ID   CYCA_CLITE              Reviewed;         124 AA.
AC   P86841; G1CWH9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 2.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Cyclotide cter-A {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:21194241};
RN   [1] {ECO:0000312|EMBL:AEK26411.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-59, TISSUE SPECIFICITY,
RP   CYCLIZATION, MASS SPECTROMETRY, PRESENCE OF DISULFIDE BONDS, 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).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 29-59, 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 stem, shoot, root, leaf, seed, pod and
CC       nodule but not in flower (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.
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=3267; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21596752};
CC   -!- MASS SPECTROMETRY: Mass=3267.19; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21194241};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; JF931997; AEK26411.1; -; mRNA.
DR   AlphaFoldDB; P86841; -.
DR   SMR; P86841; -.
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..28
FT                   /evidence="ECO:0000269|PubMed:21194241,
FT                   ECO:0000269|PubMed:21596752"
FT   PEPTIDE         29..59
FT                   /note="Cyclotide cter-A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:21194241, ECO:0000269|PubMed:21596752"
FT                   /id="PRO_0000405852"
FT   PROPEP          60..124
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:21596752"
FT                   /id="PRO_0000440092"
FT   DISULFID        33..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        42..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        29..59
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:21596752"
SQ   SEQUENCE   124 AA;  13662 MW;  8BDEE9AF2AE86EE0 CRC64;
     MASLRIAPFA LFLFLAASVM FAVEKTEAGV IPCGESCVFI PCISTVIGCS CKNKVCYRNH
     IIAAEAKTMD EHILLCQSHE DCIAKGTGNF CAPFPDQDIK YGWCFRAESE GFMLKDHLKM
     SITN