ID   CYC17_CLITE             Reviewed;          31 AA.
AC   P86849; C0HJS4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 2.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Cliotide T17 {ECO:0000303|PubMed:27007913};
DE   AltName: Full=Cyclotide cT17 {ECO:0000303|PubMed:27007913};
DE   AltName: Full=Cyclotide cter-I {ECO:0000303|PubMed:21194241};
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, PRESENCE OF DISULFIDE BONDS, CYCLIZATION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:21194241};
RX   PubMed=21194241; DOI=10.1021/cb100388j;
RA   Poth A.G., Colgrave M.L., Philip R., Kerenga B., Daly N.L., Anderson M.,
RA   Craik D.J.;
RT   "The discovery of cyclotides in the Fabaceae plant family provides new
RT   insights into the cyclization, evolution and distribution of circular
RT   proteins.";
RL   ACS Chem. Biol. 6:345-355(2011).
RN   [2]
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:21194241,
CC       ECO:0000269|PubMed:27007913}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:21194241, ECO:0000269|PubMed:27007913}.
CC   -!- MASS SPECTROMETRY: Mass=3153.96; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21194241};
CC   -!- MASS SPECTROMETRY: Mass=3154.395; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27007913};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   AlphaFoldDB; P86849; -.
DR   SMR; P86849; -.
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 T17"
FT                   /evidence="ECO:0000269|PubMed:21194241,
FT                   ECO:0000269|PubMed:27007913"
FT                   /id="PRO_0000405860"
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 (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:27007913"
SQ   SEQUENCE   31 AA;  3181 MW;  9082BA52E2609A00 CRC64;
     GTVPCGESCV FIPCITGIAG CSCKNKVCYL N