ID   CYH3_VIOHE              Reviewed;          30 AA.
AC   P85232;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Cycloviolacin-H3;
OS   Viola hederacea (Australian violet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=180952;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000269|PubMed:15824119};
RX   PubMed=15824119; DOI=10.1074/jbc.m501737200;
RA   Chen B., Colgrave M.L., Daly N.L., Rosengren K.J., Gustafson K.R.,
RA   Craik D.J.;
RT   "Isolation and characterization of novel cyclotides from Viola hederaceae:
RT   solution structure and anti-HIV activity of vhl-1, a leaf-specific
RT   expressed cyclotide.";
RL   J. Biol. Chem. 280:22395-22405(2005).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P56254}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:15824119}.
CC   -!- MASS SPECTROMETRY: Mass=3075.28; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15824119};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius 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   AlphaFoldDB; P85232; -.
DR   SMR; P85232; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012324; Cyclotide_moebius_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; PS60009; CYCLOTIDE_MOEBIUS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT   PEPTIDE         1..30
FT                   /note="Cycloviolacin-H3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:15824119"
FT                   /id="PRO_0000302127"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000250|UniProtKB:P56254,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P56254,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..27
FT                   /evidence="ECO:0000250|UniProtKB:P56254,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..30
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:15824119"
SQ   SEQUENCE   30 AA;  3102 MW;  7B0971FDFFFD26EE CRC64;
     GLPVCGETCF GGTCNTPGCI CDPWPVCTRN