ID   CYC11_CLITE             Reviewed;          31 AA.
AC   C0HKG3;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Cliotide T11 {ECO:0000303|PubMed:21596752};
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:21596752};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, PRESENCE OF DISULFIDE BONDS, CYCLIZATION, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21596752; DOI=10.1074/jbc.m111.229922;
RA   Nguyen G.K., Zhang S., Nguyen N.T., Nguyen P.Q., Chiu M.S., Hardjojo A.,
RA   Tam J.P.;
RT   "Discovery and characterization of novel cyclotides originated from
RT   chimeric precursors consisting of albumin-1 chain a and cyclotide domains
RT   in the fabaceae family.";
RL   J. Biol. Chem. 286:24275-24287(2011).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- TISSUE SPECIFICITY: Expressed in seed but not in root, nodule, flower,
CC       stem, shoot, leaf and pod (at protein level).
CC       {ECO:0000269|PubMed:21596752}.
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:21596752}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:21596752}.
CC   -!- MASS SPECTROMETRY: Mass=3240; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21596752};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC       similarity to cliotide T1 for which the DNA sequence is known.
CC       {ECO:0000305|PubMed:21596752}.
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DR   AlphaFoldDB; C0HKG3; -.
DR   SMR; C0HKG3; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT   PEPTIDE         1..31
FT                   /note="Cliotide T11"
FT                   /evidence="ECO:0000269|PubMed:21596752"
FT                   /id="PRO_0000440065"
FT   DISULFID        4..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        8..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        13..28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..31
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000303|PubMed:21596752"
SQ   SEQUENCE   31 AA;  3267 MW;  83ED50BAB37409AF CRC64;
     GIPCGESCVF IPCTITALLG CSCKDKVCYK N