ID   CYMC2_MELCT             Reviewed;          29 AA.
AC   C0HK36;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Cyclotide mech-2 {ECO:0000303|PubMed:26322745};
OS   Melicytus chathamicus (Chatham Island mahoe) (Hymenanthera latifolia var.
OS   chathamica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Melicytus.
OX   NCBI_TaxID=453349 {ECO:0000303|PubMed:26322745};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP   SPECTROMETRY, PRESENCE OF DISULFIDE BONDS, CYCLIZATION, AND STRUCTURE BY
RP   NMR.
RX   PubMed=26322745; DOI=10.1021/acschembio.5b00454;
RA   Ravipati A.S., Henriques S.T., Poth A.G., Kaas Q., Wang C.K.,
RA   Colgrave M.L., Craik D.J.;
RT   "Lysine-rich cyclotides: a new subclass of circular knotted proteins from
RT   Violaceae.";
RL   ACS Chem. Biol. 10:2491-2500(2015).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism
CC       (Potential). Binds to and induces leakage in phospholipd membranes,
CC       particularly ones containing 1-palmitoyl-2-oleophosphatidylethanolamine
CC       (POPE) (PubMed:26322745). In vitro, displays cytotoxicity against
CC       cultured cells but no hemolytic activity towards fresh erythrocytes
CC       (PubMed:26322745). {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:26322745}.
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:26322745}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:26322745}.
CC   -!- MASS SPECTROMETRY: Mass=3124.30; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:26322745};
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; C0HK36; -.
DR   SMR; C0HK36; -.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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   Cytolysis; Direct protein sequencing; Disulfide bond; Knottin;
KW   Plant defense.
FT   PEPTIDE         1..29
FT                   /note="Cyclotide mech-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:26322745"
FT                   /id="PRO_0000437515"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..29
FT                   /note="Cyclopeptide (Gly-Asp)"
FT                   /evidence="ECO:0000305|PubMed:26322745"
SQ   SEQUENCE   29 AA;  3151 MW;  B3B7AD86B7F2FA09 CRC64;
     GLPTCGETCT LGKCNTPKCT CNWPICYKD