ID   CYPLE_PSYLE             Reviewed;          30 AA.
AC   C0HL31;
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 psyleio E {ECO:0000303|PubMed:28006906};
OS   Psychotria leiocarpa.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Psychotrieae;
OC   Psychotria.
OX   NCBI_TaxID=2022332;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND CYCLIZATION.
RC   TISSUE=Leaf {ECO:0000303|PubMed:28006906};
RX   PubMed=28006906; DOI=10.1021/acs.jnatprod.6b00492;
RA   Matsuura H.N., Poth A.G., Yendo A.C., Fett-Neto A.G., Craik D.J.;
RT   "Isolation and Characterization of Cyclotides from Brazilian Psychotria:
RT   Significance in Plant Defense and Co-occurrence with Antioxidant
RT   Alkaloids.";
RL   J. Nat. Prod. 79:3006-3013(2016).
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:28006906}.
CC   -!- MASS SPECTROMETRY: Mass=3392.28; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28006906};
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:0000255|PROSITE-ProRule:PRU00395}.
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DR   AlphaFoldDB; C0HL31; -.
DR   SMR; C0HL31; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012324; Cyclotide_moebius_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 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..30
FT                   /note="Cyclotide psyleio E"
FT                   /evidence="ECO:0000269|PubMed:28006906"
FT                   /id="PRO_0000441796"
FT   DISULFID        7..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        11..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        16..28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..30
FT                   /note="Cyclopeptide (Ser-Lys)"
FT                   /evidence="ECO:0000305|PubMed:28006906"
FT   UNSURE          5
FT                   /note="I or L"
FT                   /evidence="ECO:0000303|PubMed:28006906"
FT   UNSURE          27
FT                   /note="I or L"
FT                   /evidence="ECO:0000303|PubMed:28006906"
SQ   SEQUENCE   30 AA;  3053 MW;  2F987FC0ACEA1B0A CRC64;
     SVTPIVCGET CFGGTCNTPG CSCSWPICTK