ID   CYCN_CLITE              Reviewed;          29 AA.
AC   P86900;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Cyclotide cter-N {ECO:0000303|PubMed:21593408};
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   PROTEIN SEQUENCE, CYCLIZATION, AND MASS SPECTROMETRY.
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.
CC       {ECO:0000250|UniProtKB:P86899, ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86899}.
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:21593408}.
CC   -!- MASS SPECTROMETRY: Mass=2934.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21593408};
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 cyclotide cter-M for which the DNA sequence is known.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P86900; -.
DR   SMR; P86900; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Oxidation;
KW   Plant defense; Secreted.
FT   PEPTIDE         1..29
FT                   /note="Cyclotide cter-N"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21593408"
FT                   /id="PRO_0000412639"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000250|UniProtKB:P86899,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P86899,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000250|UniProtKB:P86899,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..29
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:21593408"
SQ   SEQUENCE   29 AA;  2960 MW;  292E8BC4107DB637 CRC64;
     GSAFCGETCV LGTCYTPDCS CTALVCLKN