ID   CYCB_CLITE              Reviewed;         135 AA.
AC   P86842; A0A0K2E303; G1CWI0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 3.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Cyclotide cter-B {ECO:0000303|PubMed:21194241};
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:0000312|EMBL:AEK26412.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-60, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, CYCLIZATION, AND
RP   PRESENCE OF DISULFIDE BONDS.
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).
RN   [2] {ECO:0000312|EMBL:ALA27393.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mushtaq Z., Jamil A.;
RT   "isolation and sequence analysis of cliotide (cyclotide) gene from genomic
RT   DNA of local clitoria plant.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 30-60, PRESENCE OF DISULFIDE BONDS, CYCLIZATION, AND
RP   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:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- TISSUE SPECIFICITY: Expressed in root, seed and nodule but not in
CC       flower, stem, shoot, leaf and pod. {ECO:0000269|PubMed:21596752}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000305|PubMed:21596752}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:21194241,
CC       ECO:0000269|PubMed:21596752}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:21194241, ECO:0000269|PubMed:21596752}.
CC   -!- MASS SPECTROMETRY: Mass=3250.75; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21194241};
CC   -!- MASS SPECTROMETRY: Mass=3250; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21596752};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JF931998; AEK26412.1; -; mRNA.
DR   EMBL; KP889219; ALA27393.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86842; -.
DR   GO; GO:0006952; P:defense response; 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   Direct protein sequencing; Disulfide bond; Knottin; Plant defense; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         30..60
FT                   /note="Cyclotide cter-B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21194241, ECO:0000269|PubMed:21596752"
FT                   /id="PRO_0000405853"
FT   PROPEP          61..135
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:21596752"
FT                   /id="PRO_0000440093"
FT   DISULFID        33..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        37..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        42..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        30..60
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:21596752"
FT   CONFLICT        65
FT                   /note="F -> S (in Ref. 2; ALA27393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="F -> L (in Ref. 2; ALA27393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="F -> S (in Ref. 2; ALA27393)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   135 AA;  15268 MW;  318AC9C0A1004238 CRC64;
     MGTIARYYAH VVLFLVATSV IFTVKKTEAG VPCAESCVWI PCTVTALLGC SCKDKVCYLN
     HVIAFEAKTM DEHHLLCQSH EDCYKKGSGN FCAPFFNHDV KYGWCFRAEF EGYLLKDFLK
     MQPRDILKIS KAIAK