CYC1_CLITE
ID CYC1_CLITE Reviewed; 95 AA.
AC G1CWH0;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Cliotide T1 {ECO:0000303|PubMed:21596752};
DE Flags: Precursor; Fragment;
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:0000312|EMBL:AEK26402.1};
RN [1] {ECO:0000312|EMBL:AEK26402.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-95, PROTEIN SEQUENCE OF 1-30, FUNCTION,
RP PRESENCE OF DISULFIDE BONDS, CYCLIZATION, TISSUE SPECIFICITY, MASS
RP 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 (Probable). Active against Gram-negative bacteria E.coli ATCC 700926
CC (MIC=1.1 uM), K.pneumoniae ATTC 13883 (MIC=2.7 uM) and P.aeruginosa
CC ATCC 39018 (MIC=4.7 uM) (PubMed:21596752). Has hemolytic and cytotoxic
CC activity (PubMed:21596752). {ECO:0000255, ECO:0000255|PROSITE-
CC ProRule:PRU00395, ECO:0000269|PubMed:21596752}.
CC -!- TISSUE SPECIFICITY: Expressed in flower, stem, shoot, root, leaf, seed,
CC pod and nodule (at protein level). {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=3083; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21596752};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR EMBL; JF931988; AEK26402.1; -; mRNA.
DR AlphaFoldDB; G1CWH0; -.
DR SMR; G1CWH0; -.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR032000; Albumin_I_a.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012323; Cyclotide_bracelet_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF16720; Albumin_I_a; 1.
DR Pfam; PF03784; Cyclotide; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Knottin; Plant defense.
FT PEPTIDE 1..30
FT /note="Cliotide T1"
FT /evidence="ECO:0000269|PubMed:21596752"
FT /id="PRO_0000440047"
FT PROPEP 31..95
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:21596752"
FT /id="PRO_0000440048"
FT DISULFID 4..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 8..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 13..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 1..30
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:21596752"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:21596752"
SQ SEQUENCE 95 AA; 10476 MW; BACBD0093C99733B CRC64;
GIPCGESCVF IPCITGAIGC SCKSKVCYRN HVIAAEAKTM DDHHLLCQSH EDCITKGTGN
FCAPFPDQDI KYGWCFRAES EGFMLKDHLK MSITN