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 14-DEC-2022, entry version 15. 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}. 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; 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; Cyclotides; 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 //