ID   VITA_VIOBI              Reviewed;         103 AA.
AC   B1NRR3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Cyclotide vitri-A;
DE   AltName: Full=Vbc6;
DE   Flags: Precursor; Fragment;
OS   Viola biflora (Yellow wood violet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=214529;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABW08095.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000269|PubMed:18191970};
RX   PubMed=18191970; DOI=10.1016/j.phytochem.2007.10.023;
RA   Herrmann A., Burman R., Mylne J.S., Karlsson G., Gullbo J., Craik D.J.,
RA   Clark R.J., Goeransson U.;
RT   "The alpine violet, Viola biflora, is a rich source of cyclotides with
RT   potent cytotoxicity.";
RL   Phytochemistry 69:939-952(2008).
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:P56871}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3154; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18191970};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; EU046623; ABW08095.1; -; mRNA.
DR   AlphaFoldDB; B1NRR3; -.
DR   SMR; B1NRR3; -.
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   SUPFAM; SSF57038; SSF57038; 1.
DR   PROSITE; PS51052; CYCLOTIDE; 1.
DR   PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Knottin; Plant defense; Signal.
FT   SIGNAL          <1..9
FT                   /evidence="ECO:0000250|UniProtKB:Q5USN8"
FT   PROPEP          10..69
FT                   /evidence="ECO:0000250|UniProtKB:Q5USN8"
FT                   /id="PRO_0000341445"
FT   PEPTIDE         70..99
FT                   /note="Cyclotide vitri-A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT                   /id="PRO_0000341446"
FT   PROPEP          100..103
FT                   /evidence="ECO:0000250|UniProtKB:Q5USN8"
FT                   /id="PRO_0000341447"
FT   DISULFID        73..89
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        77..91
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        82..96
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        70..99
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5USN8"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABW08095.1"
SQ   SEQUENCE   103 AA;  10921 MW;  559C1FFDD29B0695 CRC64;
     AAFALPAFAS FEKDVITPAA LEAVLNRKAP LSNIMMENDA IVNVIANVKT VISNPVLEEA
     LLKTNHGVNG IPCGESCVWI PCITSAIGCS CKSKVCYRNS LDN