ID   CYCM_CLITE              Reviewed;         127 AA.
AC   P86899;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Cyclotide cter-M {ECO:0000303|PubMed:21593408};
DE   Flags: Precursor;
OS   Clitoria ternatea (Butterfly pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Clitoria.
OX   NCBI_TaxID=43366;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-53, STRUCTURE BY NMR OF
RP   25-53, FUNCTION, SUBCELLULAR LOCATION, CYCLIZATION, MASS SPECTROMETRY,
RP   DISULFIDE BONDS, AND OXIDATION AT MET-51.
RC   TISSUE=Leaf {ECO:0000269|PubMed:21593408};
RX   PubMed=21593408; DOI=10.1073/pnas.1103660108;
RA   Poth A.G., Colgrave M.L., Lyons R.E., Daly N.L., Craik D.J.;
RT   "Discovery of an unusual biosynthetic origin for circular proteins in
RT   legumes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:10127-10132(2011).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Displays
CC       insecticidal activity against H.armigera. Has weak hemolytic activity.
CC       Binds to phospholipid membranes. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:21593408}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21593408}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:21593408}.
CC   -!- DOMAIN: Displays an unusual domain structure in comparison to other
CC       known cyclotides as the cyclotide is followed by a C-terminal albumin-
CC       like region. {ECO:0000269|PubMed:21593408}.
CC   -!- PTM: Cyclotide cter-M is a cyclic peptide.
CC       {ECO:0000269|PubMed:21593408}.
CC   -!- MASS SPECTROMETRY: Mass=3057.25; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21593408};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; JF501210; AEB92229.1; -; mRNA.
DR   PDB; 2LAM; NMR; -; A=25-53.
DR   PDBsum; 2LAM; -.
DR   AlphaFoldDB; P86899; -.
DR   BMRB; P86899; -.
DR   SMR; P86899; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR032000; Albumin_I_a.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012324; Cyclotide_moebius_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF16720; Albumin_I_a; 1.
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   3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Hemolysis; Knottin; Oxidation; Plant defense; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:21593408"
FT   PEPTIDE         25..53
FT                   /note="Cyclotide cter-M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21593408"
FT                   /id="PRO_0000412637"
FT   PROPEP          54..127
FT                   /evidence="ECO:0000269|PubMed:21593408"
FT                   /id="PRO_0000412638"
FT   MOD_RES         51
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:21593408"
FT   DISULFID        29..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21593408"
FT   DISULFID        33..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21593408"
FT   DISULFID        38..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21593408"
FT   CROSSLNK        25..53
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:21593408"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:2LAM"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2LAM"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:2LAM"
SQ   SEQUENCE   127 AA;  14078 MW;  F8A4C74D2270F02C CRC64;
     MAYVRLTSLA VLFFLAASVM KTEGGLPTCG ETCTLGTCYV PDCSCSWPIC MKNHIIAANA
     KTVNEHRLLC TSHEDCFKKG TGNYCASFPD SNIHFGWCFH AESEGYLLKD FMNMSKDDLK
     MPLESTN