ID   CYVA_VIOCT              Reviewed;          31 AA.
AC   P84635;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Cyclotide vico-A;
OS   Viola cotyledon (Violeta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=341256;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RX   PubMed=12782038; DOI=10.1016/s0003-2697(03)00114-3;
RA   Goransson U., Broussalis A.M., Claeson P.;
RT   "Expression of Viola cyclotides by liquid chromatography-mass spectrometry
RT   and tandem mass spectrometry sequencing of intercysteine loops after
RT   introduction of charges and cleavage sites by aminoethylation.";
RL   Anal. Biochem. 318:107-117(2003).
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:12782038}.
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}.
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DR   AlphaFoldDB; P84635; -.
DR   SMR; P84635; -.
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..31
FT                   /note="Cyclotide vico-A"
FT                   /id="PRO_0000044699"
FT   DISULFID        5..21
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..28
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..31
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:12782038"
SQ   SEQUENCE   31 AA;  3295 MW;  9B437A34EAFAD577 CRC64;
     GSIPCAESCV YIPCFTGIAG CSCKNKVCYY N