ID   CYC4_CLITE              Reviewed;         123 AA.
AC   G1CWH3;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Cliotide T4;
DE   Flags: Precursor;
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:AEK26405.1};
RN   [1] {ECO:0000312|EMBL:AEK26405.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-58, FUNCTION, PRESENCE
RP   OF DISULFIDE BONDS, CYCLIZATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   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=1.0 uM), K.pneumoniae ATTC 13883 (MIC=5.5 uM) and P.aeruginosa
CC       ATCC 39018 (MIC=7.5 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=3097; 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; JF931991; AEK26405.1; -; mRNA.
DR   AlphaFoldDB; G1CWH3; -.
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; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:21596752"
FT   PEPTIDE         29..58
FT                   /note="Cliotide T4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21596752"
FT                   /id="PRO_0000440053"
FT   PROPEP          59..123
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:21596752"
FT                   /id="PRO_0000440054"
FT   DISULFID        32..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        36..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        41..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        29..58
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:21596752"
SQ   SEQUENCE   123 AA;  13530 MW;  B78CACCFB1516F4F CRC64;
     MASLRIAPLA LFFFLAASVM FTVEKTEAGI PCGESCVFIP CITAAIGCSC KSKVCYRNHV
     IAAEAKTMDD HHLLCQSHED CITKGTGNFC APFPDQDIKY GWCFRAESEG FLLKDHLKMS
     ITN