CYML3_MELLF
ID CYML3_MELLF Reviewed; 29 AA.
AC C0HK30;
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 mela-3 {ECO:0000303|PubMed:26322745};
OS Melicytus latifolius (Norfolk Island mahoe) (Hymenanthera latifolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Melicytus.
OX NCBI_TaxID=212268 {ECO:0000303|PubMed:26322745};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND PRESENCE OF DISULFIDE BONDS.
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 (PubMed:26322745). Not active against Gram-negative
CC bacterium E.coli ATCC 25922 or Gram-positive bacterium S.aureus ATCC
CC 25923 up to a concentration of 64 uM (PubMed:26322745).
CC {ECO:0000255|PROSITE-ProRule:PRU00395, 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 -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:26322745}.
CC -!- MASS SPECTROMETRY: Mass=3105.33; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:26322745};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebuis subfamily.
CC {ECO:0000303|PubMed:26322745}.
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; C0HK30; -.
DR SMR; C0HK30; -.
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; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 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 mela-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:26322745"
FT /id="PRO_0000437509"
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; 3132 MW; 2AAB613DAA65E0B3 CRC64;
GKPICGETCF KGKCYTPGCT CSYPICKKD