CYCC_CLITE
ID CYCC_CLITE Reviewed; 31 AA.
AC P86843;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Cyclotide cter-C {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, DISULFIDE BONDS, CYCLIZATION, AND MASS 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).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC {ECO:0000250|UniProtKB:P56254, ECO:0000255|PROSITE-ProRule:PRU00395}.
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 -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:21194241}.
CC -!- MASS SPECTROMETRY: Mass=3251.76; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21194241};
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 cter-B for which the DNA sequence is known.
CC {ECO:0000305}.
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DR AlphaFoldDB; P86843; -.
DR SMR; P86843; -.
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="Cyclotide cter-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:21194241"
FT /id="PRO_0000405854"
FT DISULFID 4..21
FT /evidence="ECO:0000250|UniProtKB:P56254,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 8..23
FT /evidence="ECO:0000250|UniProtKB:P56254,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 13..28
FT /evidence="ECO:0000250|UniProtKB:P56254,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 1..31
FT /note="Cyclopeptide (Gly-Asp)"
FT /evidence="ECO:0000303|PubMed:21194241"
SQ SEQUENCE 31 AA; 3278 MW; 9B6596DAD5769430 CRC64;
GVPCAESCVW IPCTVTALLG CSCKDKVCYL D