CYCQ_CLITE
ID CYCQ_CLITE Reviewed; 30 AA.
AC P86904;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Cyclotide cter-Q {ECO:0000303|PubMed:21593408};
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, CYCLIZATION, AND MASS SPECTROMETRY.
RC TISSUE=Leaf {ECO:0000269|PubMed:21593408};
RX PubMed=21593408; DOI=10.1073/pnas.1103660108;
RA Poth A.G., Colgrave M.L., Lyons R.E., Daly N.L., Craik D.J.;
RT "Discovery of an unusual biosynthetic origin for circular proteins in
RT legumes.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10127-10132(2011).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC {ECO:0000250|UniProtKB:P86899, ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86899}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:21593408}.
CC -!- MASS SPECTROMETRY: Mass=3168.47; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21593408};
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 cyclotide cter-A for which the DNA sequence is known.
CC {ECO:0000305}.
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DR AlphaFoldDB; P86904; -.
DR SMR; P86904; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Oxidation;
KW Plant defense; Secreted.
FT PEPTIDE 1..30
FT /note="Cyclotide cter-Q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:21593408"
FT /id="PRO_0000412642"
FT DISULFID 4..20
FT /evidence="ECO:0000250|UniProtKB:P86899,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 8..22
FT /evidence="ECO:0000250|UniProtKB:P86899,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 13..27
FT /evidence="ECO:0000250|UniProtKB:P86899,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 1..30
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:21593408"
SQ SEQUENCE 30 AA; 3195 MW; 19D19A52F6B3B3CE CRC64;
GIPCGESCVF IPCISTVIGC SCKNKVCYRN