ID   CYH2_VIOHE              Reviewed;          29 AA.
AC   P85233;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Cycloviolacin-H2;
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.
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:P56879}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:15824119}.
CC   -!- MASS SPECTROMETRY: Mass=3116.70; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15824119};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85233; -.
DR   SMR; P85233; -.
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..29
FT                   /note="Cycloviolacin-H2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:15824119"
FT                   /id="PRO_0000302126"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..29
FT                   /note="Cyclopeptide (Ser-Asn)"
FT                   /evidence="ECO:0000269|PubMed:15824119"
SQ   SEQUENCE   29 AA;  3143 MW;  C04A24F2D302FA51 CRC64;
     SAIACGESCV YIPCFIPGCS CRNRVCYLN