ID   VODM_VIOOD              Reviewed;          29 AA.
AC   P83839;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Vodo peptide M;
OS   Viola odorata (Sweet violet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=97441;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND 3D-STRUCTURE MODELING.
RX   PubMed=12946412; DOI=10.1016/s0031-9422(03)00218-8;
RA   Svangard E., Goransson U., Smith D., Verma C., Backlund A., Bohlin L.,
RA   Claeson P.;
RT   "Primary and 3-D modelled structures of two cyclotides from Viola
RT   odorata.";
RL   Phytochemistry 64:135-142(2003).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=16872274; DOI=10.1042/bj20060627;
RA   Ireland D.C., Colgrave M.L., Craik D.J.;
RT   "A novel suite of cyclotides from Viola odorata: sequence variation and the
RT   implications for structure, function and stability.";
RL   Biochem. J. 400:1-12(2006).
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=3077; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12946412};
CC   -!- MASS SPECTROMETRY: Mass=3075.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16872274};
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   AlphaFoldDB; P83839; -.
DR   SMR; P83839; -.
DR   GO; GO:0006952; P:defense response; ISS: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   Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT   PEPTIDE         1..29
FT                   /note="Vodo peptide M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:12946412"
FT                   /id="PRO_0000043620"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000250|UniProtKB:P56871,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..29
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:12946412,
FT                   ECO:0000269|PubMed:16872274"
SQ   SEQUENCE   29 AA;  3102 MW;  245A8ED801C4E8C3 CRC64;
     GAPICGESCF TGKCYTVQCS CSWPVCTRN