ID   CYMR1_MELRA             Reviewed;          29 AA.
AC   C0HL32;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Cyclotide mra1 {ECO:0000303|PubMed:19462049};
OS   Melicytus ramiflorus (Whitey wood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Melicytus.
OX   NCBI_TaxID=316498 {ECO:0000303|PubMed:19462049};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PRESENCE OF DISULFIDE BONDS.
RC   TISSUE=Leaf {ECO:0000303|PubMed:19462049};
RX   PubMed=19462049; DOI=10.1039/b823020j;
RA   Trabi M., Mylne J.S., Sando L., Craik D.J.;
RT   "Circular proteins from Melicytus (Violaceae) refine the conserved protein
RT   and gene architecture of cyclotides.";
RL   Org. Biomol. Chem. 7:2378-2388(2009).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:19462049}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:19462049}.
CC   -!- MASS SPECTROMETRY: Mass=3091; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19462049};
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 cyclotide mra4 for which the DNA sequence is known.
CC       {ECO:0000305|PubMed:19462049}.
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DR   AlphaFoldDB; C0HL32; -.
DR   SMR; C0HL32; -.
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..29
FT                   /note="Cyclotide mra1"
FT                   /evidence="ECO:0000269|PubMed:19462049"
FT                   /id="PRO_0000441829"
FT   DISULFID        4..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        8..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        13..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
SQ   SEQUENCE   29 AA;  3099 MW;  AD4124051031750F CRC64;
     GIPCAESCVY IPCLTSIGCS CKSKVCYRN