ID   CYC13_CLITE             Reviewed;          31 AA.
AC   C0HJS0;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Cliotide T13 {ECO:0000303|PubMed:27007913};
DE   AltName: Full=Cyclotide cT13 {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, FUNCTION, TISSUE SPECIFICITY, CYCLIZATION, PRESENCE OF
RP   DISULFIDE BONDS, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP   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. Not
CC       active against Gram-negative bacterium E.coli ATCC 700926 or Gram-
CC       positive bacterium S.aureus ATCC 12600 up to a concentration of 100 uM
CC       under low-salt conditions (PubMed:27007913). {ECO:0000255|PROSITE-
CC       ProRule:PRU00395, ECO:0000269|PubMed:27007913}.
CC   -!- TISSUE SPECIFICITY: Expressed in seed but not in root nodules.
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=3299.332; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27007913};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000303|PubMed:27007913}.
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DR   AlphaFoldDB; C0HJS0; -.
DR   SMR; C0HJS0; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012323; Cyclotide_bracelet_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; PS60008; CYCLOTIDE_BRACELET; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT   PEPTIDE         1..31
FT                   /note="Cliotide T13"
FT                   /evidence="ECO:0000269|PubMed:27007913"
FT                   /id="PRO_0000436311"
FT   DISULFID        5..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..31
FT                   /note="Cyclopeptide (Asp-Asn)"
FT                   /evidence="ECO:0000269|PubMed:27007913"
SQ   SEQUENCE   31 AA;  3325 MW;  8B7F9A52EEA7DA67 CRC64;
     DTTPCGESCV WIPCVSSIVG CSCQNKVCYQ N