ID   VARF_VIOAR              Reviewed;          29 AA.
AC   P58451;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Varv peptide F;
OS   Viola arvensis (European field pansy) (Field violet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=97415;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=10075760; DOI=10.1021/np9803878;
RA   Goeransson U., Luijendijk T., Johansson S., Bohlin L., Claeson P.;
RT   "Seven novel macrocyclic polypeptides from Viola arvensis.";
RL   J. Nat. Prod. 62:283-286(1999).
RN   [2]
RP   FUNCTION.
RX   PubMed=12477048;
RA   Lindholm P., Goransson U., Johansson S., Claeson P., Gullbo J., Larsson R.,
RA   Bohlin L., Backlund A.;
RT   "Cyclotides: a novel type of cytotoxic agents.";
RL   Mol. Cancer Ther. 1:365-369(2002).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC       cytotoxic activity against a variety of drug-resistant and drug-
CC       sensitive human tumor cell lines. {ECO:0000255|PROSITE-
CC       ProRule:PRU00395, ECO:0000269|PubMed:12477048}.
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.
CC   -!- MASS SPECTROMETRY: Mass=2856; Mass_error=3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10075760};
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   PDB; 2K7G; NMR; -; A=1-29.
DR   PDB; 3E4H; X-ray; 1.80 A; A=5-29.
DR   PDBsum; 2K7G; -.
DR   PDBsum; 3E4H; -.
DR   AlphaFoldDB; P58451; -.
DR   SMR; P58451; -.
DR   EvolutionaryTrace; P58451; -.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
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   3D-structure; Direct protein sequencing; Disulfide bond; Knottin;
KW   Plant defense.
FT   PEPTIDE         1..29
FT                   /note="Varv peptide F"
FT                   /id="PRO_0000043626"
FT   DISULFID        5..19
FT   DISULFID        9..21
FT   DISULFID        14..26
FT   CROSSLNK        1..29
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:2K7G"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:2K7G"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:3E4H"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:3E4H"
SQ   SEQUENCE   29 AA;  2983 MW;  32364DAF2DCDE893 CRC64;
     GVPICGETCT LGTCYTAGCS CSWPVCTRN