ID   CYC18_CLITE             Reviewed;          29 AA.
AC   C0HJS5;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Cliotide T18 {ECO:0000303|PubMed:27007913};
DE   AltName: Full=Cyclotide cT18 {ECO:0000303|PubMed:27007913};
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 {ECO:0000303|PubMed:27007913};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, CYCLIZATION, PRESENCE OF DISULFIDE
RP   BONDS, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=27007913; DOI=10.1111/febs.13720;
RA   Nguyen K.N., Nguyen G.K., Nguyen P.Q., Ang K.H., Dedon P.C., Tam J.P.;
RT   "Immunostimulating and Gram-negative-specific antibacterial cyclotides from
RT   the butterfly pea Clitoria ternatea.";
RL   FEBS J. 283:2067-2090(2016).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- TISSUE SPECIFICITY: Expressed in root nodules but not in seed.
CC       {ECO:0000269|PubMed:27007913}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:27007913}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:27007913}.
CC   -!- MASS SPECTROMETRY: Mass=3021.238; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27007913};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; C0HJS5; -.
DR   SMR; C0HJS5; -.
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   PIRSF; PIRSF037891; Cycloviolacin; 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; Plant defense.
FT   PEPTIDE         1..29
FT                   /note="Cliotide T18"
FT                   /evidence="ECO:0000269|PubMed:27007913"
FT                   /id="PRO_0000436315"
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-Asn)"
FT                   /evidence="ECO:0000269|PubMed:27007913"
SQ   SEQUENCE   29 AA;  3048 MW;  3227A7561882E0B3 CRC64;
     GLPICGETCF TGTCYTPGCT CSYPVCKKN