ID   VIOLA_VIOOD             Reviewed;         106 AA.
AC   Q2HY54;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Violacin-A;
DE   AltName: Full=Violacin-1;
DE   Flags: Precursor;
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, ECO:0000312|EMBL:ABC94585.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 80-106, FUNCTION, MASS
RP   SPECTROMETRY, DISULFIDE BONDS, AND STRUCTURE BY NMR.
RX   PubMed=16488428; DOI=10.1016/j.jmb.2006.01.051;
RA   Ireland D.C., Colgrave M.L., Nguyencong P., Daly N.L., Craik D.J.;
RT   "Discovery and characterization of a linear cyclotide from Viola odorata:
RT   implications for the processing of circular proteins.";
RL   J. Mol. Biol. 357:1522-1535(2006).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 80-106, 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. Has low
CC       hemolytic activity. {ECO:0000269|PubMed:16488428, ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:16488428}.
CC   -!- PTM: Violacin-A is not a cyclic peptide. {ECO:0000269|PubMed:16488428,
CC       ECO:0000269|PubMed:16872274}.
CC   -!- MASS SPECTROMETRY: Mass=3004.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16488428};
CC   -!- MASS SPECTROMETRY: Mass=3004.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16872274};
CC   -!- MISCELLANEOUS: The presence of a premature stop codon inhibits the
CC       translation of a key Asn residue that is thought to be required for
CC       cyclization.
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255}.
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DR   EMBL; DQ365813; ABC94585.1; -; mRNA.
DR   PDB; 2FQA; NMR; -; A=80-106.
DR   PDBsum; 2FQA; -.
DR   AlphaFoldDB; Q2HY54; -.
DR   EvolutionaryTrace; Q2HY54; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   SUPFAM; SSF57038; SSF57038; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Hemolysis; Knottin; Plant defense; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..79
FT                   /evidence="ECO:0000269|PubMed:16488428,
FT                   ECO:0000269|PubMed:16872274"
FT                   /id="PRO_0000294965"
FT   PEPTIDE         80..106
FT                   /note="Violacin-A"
FT                   /evidence="ECO:0000269|PubMed:16488428"
FT                   /id="PRO_0000294966"
FT   DISULFID        84..98
FT                   /evidence="ECO:0000269|PubMed:16488428"
FT   DISULFID        88..100
FT                   /evidence="ECO:0000269|PubMed:16488428"
FT   DISULFID        93..105
FT                   /evidence="ECO:0000269|PubMed:16488428"
SQ   SEQUENCE   106 AA;  11589 MW;  A44C6D66F24B7115 CRC64;
     MDAQKMKMVI GLVLVATTAF ALMIPAASAV DDFITRRAYD NLVKSGAIKD IPVMAKTIIS
     NPVLEEGMLT YYTNKKLGDS AISCGETCFK FKCYTPRCSC SYPVCK