ID   CYCA_PETHY              Reviewed;          79 AA.
AC   B3EWH5;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Cyclotide phyb-A {ECO:0000303|PubMed:22700981};
DE   Flags: Precursor;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower {ECO:0000269|Ref.1};
RX   DOI=10.1016/j.plantsci.2007.07.011;
RA   Shimamura K., Ishimizu T., Nishimura K., Matsubara K., Kodama H.,
RA   Watanabe H., Hase S., Ando T.;
RT   "Analysis of expressed sequence tags from Petunia flowers.";
RL   Plant Sci. 173:495-500(2007).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 12-79.
RC   TISSUE=Root {ECO:0000269|PubMed:21143680};
RX   PubMed=21143680; DOI=10.1111/j.1365-313x.2010.04385.x;
RA   Breuillin F., Schramm J., Hajirezaei M., Ahkami A., Favre P., Druege U.,
RA   Hause B., Bucher M., Kretzschmar T., Bossolini E., Kuhlemeier C.,
RA   Martinoia E., Franken P., Scholz U., Reinhardt D.;
RT   "Phosphate systemically inhibits development of arbuscular mycorrhiza in
RT   Petunia hybrida and represses genes involved in mycorrhizal functioning.";
RL   Plant J. 64:1002-1017(2010).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 44-73, TISSUE SPECIFICITY, DOMAIN, DISULFIDE BONDS,
RP   CYCLIZATION, AND MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000269|PubMed:22700981};
RX   PubMed=22700981; DOI=10.1074/jbc.m112.370841;
RA   Poth A.G., Mylne J.S., Grassl J., Lyons R.E., Millar A.H., Colgrave M.L.,
RA   Craik D.J.;
RT   "Cyclotides associate with leaf vasculature and are the products of a novel
RT   precursor in Petunia (Solanaceae).";
RL   J. Biol. Chem. 287:27033-27046(2012).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000250|UniProtKB:P56254, ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- TISSUE SPECIFICITY: Expressed in midvein, lamina and periphery of
CC       leaves (at protein level). {ECO:0000269|PubMed:22700981}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:22700981}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:22700981}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:22700981}.
CC   -!- MASS SPECTROMETRY: Mass=3068.29; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22700981};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; DC242826; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FN035504; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWH5; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012323; Cyclotide_bracelet_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
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.
FT   PROPEP          1..43
FT                   /evidence="ECO:0000269|PubMed:22700981"
FT                   /id="PRO_0000419342"
FT   PEPTIDE         44..73
FT                   /note="Cyclotide phyb-A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:22700981"
FT                   /id="PRO_0000419343"
FT   PROPEP          74..79
FT                   /evidence="ECO:0000269|PubMed:22700981"
FT                   /id="PRO_0000419344"
FT   DISULFID        47..63
FT                   /evidence="ECO:0000250|UniProtKB:P56254,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        51..65
FT                   /evidence="ECO:0000250|UniProtKB:P56254,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        56..70
FT                   /evidence="ECO:0000250|UniProtKB:P56254,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        44..73
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:22700981"
SQ   SEQUENCE   79 AA;  8575 MW;  A87780D3F04DA664 CRC64;
     MVGVNSLRSA LYLIVLILFV QLTYFSDARV MDVDLSRAFL PLTGIGCGES CVWIPCVSAA
     IGCSCSNKIC YRNGIIPKK