ID   CYCK_PETHY              Reviewed;          74 AA.
AC   B3EWH6;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Acyclotide phyb-K {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=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   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 44-74, TISSUE SPECIFICITY, DOMAIN, DISULFIDE BONDS, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Root {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}.
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: Contains 3 disulfide bonds. {ECO:0000269|PubMed:22700981}.
CC   -!- MASS SPECTROMETRY: Mass=3251.46; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22700981};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255}.
CC   -!- CAUTION: This peptide is linear but closely related to cyclotides.
CC       Since in UniProtKB the primary structure is preferred to classify
CC       proteins, the sequence is assigned to the cyclotide family.
CC       {ECO:0000305}.
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DR   EMBL; FN001318; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWH6; -.
DR   SMR; B3EWH6; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR036146; Cyclotide_sf.
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:0000255"
FT   PROPEP          25..43
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:22700981"
FT                   /id="PRO_0000419339"
FT   PEPTIDE         44..74
FT                   /note="Acyclotide phyb-K"
FT                   /evidence="ECO:0000269|PubMed:22700981"
FT                   /id="PRO_0000419340"
FT   DISULFID        47..64
FT                   /evidence="ECO:0000250|UniProtKB:P56254"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250|UniProtKB:P56254"
FT   DISULFID        56..71
FT                   /evidence="ECO:0000250|UniProtKB:P56254"
SQ   SEQUENCE   74 AA;  8113 MW;  F17E43791B0B0BEC CRC64;
     MARVNSLKCA LCFIVLILFV QLNCIPETRV MAVELSRVFL QTSSTDCGEP CVYIPCTITA
     LLGCSCLNKV CVRP