CYC3_CLITE
ID CYC3_CLITE Reviewed; 127 AA.
AC C0HKG1;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Cliotide T3 {ECO:0000303|PubMed:21596752};
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:0000303|PubMed:21596752};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-53, 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). Not active against Gram-negative bacteria E.coli ATCC
CC 700926, K.pneumoniae ATTC 13883 and P.aeruginosa ATCC 39018 at
CC concentration up to 100 uM (PubMed:21596752). Has cytotoxic and
CC hemolytic activity (PubMed:21596752). {ECO:0000255|PROSITE-
CC ProRule:PRU00395, ECO:0000269|PubMed:21596752}.
CC -!- TISSUE SPECIFICITY: Expressed in flower, stem, shoot, leaf and seed but
CC not in root, pod and nodule (at protein level).
CC {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=3057; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21596752};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR AlphaFoldDB; C0HKG1; -.
DR SMR; C0HKG1; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR032000; Albumin_I_a.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012324; Cyclotide_moebius_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF16720; Albumin_I_a; 1.
DR Pfam; PF03784; Cyclotide; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:21596752"
FT PEPTIDE 25..53
FT /note="Cliotide T3"
FT /evidence="ECO:0000269|PubMed:21596752"
FT /id="PRO_0000440051"
FT PROPEP 54..127
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:21596752"
FT /id="PRO_0000440052"
FT DISULFID 29..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 33..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 38..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 25..53
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:21596752"
SQ SEQUENCE 127 AA; 14078 MW; F8A4C74D2270F02C CRC64;
MAYVRLTSLA VLFFLAASVM KTEGGLPTCG ETCTLGTCYV PDCSCSWPIC MKNHIIAANA
KTVNEHRLLC TSHEDCFKKG TGNYCASFPD SNIHFGWCFH AESEGYLLKD FMNMSKDDLK
MPLESTN