ID   VHL1_VIOHE              Reviewed;          31 AA.
AC   P84522;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Leaf cyclotide 1;
DE   AltName: Full=Vhl-1;
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, FUNCTION, TISSUE SPECIFICITY, MASS SPECTROMETRY,
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
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. Has anti-
CC       human immunodeficiency virus activity. {ECO:0000269|PubMed:15824119,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:15824119}.
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. {ECO:0000269|PubMed:15824119}.
CC   -!- MASS SPECTROMETRY: Mass=3330.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15824119};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255}.
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; 1ZA8; NMR; -; A=4-31.
DR   PDBsum; 1ZA8; -.
DR   AlphaFoldDB; P84522; -.
DR   SMR; P84522; -.
DR   EvolutionaryTrace; P84522; -.
DR   GO; GO:0051607; P:defense response to virus; 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; PS60008; CYCLOTIDE_BRACELET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Direct protein sequencing; Disulfide bond;
KW   Knottin; Plant defense.
FT   PEPTIDE         1..31
FT                   /note="Leaf cyclotide 1"
FT                   /evidence="ECO:0000269|PubMed:15824119"
FT                   /id="PRO_0000044702"
FT   DISULFID        4..21
FT                   /evidence="ECO:0000269|PubMed:15824119"
FT   DISULFID        8..23
FT                   /evidence="ECO:0000269|PubMed:15824119"
FT   DISULFID        14..28
FT                   /evidence="ECO:0000269|PubMed:15824119"
FT   CROSSLNK        1..31
FT                   /note="Cyclopeptide (Ser-Asn)"
FT                   /evidence="ECO:0000269|PubMed:15824119"
FT   STRAND          9..12
FT                   /evidence="ECO:0007829|PDB:1ZA8"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:1ZA8"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:1ZA8"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1ZA8"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1ZA8"
SQ   SEQUENCE   31 AA;  3341 MW;  8EEA215E699578BD CRC64;
     SISCGESCAM ISFCFTEVIG CSCKNKVCYL N