBL:AAU04394.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf {ECO:0000312|EMBL:AAU04394.1};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 82-111, FUNCTION, 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).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC       hemolytic activity. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:16872274, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, petals, petioles, roots and
CC       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       {ECO:0000250|UniProtKB:P56871}.
CC   -!- PTM: Cycloviolacin-O13 is a cyclic peptide.
CC       {ECO:0000269|PubMed:16872274}.
CC   -!- MASS SPECTROMETRY: Mass=3122.4; 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; AY630565; AAU04394.1; -; mRNA.
DR   AlphaFoldDB; Q5USN8; -.
DR   SMR; Q5USN8; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   SUPFAM; SSF57038; SSF57038; 1.
DR   PROSITE; PS51052; CYCLOTIDE; 1.
DR   PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis; Knottin;
KW   Plant defense; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..81
FT                   /evidence="ECO:0000269|PubMed:16872274"
FT                   /id="PRO_0000294940"
FT   PEPTIDE         82..111
FT                   /note="Cycloviolacin-O13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:16872274"
FT                   /id="PRO_0000294941"
FT   PROPEP          112..115
FT                   /evidence="ECO:0000269|PubMed:16872274"
FT                   /id="PRO_0000294942"
FT   DISULFID        85..101
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        89..103
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        94..108
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        82..111
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:16872274"
SQ   SEQUENCE   115 AA;  12439 MW;  B39034B436C7F705 CRC64;
     MDAKKMFVAL VLIATFALPS LATFEKDFIT PETIQAILKK SAPLSNIMLE EDVINALLKS
     KTVISNPIIE EAFLKNSNGL NGIPCGESCV WIPCISAAIG CSCKSKVCYR NSLDN